|
Name |
Accession |
Description |
Interval |
E-value |
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-1273 |
2.17e-178 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 566.97 E-value: 2.17e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 18 EGDFELgisskqkRKKTKTVKmIGVLTLFRYSDWQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTdKFVDTAGNFSfPVN 97
Cdd:PTZ00265 31 KGTFEL-------YKKIKTQK-IPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFGVIM-KNMNLGENVN-DII 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 98 FSLSLLnpgkileeemtryayyysglGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRL 177
Cdd:PTZ00265 101 FSLVLI--------------------GIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 178 TDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAE 257
Cdd:PTZ00265 161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 258 EALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVIS--------KEYT 329
Cdd:PTZ00265 241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 330 IGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSfSERGHKPDSIKgNLEFNDVHFSYPSRANV 409
Cdd:PTZ00265 321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINI-DGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAE 488
Cdd:PTZ00265 399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKN 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 489 NI-------------------------------------CYGRGNVTM-----DEIKKAVKEANA--------------- 511
Cdd:PTZ00265 479 NIkyslyslkdlealsnyynedgndsqenknkrnscrakCAGDLNDMSnttdsNELIEMRKNYQTikdsevvdvskkvli 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 512 YEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAH 589
Cdd:PTZ00265 559 HDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAH 638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 590 RLSTVRNADVI-----------------------------------------------AGFEDGVIVEQGSHSELMK-KE 621
Cdd:PTZ00265 639 RLSTIRYANTIfvlsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKnKN 718
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 622 GVYFKLVNMQTSGSQIQSEefelNDEKAATRMapngwKSRLFRHSTQ---------------KNLKNSQMCQKSlDVETD 686
Cdd:PTZ00265 719 GIYYTMINNQKVSSKKSSN----NDNDKDSDM-----KSSAYKDSERgydpdemngnskhenESASNKKSCKMS-DENAS 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 687 GLEANvPPVSFLKVLKLNKTEWPY---------------FVVGTVCAIANGGLQPAFSVIFSEIIA-IFgpgDDAVKQQK 750
Cdd:PTZ00265 789 ENNAG-GKLPFLRNLFKRKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVStLF---DFANLEAN 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 751 CNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGT 830
Cdd:PTZ00265 865 SNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVN 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 831 RLALIAQNIANLGTGIIISFIYgwqltllllavVPIIA--VSGI--VEMKL------LAGNAKRDKKELEAAGKI----- 895
Cdd:PTZ00265 945 NIVIFTHFIVLFLVSMVMSFYF-----------CPIVAavLTGTyfIFMRVfairarLTANKDVEKKEINQPGTVfayns 1013
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 896 -----------ATEAIENIRTVVSLTQERKFESMyVEKLYGpYRNSVQKAH--IYGITFSISQAFMYFSYAGCFRFGAYL 962
Cdd:PTZ00265 1014 ddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNL-IEKAID-YSNKGQKRKtlVNSMLWGFSQSAQLFINSFAYWFGSFL 1091
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 963 IVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGLK---PDKFEGNITFNEV 1039
Cdd:PTZ00265 1092 IRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDV 1171
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1040 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-------------------------------- 1087
Cdd:PTZ00265 1172 NFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvg 1251
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1088 ---------------PLAGTVFVDFGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIV 1152
Cdd:PTZ00265 1252 mknvnefsltkeggsGEDSTVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVK 1329
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1153 SAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL----DKAr 1228
Cdd:PTZ00265 1330 RACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA- 1408
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1229 eGRTCIVIAHRLSTIQNADLIVVFQN-----GRVKEHGTHQQLL-AQKGIY 1273
Cdd:PTZ00265 1409 -DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVY 1458
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
45-635 |
1.30e-177 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 537.06 E-value: 1.30e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 45 LFRYSdWQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTDKFVdTAGNFSFpvnfslsllnpgkileeeMTRYAYYYSGLG 124
Cdd:COG1132 12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-AGGDLSA------------------LLLLLLLLLGLA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 125 AGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFA 204
Cdd:COG1132 72 LLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 205 GFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLE 284
Cdd:COG1132 152 ALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 285 NAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAA 364
Cdd:COG1132 232 ELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 365 YVIFDIIDNNPKIDSfSERGHKPDSIKGNLEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQR 444
Cdd:COG1132 312 ERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 445 LYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDT 524
Cdd:COG1132 389 FYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 525 LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFE 604
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
570 580 590
....*....|....*....|....*....|.
gi 9961250 605 DGVIVEQGSHSELMKKEGVYFKLVNMQTSGS 635
Cdd:COG1132 549 DGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
696-1284 |
3.71e-168 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 512.40 E-value: 3.71e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 696 SFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDdavkQQKCNIFSLIFLFLGIISFFTFFLQGF 774
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGD----LSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 775 TFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGW 854
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 855 QLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKA 934
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 935 HIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQ 1014
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1015 PLIDSySEEGLKPDKFEGNITFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVf 1094
Cdd:COG1132 322 PEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1095 vdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETR 1174
Cdd:COG1132 398 ------LIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTV 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1175 VGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQN 1254
Cdd:COG1132 470 VGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDD 549
|
570 580 590
....*....|....*....|....*....|
gi 9961250 1255 GRVKEHGTHQQLLAQKGIYFSMVSVQAGTQ 1284
Cdd:COG1132 550 GRIVEQGTHEELLARGGLYARLYRLQFGEE 579
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
395-631 |
9.06e-153 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 458.54 E-value: 9.06e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 475 VSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 555 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1034-1280 |
6.54e-149 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 448.53 E-value: 6.54e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQ 1113
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI-------LLDGVDIRDLNLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFDCSIAENIAYGDNSRvvSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIA 1193
Cdd:cd03249 74 WLRSQIGLVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIY 1273
Cdd:cd03249 152 RALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVY 231
|
....*..
gi 9961250 1274 FSMVSVQ 1280
Cdd:cd03249 232 AKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
123-632 |
6.87e-141 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 445.43 E-value: 6.87e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 123 LGAGVLVAAYIQV------SFWTLAAGRQI-RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDdISKISEGIGDKVGMF 195
Cdd:COG2274 198 LAIGLLLALLFEGllrllrSYLLLRLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 196 FQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 275
Cdd:COG2274 277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 276 LERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF--SVGQAAPC 353
Cdd:COG2274 357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLG--QLIAFNILSGRFlaPVAQLIGL 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 354 IDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDsIKGNLEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGC 433
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSGS 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 434 GKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYE 513
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 514 FIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 593
Cdd:COG2274 593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
|
490 500 510
....*....|....*....|....*....|....*....
gi 9961250 594 VRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQT 632
Cdd:COG2274 673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
701-1017 |
1.20e-139 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 427.25 E-value: 1.20e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 701 LKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAG 780
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 781 EILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLL 860
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 861 LAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGIT 940
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 941 FSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLI 1017
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-367 |
2.96e-137 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 420.91 E-value: 2.96e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 57 MSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFSL-SLLNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQV 135
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITGNSSGLnSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 136 SFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWK 215
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 216 LTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAI 295
Cdd:cd18558 161 LTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 296 SANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 367
Cdd:cd18558 241 TFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
42-628 |
6.25e-135 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 429.53 E-value: 6.25e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 42 VLTLFRYSDWQDKLFMSLGTIMAIahgSGLPLMMIVF--GEMTDKFVDTAGNFSFPVN-FSLSLLNPGkileeemtryay 118
Cdd:TIGR00958 149 LFRLLGLSGRDWPWLISAFVFLTL---SSLGEMFIPFytGRVIDTLGGDKGPPALASAiFFMCLLSIA------------ 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 119 yySGLGAGVLVAAYiqvsfwTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQA 198
Cdd:TIGR00958 214 --SSVSAGLRGGSF------NYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRN 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 199 VATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELER 278
Cdd:TIGR00958 286 LVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASR 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 279 YQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQAAPCIDAFA 358
Cdd:TIGR00958 366 FKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGN----LVSFLLYQEQLGEAVRVLSYVY 441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 359 N----ARGAAYVIFDIIDNNPKIDSfsERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCG 434
Cdd:TIGR00958 442 SgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSG 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 435 KSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEF 514
Cdd:TIGR00958 520 KSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDF 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 515 IMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAalDKAREGRTTIVIAHRLSTV 594
Cdd:TIGR00958 600 IMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTV 677
|
570 580 590
....*....|....*....|....*....|....
gi 9961250 595 RNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLV 628
Cdd:TIGR00958 678 ERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
689-1281 |
1.17e-129 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 415.39 E-value: 1.17e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 689 EANVPPVSFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIaifgpgDDAVKQQkcNIFSLIFLFLGIISFFT 768
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVI------DRVLPNQ--DLSTLWVLAIGLLLALL 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 769 F-----FLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLaTDAAQVQGATGTRLALIAQNIANLG 843
Cdd:COG2274 208 FegllrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 844 TGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAgnaKRDKKELEAAGKIAT---EAIENIRTVVSLTQERKFESMYv 920
Cdd:COG2274 285 IFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLR---RLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRW- 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 921 EKLYGPYRNSVQKAHIYGITFS-ISQAFMYFSYAGCFRFGAYLIVNGHMRFrDVILVFSAIVFGAVA-LGHASSFAPDYA 998
Cdd:COG2274 361 ENLLAKYLNARFKLRRLSNLLStLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQLIGLLQRFQ 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 999 KAKLSAAHLFMLFERQPLIDSySEEGLKPDKFEGNITFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTV 1078
Cdd:COG2274 440 DAKIALERLDDILDLPPEREE-GRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1079 VQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAA 1158
Cdd:COG2274 518 LKLLLGLYEPTSGRI-------LIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAARLA 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1159 NIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1238
Cdd:COG2274 589 GLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH 668
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 9961250 1239 RLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQA 1281
Cdd:COG2274 669 RLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
111-631 |
1.88e-125 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 399.84 E-value: 1.88e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 111 EEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGD 190
Cdd:TIGR02204 55 GLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGS 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:TIGR02204 135 SLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIGAfSVGQ 349
Cdd:TIGR02204 215 HEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTlGQFVFYAVMVAG-SIGT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 350 AAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVG 429
Cdd:TIGR02204 294 LSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 430 SSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEA 509
Cdd:TIGR02204 374 PSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAA 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 510 NAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAH 589
Cdd:TIGR02204 454 HAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAH 533
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 9961250 590 RLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:TIGR02204 534 RLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
57-367 |
6.13e-119 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 371.81 E-value: 6.13e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 57 MSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFslsllnpgkilEEEMTRYAYYYSGLGAGVLVAAYIQVS 136
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEF-----------LDDVNKYALYFVYLGIGSFVLSYIQTA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 137 FWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKL 216
Cdd:cd18577 70 CWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 217 TLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAIS 296
Cdd:cd18577 150 TLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 297 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVI 367
Cdd:cd18577 230 SGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
684-1277 |
2.04e-117 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 382.53 E-value: 2.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 684 ETDGLEANVPPVSFlKVLKLNKTEWPYFVVGTV---CAIANGGLQPAFSvifSEIIAIFGpGDDAVKQQKCNIFSLIFLF 760
Cdd:TIGR00958 137 EAEQGQSETADLLF-RLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYT---GRVIDTLG-GDKGPPALASAIFFMCLLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 761 LGiiSFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNIA 840
Cdd:TIGR00958 212 IA--SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLNVNVLLRNLV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 841 NLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYV 920
Cdd:TIGR00958 288 MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 921 EKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRfRDVILVFsaiVFGAVALGHA----SSFAPD 996
Cdd:TIGR00958 368 EALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVS-SGNLVSF---LLYQEQLGEAvrvlSYVYSG 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 997 YAKAKLSAAHLFMLFERQPLIDSysEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKS 1076
Cdd:TIGR00958 444 MMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1077 TVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAK 1156
Cdd:TIGR00958 522 TVAALLQNLYQPTGGQV-------LLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAK 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1157 AANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEalDKAREGRTCIVI 1236
Cdd:TIGR00958 593 AANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLI 670
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 9961250 1237 AHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMV 1277
Cdd:TIGR00958 671 AHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
129-631 |
9.95e-114 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 367.89 E-value: 9.95e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 129 VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIV 208
Cdd:TIGR02203 69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 209 GFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKE 288
Cdd:TIGR02203 149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 289 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNaMTVFFSiligafSVGQAAPCIDAFANARG------ 362
Cdd:TIGR02203 229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT------AMIALIRPLKSLTNVNApmqrgl 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 363 -AAYVIFDIIDNNPKIDsfsERGHKPDSIKGNLEFNDVHFSYPSRaNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQL 441
Cdd:TIGR02203 302 aAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 442 IQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGR-GNVTMDEIKKAVKEANAYEFIMKLPQ 520
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 521 KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVI 600
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
490 500 510
....*....|....*....|....*....|.
gi 9961250 601 AGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
265-636 |
3.32e-112 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 364.91 E-value: 3.32e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 265 TVIAFGGQNKELERYQKHLENAKEIGIKKAISAN---------ISMGIAFLLIYASYAlafwygstlVISKEYTIGNamt 335
Cdd:COG5265 230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaliIALGLTAMMLMAAQG---------VVAGTMTVGD--- 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 336 vfFsILIGAFSVGQAAPCidafaNARGAAY-----------VIFDIIDNNPKIDSfserghKPDSI-----KGNLEFNDV 399
Cdd:COG5265 298 --F-VLVNAYLIQLYIPL-----NFLGFVYreirqaladmeRMFDLLDQPPEVAD------APDAPplvvgGGEVRFENV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 400 HFSY-PSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQE 478
Cdd:COG5265 364 SFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 479 PVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:COG5265 441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 559 ATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQTSGSQ 636
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEE 598
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
394-627 |
1.05e-111 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 349.61 E-value: 1.05e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKL 627
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
752-1280 |
5.36e-111 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 360.94 E-value: 5.36e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIF---LFLGIISFFTFFLqgftFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGAT 828
Cdd:TIGR02204 59 RYFAFLLvvaLVLALGTAARFYL----VTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 829 GTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVS 908
Cdd:TIGR02204 133 GSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 909 LTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDV-ILVFSAiVFGAVAL 987
Cdd:TIGR02204 213 FGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgQFVFYA-VMVAGSI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 988 GHASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLAL 1067
Cdd:TIGR02204 292 GTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVAL 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1068 VGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGdnsRV-V 1146
Cdd:TIGR02204 372 VGPSGAGKSTLFQLLLRFYDPQSGRI-------LLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG---RPdA 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1147 SQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK 1226
Cdd:TIGR02204 442 TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALET 521
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1227 AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1280
Cdd:TIGR02204 522 LMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
142-631 |
1.17e-108 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 354.71 E-value: 1.17e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 142 AGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDD------------ISKISEGigdkvgmffqavATFFAGFIVG 209
Cdd:PRK11176 93 SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREG------------ASIIGLFIMM 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 210 FIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEI 289
Cdd:PRK11176 161 FYYSWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQ 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 290 GIKKAISANISMGIAFLLiyASYALAF--WYGSTLVISKEYTIGnAMTVFFSILIGAFSVGQAAPCIDA-FANARGAAYV 366
Cdd:PRK11176 241 GMKMVSASSISDPIIQLI--ASLALAFvlYAASFPSVMDTLTAG-TITVVFSSMIALMRPLKSLTNVNAqFQRGMAACQT 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 367 IFDIIDNNPKIDsfsERGHKPDSIKGNLEFNDVHFSYPSRaNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLY 446
Cdd:PRK11176 318 LFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 447 DPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNV-TMDEIKKAVKEANAYEFIMKLPQKFDTL 525
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 526 VGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFED 605
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
490 500
....*....|....*....|....*.
gi 9961250 606 GVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
394-631 |
5.85e-108 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 339.59 E-value: 5.85e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
711-1007 |
7.87e-107 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 339.64 E-value: 7.87e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVK-----------------QQKCNIFSLIFLFLGIISFFTFFLQG 773
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNItgnssglnssagpfeklEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 774 FTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYG 853
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 854 WQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQK 933
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 934 AHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMR-FRDVILVFSAIVFGAVALGHASSFAPdYAKAKLSAAHL 1007
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1034-1273 |
8.69e-103 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 325.34 E-value: 8.69e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQ 1113
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID-------GHDVRDYTLA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIA 1193
Cdd:cd03251 73 SLRRQIGLVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIY 1273
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1006-1281 |
2.20e-101 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 335.64 E-value: 2.20e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1006 HLFMLFERQPLI-DSYSEEGLKPDkfEGNITFNEVVFNY-PTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE 1083
Cdd:COG5265 331 RMFDLLDQPPEVaDAPDAPPLVVG--GGEVRFENVSFGYdPER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1084 RFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPF 1163
Cdd:COG5265 406 RFYDVTSGRI-------LIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDF 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1164 IETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTI 1243
Cdd:COG5265 477 IESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTI 556
|
250 260 270
....*....|....*....|....*....|....*...
gi 9961250 1244 QNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQA 1281
Cdd:COG5265 557 VDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
696-1283 |
1.20e-100 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 332.45 E-value: 1.20e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 696 SFLKVLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGF 774
Cdd:TIGR02203 1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 775 TFGKageiLTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG-ATGTRLALIAQNIANLGTgIIISFIYG 853
Cdd:TIGR02203 81 VSNK----VVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASaATDAFIVLVRETLTVIGL-FIVLLYYS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 854 WQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQE----RKFESMYVEKLygpyRN 929
Cdd:TIGR02203 154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQayetRRFDAVSNRNR----RL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 930 SVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFM 1009
Cdd:TIGR02203 230 AMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1010 LFERQPLIDsysEEGLKPDKFEGNITFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPL 1089
Cdd:TIGR02203 310 LLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1090 AGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQdEIVSAAKAANIHPFIETLPH 1169
Cdd:TIGR02203 386 SGQI-------LLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADRA-EIERALAAAYAQDFVDKLPL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1170 KYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1249
Cdd:TIGR02203 458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
|
570 580 590
....*....|....*....|....*....|....
gi 9961250 1250 VVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGT 1283
Cdd:TIGR02203 538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQFRE 571
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1034-1280 |
1.50e-98 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 314.17 E-value: 1.50e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQ 1113
Cdd:cd03253 1 IEFENVTFAYDP--GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSI-------LIDGQDIREVTLD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIA 1193
Cdd:cd03253 72 SLRRAIGVVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIY 1273
Cdd:cd03253 150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLY 229
|
....*..
gi 9961250 1274 FSMVSVQ 1280
Cdd:cd03253 230 AEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
392-622 |
1.90e-98 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 313.39 E-value: 1.90e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYpsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEG 622
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
358-622 |
5.06e-95 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 316.70 E-value: 5.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 358 ANARGAAYVIFDIIDNNPKIdsfSERGHKPDSIKGN--LEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGK 435
Cdd:COG4988 302 ANGIAAAEKIFALLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGK 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 436 STTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFI 515
Cdd:COG4988 377 STLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFV 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 516 MKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVR 595
Cdd:COG4988 457 AALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA 536
|
250 260
....*....|....*....|....*..
gi 9961250 596 NADVIAGFEDGVIVEQGSHSELMKKEG 622
Cdd:COG4988 537 QADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1032-1271 |
5.55e-94 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 301.07 E-value: 5.55e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1032 GNITFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLN 1111
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI-------LIDGIDIRDIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 VQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIA 1191
Cdd:cd03254 72 RKSLRSMIGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1192 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1271
Cdd:cd03254 150 IARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
295-657 |
9.77e-94 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 313.82 E-value: 9.77e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 295 ISANISMGIAFLLiyasyalafwyGSTLVISKEYTIGN--AMTVFFSILIG------AF--SVGQAAPCIDAFanargaa 364
Cdd:PRK13657 248 AASTITMLAILVL-----------GAALVQKGQLRVGEvvAFVGFATLLIGrldqvvAFinQVFMAAPKLEEF------- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 365 yviFDIIDNNPKIDsfsERGHKPD--SIKGNLEFNDVHFSYPSRAnvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI 442
Cdd:PRK13657 310 ---FEVEDAVPDVR---DPPGAIDlgRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 443 QRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKF 522
Cdd:PRK13657 382 QRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 523 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAG 602
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 603 FEDGVIVEQGSHSELMKKEGVYFKLVNMQtsgsqiqseeFELNDEKAATRMAPNG 657
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAALLRAQ----------GMLQEDERRKQPAAEG 586
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
138-627 |
3.46e-91 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 305.92 E-value: 3.46e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 138 WTLaagRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDIskisegigDKVGMFF-QAVATFFAGFIVGFIrgwkL 216
Cdd:COG4987 82 ATL---RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----A 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 217 TLVIMAISPILGLS-------AAVWAKILSAFSDKELAAYAKAG-----AVAEEALGAIRTVIAFGGQNKELERYQKHLE 284
Cdd:COG4987 147 VAFLAFFSPALALVlalglllAGLLLPLLAARLGRRAGRRLAAAraalrARLTDLLQGAAELAAYGALDRALARLDAAEA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 285 NAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVgqAAPCIDAFAN---AR 361
Cdd:COG4987 227 RLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFEA--LAPLPAAAQHlgrVR 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 362 GAAYVIFDIIDNNPKIDSFSERGHKPDSikGNLEFNDVHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQL 441
Cdd:COG4987 304 AAARRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 442 IQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQK 521
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 522 FDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIA 601
Cdd:COG4987 461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
|
490 500
....*....|....*....|....*.
gi 9961250 602 GFEDGVIVEQGSHSELMKKEGVYFKL 627
Cdd:COG4987 541 VLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
753-1282 |
6.02e-89 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 300.40 E-value: 6.02e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 753 IFSLIFLfLGIISFFTFFLQGFTFGKAGEILTRRLrsmaFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 832
Cdd:PRK11176 71 VIGLMIL-RGITSFISSYCISWVSGKVVMTMRRRL----FGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGAL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 833 ALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVS-GIVemkllagnAKR----DKKELEAAGKIATEAIENIR--T 905
Cdd:PRK11176 144 ITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVV--------SKRfrniSKNMQNTMGQVTTSAEQMLKghK 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 906 VVSLTQERKFESMYVEKLYGPYRNS----VQKAHIYG--ITFSISQAFMYFSYAGCFRFGAYLIVNGhmrfrDVILVFSA 979
Cdd:PRK11176 216 EVLIFGGQEVETKRFDKVSNRMRQQgmkmVSASSISDpiIQLIASLALAFVLYAASFPSVMDTLTAG-----TITVVFSS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 980 IVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLIDsyseEG-LKPDKFEGNITFNEVVFNYPTRaNVPVLQGLSLE 1058
Cdd:PRK11176 291 MIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEKD----EGkRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFK 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1059 VKKGQTLALVGSSGCGKSTVVQLLERFYDplagtvfVDFGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIA 1138
Cdd:PRK11176 366 IPAGKTVALVGRSGSGKSTIANLLTRFYD-------IDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIA 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1139 YGDNSRVvSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEK 1218
Cdd:PRK11176 439 YARTEQY-SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESER 517
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1219 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAG 1282
Cdd:PRK11176 518 AIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
700-1271 |
9.56e-87 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 293.59 E-value: 9.56e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 700 VLKLNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIA--IFGPGDDAvkqqkcNIFSLIFLFLGII---SFFTFFLQGF 774
Cdd:COG4988 8 LKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPLS------ALLPLLGLLLAVLllrALLAWLRERA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 775 TFgKAGEILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTrLATDaaQVQGATG------TRLALIAqnIANLGTGIII 848
Cdd:COG4988 82 AF-RAAARVKRRLRRRLLEKLLALGPAWLRGK--STGELAT-LLTE--GVEALDGyfarylPQLFLAA--LVPLLILVAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 849 SFIYgWQLTLLLLAVVPIIAVSGIVEMKllaGNAKRDKKELEAAGKIATEAIENIRTVVSLtqerkfesmyveKLYGpyR 928
Cdd:COG4988 154 FPLD-WLSGLILLVTAPLIPLFMILVGK---GAAKASRRQWRALARLSGHFLDRLRGLTTL------------KLFG--R 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 929 NSVQKAHIYGITFSISQA-----------------FMYFSYAG-----CFRFgayliVNGHMRFRD--VILVFSAIVFGA 984
Cdd:COG4988 216 AKAEAERIAEASEDFRKRtmkvlrvaflssavlefFASLSIALvavyiGFRL-----LGGSLTLFAalFVLLLAPEFFLP 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 985 V-ALG---HASsfapdyAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKfEGNITFNEVVFNYPTRAnvPVLQGLSLEVK 1060
Cdd:COG4988 291 LrDLGsfyHAR------ANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1061 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYG 1140
Cdd:COG4988 362 PGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI-------LINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLG 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1141 DnsRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVV 1220
Cdd:COG4988 435 R--PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEI 512
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1221 QEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1271
Cdd:COG4988 513 LQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
199-632 |
9.89e-86 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 294.73 E-value: 9.89e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 199 VATFFAgfiVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELER 278
Cdd:TIGR01846 266 VVVFLA---VMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 279 YQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAFS--VGQAAPCIDA 356
Cdd:TIGR01846 343 WDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQ--LVAFNMLAGRVTqpVLRLAQLWQD 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 357 FANARGAAYVIFDIIdNNPKIDSFSERGHKPDsIKGNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKS 436
Cdd:TIGR01846 421 FQQTGIALERLGDIL-NSPTEPRSAGLAALPE-LRGAITFENIRFRYAPDSPE-VLSNLNLDIKPGEFIGIVGPSGSGKS 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 437 TTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIM 516
Cdd:TIGR01846 498 TLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFIS 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 517 KLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN 596
Cdd:TIGR01846 578 ELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRA 657
|
410 420 430
....*....|....*....|....*....|....*.
gi 9961250 597 ADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQT 632
Cdd:TIGR01846 658 CDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQS 693
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1025-1257 |
3.98e-85 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 276.66 E-value: 3.98e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1025 LKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDG 1104
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV-------LLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1105 QEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSG 1184
Cdd:cd03248 76 KPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1185 GQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1257
Cdd:cd03248 154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
394-631 |
1.96e-84 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 275.13 E-value: 1.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03252 1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
394-606 |
2.93e-83 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 269.25 E-value: 2.93e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAENIcygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03228 80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961250 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 606
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
387-608 |
4.12e-83 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 270.88 E-value: 4.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 387 PDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN 466
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 467 YLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVI 608
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
711-1007 |
1.18e-80 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 267.03 E-value: 1.18e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIF-----GPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTR 785
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 786 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVP 865
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 866 IIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQ 945
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 946 AFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHL 1007
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
783-1278 |
1.33e-80 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 276.26 E-value: 1.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 783 LTRRLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATgtrLALIAQNIANLGTGIIISFIYGWQLTLLLLA 862
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 863 VVPIIAVSGIVeMKLLAG--NAKRDKKELEAAGKIATEAIENIRTVVSLT----QERKFESMY-VEKLYGpyRNSVQKAH 935
Cdd:COG4987 161 LALGLLLAGLL-LPLLAArlGRRAGRRLAAARAALRARLTDLLQGAAELAaygaLDRALARLDaAEARLA--AAQRRLAR 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 936 IYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDV-ILVFSAI-VFGAVA-LGHASSFAPDYAKAklsAAHLFMLFE 1012
Cdd:COG4987 238 LSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLaLLVLAALaLFEALApLPAAAQHLGRVRAA---ARRLNELLD 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1013 RQPLIDSYSEEGLKPDkfEGNITFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGT 1092
Cdd:COG4987 315 APPAVTEPAEPAPAPG--GPSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGS 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1093 VfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYE 1172
Cdd:COG4987 392 I-------TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLD 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1173 TRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVF 1252
Cdd:COG4987 463 TWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVL 542
|
490 500
....*....|....*....|....*.
gi 9961250 1253 QNGRVKEHGTHQQLLAQKGIYFSMVS 1278
Cdd:COG4987 543 EDGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1034-1280 |
4.56e-78 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 257.41 E-value: 4.56e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNV 1112
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-------LVDGHDLALADP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAI 1192
Cdd:cd03252 72 AWLRRQVGVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1193 ARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGI 1272
Cdd:cd03252 150 ARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGL 229
|
....*...
gi 9961250 1273 YFSMVSVQ 1280
Cdd:cd03252 230 YAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
956-1271 |
6.87e-78 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 269.14 E-value: 6.87e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 956 FRFGAYLIVNGHMRFRDVI--LVFSAIVFGAvaLGHASSFApdyAKAKLSAAHLFMLFErqpLIDSYSEEGLKPD----- 1028
Cdd:PRK13657 258 LVLGAALVQKGQLRVGEVVafVGFATLLIGR--LDQVVAFI---NQVFMAAPKLEEFFE---VEDAVPDVRDPPGaidlg 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1029 KFEGNITFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAK 1108
Cdd:PRK13657 330 RVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI-------LIDGTDIR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1109 KLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQ 1188
Cdd:PRK13657 401 TVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQ 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1189 RIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:PRK13657 479 RLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA 558
|
...
gi 9961250 1269 QKG 1271
Cdd:PRK13657 559 RGG 561
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
709-1273 |
1.92e-77 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 271.43 E-value: 1.92e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 709 PYFVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDdavkqqkcnifSLIFLFLGIIsfFTFFLQGFTFGKAGeILTRRLR 788
Cdd:TIGR03796 157 LYLLLAGLLLVLPGLVIPAFSQIFVDEILVQGRQD-----------WLRPLLLGMG--LTALLQGVLTWLQL-YYLRRLE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 789 ---SMAFKA-----MLRQDMSWFDdhKNSTGALSTRLATdAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLL 860
Cdd:TIGR03796 223 iklAVGMSArflwhILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIG 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 861 LAVVPIIAVSGIVEMKLLAGNAKRDKKEleaAGKIATEAIENIRTVVSLtQERKFESMYVEKLYGPYR---NSVQKAHIY 937
Cdd:TIGR03796 300 IAFAAINVLALQLVSRRRVDANRRLQQD---AGKLTGVAISGLQSIETL-KASGLESDFFSRWAGYQAkllNAQQELGVL 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 938 GITFS-ISQAFMYFSYAGCFRFGAYLIVNGHMR------FRDVILVFSAIVFGAVALGHA-SSFAPDYAKAK--LSAAhL 1007
Cdd:TIGR03796 376 TQILGvLPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTlQELEGDLNRLDdvLRNP-V 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1008 FMLFERQPLIDSYSEEglkPDKFEGNITFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD 1087
Cdd:TIGR03796 455 DPLLEEPEGSAATSEP---PRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQ 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1088 PLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKAANIHPFIETL 1167
Cdd:TIGR03796 531 PWSGEI-------LFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSR 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1168 PHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALdkAREGRTCIVIAHRLSTIQNAD 1247
Cdd:TIGR03796 602 PGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCD 679
|
570 580
....*....|....*....|....*.
gi 9961250 1248 LIVVFQNGRVKEHGTHQQLLAQKGIY 1273
Cdd:TIGR03796 680 EIIVLERGKVVQRGTHEELWAVGGAY 705
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1034-1256 |
8.56e-77 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 250.76 E-value: 8.56e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQ 1113
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI-------LIDGVDLRDLDLE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFDCSIAENIaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtqLSGGQKQRIAIA 1193
Cdd:cd03228 73 SLRKNIAYVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGR 1256
Cdd:cd03228 109 RALLRDPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
51-377 |
3.15e-75 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 252.37 E-value: 3.15e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 51 WQDKLFMSLGTIMAIAHGSGLPLMMIVFGEMTDkfvdtagnfsfpvnfSLSLLNPGKILEEeMTRYAYYYSGLGAGVLVA 130
Cdd:cd18578 5 KPEWPLLLLGLIGAIIAGAVFPVFAILFSKLIS---------------VFSLPDDDELRSE-ANFWALMFLVLAIVAGIA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 131 AYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFD--INDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIV 208
Cdd:cd18578 69 YFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLII 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 209 GFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKE 288
Cdd:cd18578 149 AFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 289 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIF 368
Cdd:cd18578 229 KGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIF 308
|
....*....
gi 9961250 369 DIIDNNPKI 377
Cdd:cd18578 309 RLLDRKPEI 317
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
57-345 |
3.41e-75 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 250.64 E-value: 3.41e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 57 MSLGTIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFslsllnpgkileeemtrYAYYYSGLGAGVLVAAYIQVS 136
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNV-----------------YSLALLLLGLAQFILSFLQSY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 137 FWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKL 216
Cdd:pfam00664 64 LLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 217 TLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAIS 296
Cdd:pfam00664 144 TLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 9961250 297 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 345
Cdd:pfam00664 224 NGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
850-1282 |
3.88e-73 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 258.52 E-value: 3.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 850 FIYGWQLTLLLLAVVPI-----IAVSGIVEMKLlagnakRDKKELEAAGK-IATEAIENIRTVVSLTQERKFESMYVEKL 923
Cdd:TIGR01846 274 FFYSPTLTGVVIGSLVCyallsVFVGPILRKRV------EDKFERSAAATsFLVESVTGIETIKATATEPQFQNRWDRQL 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 924 YGpYRNSVQKAHIYGITFS-ISQAFMYFSYAGCFRFGAYLIVNGHMRfrdvilVFSAIVFGAVAlGHASSFAPDYAKAKL 1002
Cdd:TIGR01846 348 AA-YVAASFRVTNLGNIAGqAIELIQKLTFAILLWFGAHLVIGGALS------PGQLVAFNMLA-GRVTQPVLRLAQLWQ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1003 SAAHLFMLFERQPLI-----DSYSEEGLKPDKFEGNITFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKST 1077
Cdd:TIGR01846 420 DFQQTGIALERLGDIlnsptEPRSAGLAALPELRGAITFENIRFRYAPDS-PEVLSNLNLDIKPGEFIGIVGPSGSGKST 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1078 VVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrvVSQDEIVSAAKA 1157
Cdd:TIGR01846 499 LTKLLQRLYTPQHGQV-------LVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG--APFEHVIHAAKL 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1158 ANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA 1237
Cdd:TIGR01846 570 AGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIA 649
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 9961250 1238 HRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAG 1282
Cdd:TIGR01846 650 HRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
795-1280 |
6.15e-72 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 254.88 E-value: 6.15e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 795 MLRQDMSWFDDHknSTGALSTRlatdaaqVQGATGTRLALIAQNIANLGTGI--IIS----FIYGWQLTL----LLLAVV 864
Cdd:TIGR03797 219 LLRLPVSFFRQY--STGDLASR-------AMGISQIRRILSGSTLTTLLSGIfaLLNlglmFYYSWKLALvavaLALVAI 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 865 PIIAVSGIVemkllagNAKRDKKELEAAGKIATEAIENIRTVVSL----TQERKFesMYVEKLYGPYRNSVQKAH-IYGI 939
Cdd:TIGR03797 290 AVTLVLGLL-------QVRKERRLLELSGKISGLTVQLINGISKLrvagAENRAF--ARWAKLFSRQRKLELSAQrIENL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 940 TFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDvILVFSAivfgavALGHASSFAPDYAKAKLSAAHLFMLFER-QPLID 1018
Cdd:TIGR03797 361 LTVFNAVLPVLTSAALFAAAISLLGGAGLSLGS-FLAFNT------AFGSFSGAVTQLSNTLISILAVIPLWERaKPILE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1019 S---YSEEGLKPDKFEGNITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVF 1094
Cdd:TIGR03797 434 AlpeVDEAKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVF 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1095 vdfgfqlLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsrVVSQDEIVSAAKAANIHPFIETLPHKYETR 1174
Cdd:TIGR03797 512 -------YDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTV 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1175 VGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVFQN 1254
Cdd:TIGR03797 582 ISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDA 659
|
490 500
....*....|....*....|....*.
gi 9961250 1255 GRVKEHGTHQQLLAQKGIYFSMVSVQ 1280
Cdd:TIGR03797 660 GRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
295-640 |
2.32e-71 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 250.58 E-value: 2.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 295 ISANISMgIAFLLIyasyalafwyGSTLVISKEYTIGNAMTV--FFSILIGAFSvgQAAPCIDAFANARGAAYVIFDIID 372
Cdd:TIGR01192 248 MASTISM-MCILVI----------GTVLVIKGELSVGEVIAFigFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLED 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 373 NNPKIDSFSERGHKPDsIKGNLEFNDVHFSYPSRAnvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGT 452
Cdd:TIGR01192 315 SVFQREEPADAPELPN-VKGAVEFRHITFEFANSS--QGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQ 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 453 INIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQ 532
Cdd:TIGR01192 392 ILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNR 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 612
Cdd:TIGR01192 472 LSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKG 551
|
330 340
....*....|....*....|....*...
gi 9961250 613 SHSELMKKEGVYFKLvnMQTSGSQIQSE 640
Cdd:TIGR01192 552 SFQELIQKDGRFYKL--LRRSGLLTNQP 577
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
711-985 |
6.03e-71 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 238.70 E-value: 6.03e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQqKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSM 790
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQ-ALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 791 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVS 870
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 871 GIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYF 950
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250 260 270
....*....|....*....|....*....|....*..
gi 9961250 951 SYAGCFRFGAYLIVNGHMRFRDVI--LVFSAIVFGAV 985
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVGDLVafLSLFAQLFGPL 274
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
392-612 |
1.06e-67 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 227.09 E-value: 1.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 612
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
356-600 |
9.75e-67 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 235.26 E-value: 9.75e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 356 AFANARGAAYVIFDIIDNNPKIdsFSERGHKPDSIKGNLEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGK 435
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 436 STTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFI 515
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 516 MKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVR 595
Cdd:TIGR02857 442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521
|
....*
gi 9961250 596 NADVI 600
Cdd:TIGR02857 522 LADRI 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
392-613 |
6.66e-66 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 221.98 E-value: 6.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFSTTIAENICyGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:cd03244 80 ISIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 613
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
123-657 |
2.65e-65 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 232.30 E-value: 2.65e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 123 LGAGVLVAA--YIQVSFWTL----AAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFF 196
Cdd:PRK10789 39 IGTMVLIAVvvYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 197 QAVATFFAGFIVGFIR-GWKLTLVIMAISPILGLSAAVWAKIL--------SAFSdkelaayaKAGAVAEEALGAIRTVI 267
Cdd:PRK10789 119 DSLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLherfklaqAAFS--------SLNDRTQESLTSIRMIK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 268 AFGgqnkeLERYQKHL--ENAKEIGIKKA----ISANISMGIaFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSIL 341
Cdd:PRK10789 191 AFG-----LEDRQSALfaADAEDTGKKNMrvarIDARFDPTI-YIAIGMANLLAIGGGSWMVVNGSLTLG-QLTSFVMYL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 342 igafsvGQAAPCIDAFA---N--ARG-AAYV-IFDIIDNNPKIDSfserGHKP-DSIKGNLEFNDVHFSYPsRANVKILK 413
Cdd:PRK10789 264 ------GLMIWPMLALAwmfNivERGsAAYSrIRAMLAEAPVVKD----GSEPvPEGRGELDVNIRQFTYP-QTDHPALE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 414 GLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYG 493
Cdd:PRK10789 333 NVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 494 RGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQA 573
Cdd:PRK10789 413 RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILH 492
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 574 ALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQtsgsQIqseEFELNDEKAATRM 653
Cdd:PRK10789 493 NLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ----QL---EAALDDAPEIREE 565
|
....
gi 9961250 654 APNG 657
Cdd:PRK10789 566 AVDA 569
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
28-630 |
7.92e-64 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 239.16 E-value: 7.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 28 KQKRKKTKTVKMIgVLTLFRYSdwQDKLFMSLGTIMAiahGSGLPLMMIVFGemtdKFVDTAGNFSFpvnfslsllnpgk 107
Cdd:PTZ00265 804 KRKPKAPNNLRIV-YREIFSYK--KDVTIIALSILVA---GGLYPVFALLYA----KYVSTLFDFAN------------- 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 108 iLEEEMTRYAYYYSGLGAGVLVAAYIQvSFWTLAAGRQIRK-IRQKFFHAILRQEIGWFDINDTTE--LNTRLTDDISKI 184
Cdd:PTZ00265 861 -LEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDQDKHAPglLSAHINRDVHLL 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 185 SEGIGDKVGMFFQAVATFFAGFIVGF----IRGWKLTLV------IMAISPILGLSAAVWAKIL----SAF---SDKELA 247
Cdd:PTZ00265 939 KTGLVNNIVIFTHFIVLFLVSMVMSFyfcpIVAAVLTGTyfifmrVFAIRARLTANKDVEKKEInqpgTVFaynSDDEIF 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 248 AYAKAGAvaEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKE 327
Cdd:PTZ00265 1019 KDPSFLI--QEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGT 1096
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 328 YTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGHK---PDSIKGNLEFNDVHFSYP 404
Cdd:PTZ00265 1097 ILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYI 1176
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD------------------------------------- 447
Cdd:PTZ00265 1177 SRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvn 1256
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 448 -----------------PDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEAN 510
Cdd:PTZ00265 1257 efsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAA 1336
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 511 AYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL----DKAreGRTTIV 586
Cdd:PTZ00265 1337 IDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIIT 1414
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 9961250 587 IAHRLSTVRNADVIAGFED----GVIVE-QGSHSELMK-KEGVYFKLVNM 630
Cdd:PTZ00265 1415 IAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1032-1257 |
1.58e-63 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 215.15 E-value: 1.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1032 GNITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLN 1111
Cdd:cd03245 1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSV-------LLDGTDIRQLD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 VQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIA 1191
Cdd:cd03245 73 PADLRRNIGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1192 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1257
Cdd:cd03245 151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
123-631 |
2.11e-63 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 229.84 E-value: 2.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 123 LGAGVLVAAYIQVSFwTLAAGRQIRKIRQKFFHAI--------LRQEIGWFDINDTTELNTRlTDDISKISEGIGDKvgM 194
Cdd:TIGR03797 178 IALALLAAAVGAAAF-QLAQSLAVLRLETRMDASLqaavwdrlLRLPVSFFRQYSTGDLASR-AMGISQIRRILSGS--T 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 195 FFQAVATFFAGFIVG--FIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 272
Cdd:TIGR03797 254 LTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 273 NKELERYQKHLENAKEIGIKKAISANI-SMGIAFLLIYASYALaFWYGSTLVISKEYTIGNAMTvfFSILIGAFSVGqaa 351
Cdd:TIGR03797 334 NRAFARWAKLFSRQRKLELSAQRIENLlTVFNAVLPVLTSAAL-FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGA--- 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 352 pcIDAFANARGAAYVIF-------DIIDNNPKIDsfsERGHKPDSIKGNLEFNDVHFSYPSRANVkILKGLNLKVQSGQT 424
Cdd:TIGR03797 408 --VTQLSNTLISILAVIplwerakPILEALPEVD---EAKTDPGKLSGAIEVDRVTFRYRPDGPL-ILDDVSLQIEPGEF 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 425 VALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICyGRGNVTMDEIKK 504
Cdd:TIGR03797 482 VAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAPLTLDEAWE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 505 AVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRtt 584
Cdd:TIGR03797 561 AARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR-- 638
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 9961250 585 IVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:TIGR03797 639 IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
752-1269 |
6.18e-63 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 225.40 E-value: 6.18e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIFLFLGIISFFTF-----FLQGFTFGKAGEILTRRLRSMAFKAMLRQDMswfddhkNSTGALSTRLATDAAQVQG 826
Cdd:COG4618 55 SVDTLLMLTLLALGLYAVmglldAVRSRILVRVGARLDRRLGPRVFDAAFRAAL-------RGGGGAAAQALRDLDTLRQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 827 A-TGTrlALIAqnianlgtgiIISFIygWqlTLLLLAVV----P---IIAVSGIVEMKLLA-GNAKRDKKELEAAGKIAT 897
Cdd:COG4618 128 FlTGP--GLFA----------LFDLP--W--APIFLAVLflfhPllgLLALVGALVLVALAlLNERLTRKPLKEANEAAI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 898 EAIE-------NIRTVVSLtqerkfeSMYVE------KLYGPYRNSVQKAHIYGITFS-ISQAFMYFSYAGCFRFGAYLI 963
Cdd:COG4618 192 RANAfaeaalrNAEVIEAM-------GMLPAlrrrwqRANARALALQARASDRAGGFSaLSKFLRLLLQSAVLGLGAYLV 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 964 VNGHMrfrdvilvfSA--IVFGAVALGHAssFAP-DYA--------KAKLSAAHLFMLFERQPLidsySEEGLKPDKFEG 1032
Cdd:COG4618 265 IQGEI---------TPgaMIAASILMGRA--LAPiEQAiggwkqfvSARQAYRRLNELLAAVPA----EPERMPLPRPKG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NITFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKklnv 1112
Cdd:COG4618 330 RLSVENLTVVPP-GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSV-------RLDGADLS---- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWLRAQLG--I--VSQEPILFDCSIAENIA-YGDnsrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQK 1187
Cdd:COG4618 398 QWDREELGrhIgyLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQR 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL 1266
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEV 553
|
...
gi 9961250 1267 LAQ 1269
Cdd:COG4618 554 LAR 556
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
391-620 |
1.98e-60 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 218.08 E-value: 1.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 391 KGNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:COG4618 328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFSTTIAENICygR-GNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:COG4618 407 HIGYLPQDVELFDGTIAENIA--RfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYG 484
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:COG4618 485 DPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
412-1276 |
2.82e-60 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 227.91 E-value: 2.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqdirnfNVNYlreiigvVSQEPVLFSTTIAENIC 491
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------SVAY-------VPQQAWIQNDSLRENIL 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 492 YGRGnvTMDEIKKAVKEANAYEFIMK-LPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 570
Cdd:TIGR00957 721 FGKA--LNEKYYQQVLEACALLPDLEiLPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 571 VqaaLDKA------REGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFK-LVNMQTSGSQIQSEEFE 643
Cdd:TIGR00957 799 I---FEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfLRTYAPDEQQGHLEDSW 875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 644 LNDEKAATRMAPNGWKSRLFRHSTQKNLKNsQMCQKSLDVETDGLEANvpPVSFLKVLKLNKTEWPYF-----VVGTV-- 716
Cdd:TIGR00957 876 TALVSGEGKEAKLIENGMLVTDVVGKQLQR-QLSASSSDSGDQSRHHG--SSAELQKAEAKEETWKLMeadkaQTGQVel 952
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 717 -------CAIangGLQPAFSVIF---SEIIAIFGPG-------DDAV---KQQKCNIFSLIFLFLGIISFFTFFLQGFTF 776
Cdd:TIGR00957 953 svywdymKAI---GLFITFLSIFlfvCNHVSALASNywlslwtDDPMvngTQNNTSLRLSVYGALGILQGFAVFGYSMAV 1029
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 777 GKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIAN-LGTGIIISFIygwq 855
Cdd:TIGR00957 1030 SIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIGALIVILLA---- 1103
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 856 lTLLLLAVVPIIAVSGIVEMKLLAGNAkRDKKELEAAGKIA-----TEAIENIRTVVSLTQERKFEsmyveklygpyrns 930
Cdd:TIGR00957 1104 -TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQERFI-------------- 1167
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 931 vqkaHIYGITFSISQAFMYfsyagcfrfgAYLIVNGHMRFR-----DVILVFSAIvFGAVAlghASSFAPDYAKAKLS-- 1003
Cdd:TIGR00957 1168 ----HQSDLKVDENQKAYY----------PSIVANRWLAVRlecvgNCIVLFAAL-FAVIS---RHSLSAGLVGLSVSys 1229
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1004 ---AAHLFMLFERQPLIDS----------YSE---------EGLKPDKF---EGNITFNEVVFNYPTRANVpVLQGLSLE 1058
Cdd:TIGR00957 1230 lqvTFYLNWLVRMSSEMETnivaverlkeYSEtekeapwqiQETAPPSGwppRGRVEFRNYCLRYREDLDL-VLRHINVT 1308
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1059 VKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIa 1138
Cdd:TIGR00957 1309 IHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI-------IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL- 1380
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1139 ygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEK 1218
Cdd:TIGR00957 1381 --DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDN 1458
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1219 VVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1276
Cdd:TIGR00957 1459 LIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
129-629 |
3.23e-60 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 220.77 E-value: 3.23e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 129 VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDdISKISEGIGDKVGMFFQAVATFFA-GFI 207
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIvGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 208 VGFiRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGqnkELERYQK---HLE 284
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsEFG 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 285 NAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTvfFSILIGAFsvgqaapcIDAFANargaa 364
Cdd:TIGR01193 366 DYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLIT--FNALLSYF--------LTPLEN----- 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 365 yvifdIIDNNPK----------------IDSFSERGHKPDS---IKGNLEFNDVHFSYPSRANvkILKGLNLKVQSGQTV 425
Cdd:TIGR01193 431 -----IINLQPKlqaarvannrlnevylVDSEFINKKKRTElnnLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKT 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 426 ALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYG-RGNVTMDEIKK 504
Cdd:TIGR01193 504 TIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWA 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 505 AVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTT 584
Cdd:TIGR01193 584 ACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTI 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 9961250 585 IVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVN 629
Cdd:TIGR01193 663 IFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
333-627 |
3.72e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 217.39 E-value: 3.72e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 333 AMTVF-----FSILI---GAFS-VGQaapCIdafanarGAAYVIFDIIDNNPKIdSFSERgHKPDSIKGNLEFNDVHFSY 403
Cdd:PRK11160 281 ALFVFaalaaFEALMpvaGAFQhLGQ---VI-------ASARRINEITEQKPEV-TFPTT-STAAADQVSLTLNNVSFTY 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 404 PSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFS 483
Cdd:PRK11160 349 PDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFS 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 484 TTIAENICYGRGNVTmDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 563
Cdd:PRK11160 428 ATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 564 DTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKL 627
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
400-1285 |
3.98e-60 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 227.17 E-value: 3.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 400 HFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLYDPDEGTINIDGQdirnfnvnylreiIGVVSQE 478
Cdd:PLN03232 621 YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS-------------VAYVPQV 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 479 PVLFSTTIAENICYGrGNVTMDEIKKAVkEANAYEFIMKL-PQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:PLN03232 688 SWIFNATVRENILFG-SDFESERYWRAI-DVTALQHDLDLlPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 558 EATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLvnMQTSGSQ 636
Cdd:PLN03232 766 DPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL--MENAGKM 843
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 637 IQSEEFELNDEKAaTRMAPN---GWKSRLFrHSTQKNLKNSQMCQKSLDVETDGLEANVppvsflkVLKLNKTEWPYFVV 713
Cdd:PLN03232 844 DATQEVNTNDENI-LKLGPTvtiDVSERNL-GSTKQGKRGRSVLVKQEERETGIISWNV-------LMRYNKAVGGLWVV 914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 714 GT--VCAIANGGLQPAFSVIFSeiiaiFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMA 791
Cdd:PLN03232 915 MIllVCYLTTEVLRVSSSTWLS-----IWTDQSTPKSYSPGFYIVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAM 989
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 792 FKAMLRQDMSWFddHKNSTGALSTRLATDAAQvqgatgtrlalIAQNIANLGTGIIISFiygWQL--TLLLLAVVPIIAV 869
Cdd:PLN03232 990 LNSILRAPMLFF--HTNPTGRVINRFSKDIGD-----------IDRNVANLMNMFMNQL---WQLlsTFALIGTVSTISL 1053
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 870 SGIVEMKLL-------AGNAKRDKKELEAAGKIATEAI--ENIRTVVSLTQERKFESMyvEKLYGPYRNSVQKAHIYGIT 940
Cdd:PLN03232 1054 WAIMPLLILfyaaylyYQSTSREVRRLDSVTRSPIYAQfgEALNGLSSIRAYKAYDRM--AKINGKSMDNNIRFTLANTS 1131
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 941 F-------SISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVILVFSAIVFGAVALghASSFAPDYAKAKLSAAHLfmlfER 1013
Cdd:PLN03232 1132 SnrwltirLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTL--LSGVLRQASKAENSLNSV----ER 1205
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1014 -QPLIDSYSE-----EGLKPDK---FEGNITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE 1083
Cdd:PLN03232 1206 vGNYIDLPSEataiiENNRPVSgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALF 1283
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1084 RFydplagtVFVDFGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPF 1163
Cdd:PLN03232 1284 RI-------VELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDV 1353
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1164 IETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTI 1243
Cdd:PLN03232 1354 IDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI 1433
|
890 900 910 920
....*....|....*....|....*....|....*....|..
gi 9961250 1244 QNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTQN 1285
Cdd:PLN03232 1434 IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
783-1280 |
4.20e-60 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 217.27 E-value: 4.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 783 LTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR-LALIAQNIANLGTGIIISFIYGWQLTLLLL 861
Cdd:PRK10789 67 LAVELREDFYRQLSRQHPEFYLRHR--TGDLMARATNDVDRVVFAAGEGvLTLVDSLVMGCAVLIVMSTQISWQLTLLAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 862 AVVPIIAVSgivemkllagnAKRDKKELEAAGKIATEAIE--NIRTVVSLTQERKFESMYVEKlygpyRNSVQKAHI--- 936
Cdd:PRK10789 145 LPMPVMAIM-----------IKRYGDQLHERFKLAQAAFSslNDRTQESLTSIRMIKAFGLED-----RQSALFAADaed 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 937 --------------YGITFSISQAFMYFSYAGCfrfGAYLIVNGHMrfrdvilvfsaivfgavALGHASSFA-------- 994
Cdd:PRK10789 209 tgkknmrvaridarFDPTIYIAIGMANLLAIGG---GSWMVVNGSL-----------------TLGQLTSFVmylglmiw 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 995 PDYAKAKL-------SAAH--LFMLFERQPLIDSySEEGLKPDKfeGNITFNEVVFNYPTrANVPVLQGLSLEVKKGQTL 1065
Cdd:PRK10789 269 PMLALAWMfnivergSAAYsrIRAMLAEAPVVKD-GSEPVPEGR--GELDVNIRQFTYPQ-TDHPALENVNFTLKPGQML 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1066 ALVGSSGCGKSTVVQLLERFYDPLAGtvfvDFGFQlldGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSrv 1145
Cdd:PRK10789 345 GICGPTGSGKSTLLSLIQRHFDVSEG----DIRFH---DIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD-- 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1146 VSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD 1225
Cdd:PRK10789 416 ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLR 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1226 KAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1280
Cdd:PRK10789 496 QWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
996-1251 |
1.98e-59 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 214.07 E-value: 1.98e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 996 DYAKAKLSAAHLFMLFERQPLIDSYSEEGLKPDKFEgnITFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGK 1075
Cdd:TIGR02857 286 ARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGK 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1076 STVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDnsRVVSQDEIVSAA 1155
Cdd:TIGR02857 362 STLLNLLLGFVDPTEGSI-------AVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREAL 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1156 KAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIV 1235
Cdd:TIGR02857 433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
|
250
....*....|....*.
gi 9961250 1236 IAHRLSTIQNADLIVV 1251
Cdd:TIGR02857 513 VTHRLALAALADRIVV 528
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
758-1286 |
1.08e-57 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 210.73 E-value: 1.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 758 FLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGTRLALIAQ 837
Cdd:PRK10790 71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 838 NIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKF-E 916
Cdd:PRK10790 149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFgE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 917 SMyveklygpyrNSVQKAHiygitfsisqafmYFSYAGCFRFGAYLIvnghmrfRDVILVFSAIVF------------GA 984
Cdd:PRK10790 229 RM----------GEASRSH-------------YMARMQTLRLDGFLL-------RPLLSLFSALILcgllmlfgfsasGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 985 VALGHASSFApDY------------------AKAKLSAAHLFMLFE--RQPL-IDSYSEEGlkpdkfeGNITFNEVVFNY 1043
Cdd:PRK10790 279 IEVGVLYAFI-SYlgrlneplielttqqsmlQQAVVAGERVFELMDgpRQQYgNDDRPLQS-------GRIDIDNVSFAY 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1044 ptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVS 1123
Cdd:PRK10790 351 --RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEI-------RLDGRPLSSLSHSVLRQGVAMVQ 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 QEPILFDCSIAENIAYGdnsRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQIL 1203
Cdd:PRK10790 422 QDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQIL 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1204 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGT 1283
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAG 578
|
...
gi 9961250 1284 QNL 1286
Cdd:PRK10790 579 EEL 581
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1032-1262 |
2.00e-57 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 197.72 E-value: 2.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1032 GNITFNEVVFNYptRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKL 1110
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSI-------LIDGVDISKI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1111 NVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRI 1190
Cdd:cd03244 72 GLHDLRSRISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1191 AIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1262
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
756-1279 |
4.59e-57 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 211.52 E-value: 4.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 756 LIFLFLGIISFFtfflQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLaTDAAQVQGATG-TRLAL 834
Cdd:TIGR01193 204 IAYIIQQILSYI----QIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRR--TGEIVSRF-TDASSIIDALAsTILSL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 835 IAqniaNLGTGIIISFIYGWQ---LTLLLLAVVPIIAVSGIVEMKLLAgnaKRDKKELEAAGKIATEAIEN---IRTVVS 908
Cdd:TIGR01193 277 FL----DMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVIIILFKRTFN---KLNHDAMQANAVLNSSIIEDlngIETIKS 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 909 LTQE----RKFESMYVEKLYGPYRNS----VQKAHIYGITFSISQAFMYFsyagcfrfGAYLIVNGHMRFRDVIlVFSAI 980
Cdd:TIGR01193 350 LTSEaerySKIDSEFGDYLNKSFKYQkadqGQQAIKAVTKLILNVVILWT--------GAYLVMRGKLTLGQLI-TFNAL 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 981 V-FGAVALGHASSFAPDYAKAKLSAAHLFMLFerqpLIDSYSEEGLKPDKFE---GNITFNEVVFNYPTraNVPVLQGLS 1056
Cdd:TIGR01193 421 LsYFLTPLENIINLQPKLQAARVANNRLNEVY----LVDSEFINKKKRTELNnlnGDIVINDVSYSYGY--GSNILSDIS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1057 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAEN 1136
Cdd:TIGR01193 495 LTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI-------LLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILEN 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1137 IAYGdNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTES 1216
Cdd:TIGR01193 568 LLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTIT 646
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1217 EKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSV 1279
Cdd:TIGR01193 647 EKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
389-1277 |
4.56e-55 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 211.13 E-value: 4.56e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 389 SIKgnlefnDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLYDPDEGTINIDGqdirnfNVNY 467
Cdd:PLN03130 616 SIK------NGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRG------TVAY 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 468 lreiigvVSQEPVLFSTTIAENICYGrGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARAL 547
Cdd:PLN03130 684 -------VPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 548 VRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFK 626
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK 835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 627 LvnMQTSGS--QIQSEEFELNDEKAATRMAPNGWKSRLFRHSTQKNLKNSQmcqKSLDVETDGLEANVppVSFlKVLKLN 704
Cdd:PLN03130 836 L--MENAGKmeEYVEENGEEEDDQTSSKPVANGNANNLKKDSSSKKKSKEG---KSVLIKQEERETGV--VSW-KVLERY 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 705 KTEWP-YFVVGTV--CAIANGGLQPAFSVIFSEIIAIFGPgddavKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGE 781
Cdd:PLN03130 908 KNALGgAWVVMILflCYVLTEVFRVSSSTWLSEWTDQGTP-----KTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSL 982
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 782 ILTRRLRSMAFKAMLRQDMSWFddHKNSTGALSTRLATDaaqvqgatgtrLALIAQNIANLGTGIIISFiygWQL--TLL 859
Cdd:PLN03130 983 YAAKRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKD-----------LGDIDRNVAVFVNMFLGQI---FQLlsTFV 1046
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 860 LLAVVPIIAVSGIveMKLLAG---------NAKRDKKELEaagkiateaienirtvvSLTQERKFeSMYVEKLYG----- 925
Cdd:PLN03130 1047 LIGIVSTISLWAI--MPLLVLfygaylyyqSTAREVKRLD-----------------SITRSPVY-AQFGEALNGlstir 1106
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 926 PYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYL-IVNGHMrfrdVILVFSAIVFGAVALGHASSFAP------DYA 998
Cdd:PLN03130 1107 AYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWLAIRLeTLGGLM----IWLTASFAVMQNGRAENQAAFAStmglllSYA 1182
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 999 -------KAKLSAAHL----FMLFER-QPLIDSYSE-----EGLKPDK---FEGNITFNEVVFNYptRANVP-VLQGLSL 1057
Cdd:PLN03130 1183 lnitsllTAVLRLASLaensLNAVERvGTYIDLPSEaplviENNRPPPgwpSSGSIKFEDVVLRY--RPELPpVLHGLSF 1260
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1058 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENI 1137
Cdd:PLN03130 1261 EISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRI-------LIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1138 aygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE 1217
Cdd:PLN03130 1334 ---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD 1410
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1218 KVVQEALDKarEGRTC--IVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFS-MV 1277
Cdd:PLN03130 1411 ALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMV 1471
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
141-591 |
9.64e-55 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 200.28 E-value: 9.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 141 AAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDIskisEGIGDkvgMFFQAVATFFAGFIVGFIrgwkLTLVI 220
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGAA----AVAAI 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 221 MAISP----ILGLSAAVWAKILSAFS-----DKELAAYAKAGAVAEEALGAIR---TVIAFGGQNKELERYQKHLENAKE 288
Cdd:TIGR02868 149 AVLSVpaalILAAGLLLAGFVAPLVSlraarAAEQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTR 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 289 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTiGNAMTVFFSILIGAFSVGQAAP-CIDAFANARGAAYVI 367
Cdd:TIGR02868 229 AERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFEAFAALPaAAQQLTRVRAAAERI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 368 FDIIDNNPKIDSFSERGHKPDSIKG-NLEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLY 446
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 447 DPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLV 526
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 527 GERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 591
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
392-643 |
3.20e-54 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 200.33 E-value: 3.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYpsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:PRK10790 339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFSTTIAENICYGRgNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:PRK10790 417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKLVNMQ 631
Cdd:PRK10790 496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
|
250
....*....|..
gi 9961250 632 TSGSQIQSEEFE 643
Cdd:PRK10790 576 LAGEELAASVRE 587
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1003-1276 |
3.44e-54 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 199.67 E-value: 3.44e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1003 SAAHLFMLFERQPLIDSYSEEGLKPDKfeGNITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1082
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1083 ERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYgdnsrvvsqdeivsAAKAANIHP 1162
Cdd:PRK11160 387 TRAWDPQQGEI-------LLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--------------AAPNASDEA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1163 FIETL-----------PHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGR 1231
Cdd:PRK11160 446 LIEVLqqvgleklledDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK 525
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 9961250 1232 TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1276
Cdd:PRK11160 526 TVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
258-620 |
3.96e-54 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 199.11 E-value: 3.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 258 EALGAIRTViafggQNKELERYQKHLENAKEIGIKKAISANISMgiAFLLIYASYALAFwyGSTLVISKEYTIGnaMTVF 337
Cdd:TIGR01842 194 EAMGMMGNL-----TKRWGRFHSKYLSAQSAASDRAGMLSNLSK--YFRIVLQSLVLGL--GAYLAIDGEITPG--MMIA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 338 FSILigafsVGQAAPCID-------AFANARGAAYVIFDIIDNNPkidsFSERGHKPDSIKGNLEFNDVHFSYPSrANVK 410
Cdd:TIGR01842 263 GSIL-----VGRALAPIDgaiggwkQFSGARQAYKRLNELLANYP----SRDPAMPLPEPEGHLSVENVTIVPPG-GKKP 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENI 490
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 491 CYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 570
Cdd:TIGR01842 413 ARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQA 492
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 9961250 571 VQAALDKAR-EGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:TIGR01842 493 LANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
356-624 |
4.90e-53 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 196.60 E-value: 4.90e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 356 AFANARGAAYVIFDIIDNNpkiDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGK 435
Cdd:PRK11174 313 AKAQAVGAAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 436 STtvqLIQRL--YDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYE 513
Cdd:PRK11174 390 TS---LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSE 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 514 FIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLST 593
Cdd:PRK11174 467 FLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
250 260 270
....*....|....*....|....*....|.
gi 9961250 594 VRNADVIAGFEDGVIVEQGSHSELMKKEGVY 624
Cdd:PRK11174 547 LAQWDQIWVMQDGQIVQQGDYAELSQAGGLF 577
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
394-621 |
3.60e-52 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 182.92 E-value: 3.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPV--LFSTTIAENICYG---RGnVTMDEIKKAVKEA----NAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIA 544
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenLG-LPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-618 |
4.53e-52 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 192.04 E-value: 4.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN--VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 ---IGVVSQEPV--LF-STTIAENICYG---RGNVTMDEIKKAVKEANA-----YEFIMKLPqkfdtlvgergAQLSGGQ 537
Cdd:COG1123 341 rrrVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSH 614
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489
|
....
gi 9961250 615 SELM 618
Cdd:COG1123 490 EEVF 493
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
394-617 |
1.81e-51 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 180.84 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD-----PDEGTINIDGQDIR--NFNVN 466
Cdd:cd03260 1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 467 YLREIIGVVSQEPVLFSTTIAENICYG---RGNVTMDEIKKAVKEANAyefIMKLPQKFDTLVGERGaqLSGGQKQRIAI 543
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlHGIKLKEELDERVEEALR---KAALWDEVKDRLHALG--LSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 544 ARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
395-606 |
1.88e-51 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 180.36 E-value: 1.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYPSRaNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 475 VSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEANAyefIMKLPQKFDTLVgergAQLSGGQKQRIAIARALVRN 550
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDG 606
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
959-1269 |
5.25e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 189.87 E-value: 5.25e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 959 GAYLIVNGHMRFRDVILvfSAIVFGAvALG---HASSFAPDYAKAKLSAAHLFMLFERQPLidsySEEGLKPDKFEGNIT 1035
Cdd:TIGR01842 246 GAYLAIDGEITPGMMIA--GSILVGR-ALApidGAIGGWKQFSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1036 FNEVVFnYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKklnvQWL 1115
Cdd:TIGR01842 319 VENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSV-------RLDGADLK----QWD 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1116 RAQLG----IVSQEPILFDCSIAENIA-YGDNsrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRI 1190
Cdd:TIGR01842 387 RETFGkhigYLPQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRI 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1191 AIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:TIGR01842 464 ALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
394-608 |
9.73e-50 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 173.94 E-value: 9.73e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAENIcygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03246 80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 554 LLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVI 608
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1055-1276 |
2.07e-49 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 185.82 E-value: 2.07e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1055 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIA 1134
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSL-------KINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1135 ENIAYGDNSrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDT 1214
Cdd:PRK11174 441 DNVLLGNPD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1215 ESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1276
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
394-617 |
4.06e-49 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 174.80 E-value: 4.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--RNFNVNYLREI 471
Cdd:COG1126 2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFS-TTIAENICYG----RGnvtmdeIKKAVKEANAYEFIMK--LPQKFDtlvgERGAQLSGGQKQRIAIA 544
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvKK------MSKAEAEERAMELLERvgLADKAD----AYPAQLSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG1126 149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMrDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
394-613 |
1.90e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 176.42 E-value: 1.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI- 471
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 --IGVVSQEPVLFST-TIAENICY-----GrgnVTMDEIKKAVKE----------ANAYefimklPqkfdtlvgergAQL 533
Cdd:COG1135 82 rkIGMIFQHFNLLSSrTVAENVALpleiaG---VPKAEIRKRVAEllelvglsdkADAY------P-----------SQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 534 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVE 610
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVE 221
|
...
gi 9961250 611 QGS 613
Cdd:COG1135 222 QGP 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
412-561 |
3.52e-48 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 168.60 E-value: 3.52e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFS-TTIAENI 490
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 491 CYGRgnvTMDEIKKAVKEANAYEFIMKLPQKF--DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:pfam00005 81 RLGL---LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
394-612 |
1.07e-47 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 168.26 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRaNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNvNYLREIIG 473
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAENIcygrgnvtmdeikkavkeanayefimklpqkfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 554 LLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG 612
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
394-612 |
2.59e-47 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 169.22 E-value: 2.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN---VNYLR 469
Cdd:cd03257 2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 470 EIIGVVSQEPvlFST-----TIAENIC-----YGRGNvtmdeiKKAVKEANAYEFIMKLPQKfDTLVGERGAQLSGGQKQ 539
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAeplriHGKLS------KKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
394-589 |
8.24e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.92 E-value: 8.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:COG4619 1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAENI----CYGRGNVTMDEIKKAVKEANayefimkLPQKF-DTLVGErgaqLSGGQKQRIAIARALV 548
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9961250 549 RNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
394-617 |
8.50e-47 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 167.76 E-value: 8.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI- 471
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 --IGVVSQEPVLFST-TIAENICYGR--GNVTMDEIKKAVKE----------ANAYefimklPqkfdtlvgergAQLSGG 536
Cdd:cd03258 82 rrIGMIFQHFNLLSSrTVFENVALPLeiAGVPKAEIEERVLEllelvgledkADAY------P-----------AQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 613
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....
gi 9961250 614 HSEL 617
Cdd:cd03258 225 VEEV 228
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
394-611 |
1.82e-46 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 166.76 E-value: 1.82e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI- 471
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARLr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 ---IGVVSQEPVLFST-TIAENICYGRgnvTMDEIKKAVKEANAYEFIMKLpqkfdtLVGERG----AQLSGGQKQRIAI 543
Cdd:COG1136 85 rrhIGFVFQFFNLLPElTALENVALPL---LLAGVSRKERRERARELLERV------GLGDRLdhrpSQLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 544 ARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIA-HRLSTVRNADVIAGFEDGVIVEQ 611
Cdd:COG1136 156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
394-619 |
2.27e-46 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 166.69 E-value: 2.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:COG1127 6 IEVRNLTKSFGDR---VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 -IGVVSQEPVLFST-TIAENICYG---RGNVTMDEIKKAVkeanayefIMKLpqkfdTLVGERGA------QLSGGQKQR 540
Cdd:COG1127 83 rIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 541 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG1127 150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229
|
..
gi 9961250 618 MK 619
Cdd:COG1127 230 LA 231
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1034-1270 |
3.27e-46 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 165.97 E-value: 3.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQ 1113
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVD-------GKDITKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPI--LFDCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQK 1187
Cdd:COG1122 72 ELRRKVGLVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQ 1265
Cdd:COG1122 141 QRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPRE 220
|
....*
gi 9961250 1266 LLAQK 1270
Cdd:COG1122 221 VFSDY 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
394-612 |
6.63e-46 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 164.61 E-value: 6.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrnFNVNYLREIIG 473
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFST-TIAENICYG--RGNVTMDEIKKAVKEAnayEFIMKLpqkfDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVREL---LELVGL----EGLLNRYPHELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 612
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1039-1257 |
7.72e-46 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 162.77 E-value: 7.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1039 VVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQ 1118
Cdd:cd03246 6 VSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-------RLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1119 LGIVSQEPILFDCSIAENIaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtqLSGGQKQRIAIARALIR 1198
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1199 QPQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1257
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
394-608 |
1.00e-45 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 164.20 E-value: 1.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN----YL 468
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 469 REIIGVVSQEPVLFST-TIAENI---CYGRGnvtmdeIKKAVKEANAYEFI--MKLPQKFDTLVgergAQLSGGQKQRIA 542
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVelpLLLAG------VPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTVRNADVIAGFEDGVI 608
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
394-629 |
1.37e-45 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 1.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYlREIIG 473
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFST-TIAENICY-GRgnvtMDEIKKAVKEANAYEFI--MKLPQKFDTLVGergaQLSGGQKQRIAIARALVR 549
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRFfAR----LYGLPRKEARERIDELLelFGLTDAADRKVG----TLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFEDGVIVEQGSHSELMKK--EGVYF 625
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARllEDVFL 228
|
....
gi 9961250 626 KLVN 629
Cdd:COG1131 229 ELTG 232
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1034-1266 |
1.85e-45 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 163.89 E-value: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGTVfvdfgfqLLDGQE-- 1106
Cdd:cd03260 1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEV-------LLDGKDiy 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1107 AKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQ----DEIVSAA--KAAnihpfietLPhkyeTRVGDK-- 1178
Cdd:cd03260 71 DLDVDVLELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLkeelDERVEEAlrKAA--------LW----DEVKDRlh 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1179 GTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:cd03260 139 ALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRL 218
|
....*....
gi 9961250 1258 KEHGTHQQL 1266
Cdd:cd03260 219 VEFGPTEQI 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
394-618 |
5.37e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 171.24 E-value: 5.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIRNFNVNYLRE 470
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEP--VLFSTTIAENICYG--RGNVTMDEIKKAVKEANAYEFImklpqkfDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGL-------ERRLDRYPHQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELM 618
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
394-618 |
8.36e-45 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 162.47 E-value: 8.36e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFS-TTIAENIcygrGNV-TMDEIKKAVKEANAYEFI--MKLPQKfdTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI----ALVpKLLKWPKEKIRERADELLalVGLDPA--EFADRYPHELSGGQQQRVGVARALAA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRL-STVRNADVIAGFEDGVIVEQGSHSELM 618
Cdd:cd03295 153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
394-621 |
1.25e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 162.98 E-value: 1.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF-NVNYLREII 472
Cdd:TIGR04520 1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPQKfdtlvgergaqLSGGQKQRIAIA 544
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1034-1269 |
1.26e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 170.08 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAN--VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLN 1111
Cdd:COG1123 261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI-------LFDGKDLTKLS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 ---VQWLRAQLGIVSQEPIL-FDC--SIAENIAYG-DNSRVVSQDEIvsAAKAANI-------HPFIETLPHkyetrvgd 1177
Cdd:COG1123 334 rrsLRELRRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAER--RERVAELlervglpPDLADRYPH-------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1178 kgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQN 1254
Cdd:COG1123 404 ---ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYD 480
|
250
....*....|....*
gi 9961250 1255 GRVKEHGTHQQLLAQ 1269
Cdd:COG1123 481 GRIVEDGPTEEVFAN 495
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
394-617 |
1.60e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 165.27 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI-------RNfnvn 466
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtglppekRN---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 467 ylreiIGVVSQEPVLFS-TTIAENICYG---RGnVTMDEIKKAVKEANAyefIMKLPQKFDTLVgergAQLSGGQKQRIA 542
Cdd:COG3842 79 -----VGMVFQDYALFPhLTVAENVAFGlrmRG-VPKAEIRARVAELLE---LVGLEGLADRYP----HQLSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
394-606 |
3.97e-44 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 158.12 E-value: 3.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIR--NFNVNYLREI 471
Cdd:cd03229 1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdlEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFST-TIAENICYGrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRN 550
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 606
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1050-1257 |
5.69e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.83 E-value: 5.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQWLRAQLGIVSQEPILF 1129
Cdd:COG4619 14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIY-------LDGKPLSAMPPPEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIA--YGDNSRVVSQDEIVSAAKAANIHPFIetlphkYETRVgdkgTQLSGGQKQRIAIARALIRQPQILLLDE 1207
Cdd:COG4619 87 GGTVRDNLPfpFQLRERKFDRERALELLERLGLPPDI------LDKPV----ERLSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1208 ATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:COG4619 157 PTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
392-613 |
6.21e-44 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 158.73 E-value: 6.21e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03369 5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFSTTIAENI-CYGRgnVTMDEIKKAVKeanayefimklpqkfdtlVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 613
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1034-1261 |
7.30e-44 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 157.47 E-value: 7.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQ 1113
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-------TLDGVPVSDLEKA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wLRAQLGIVSQEPILFDCSIAENIaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkGTQLSGGQKQRIAIA 1193
Cdd:cd03247 73 -LSSLISVLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALA 110
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHG 1261
Cdd:cd03247 111 RILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1036-1256 |
9.79e-44 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 158.01 E-value: 9.79e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1036 FNEVVFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQWL 1115
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVD-------GKDLTKLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1116 RAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQR 1189
Cdd:cd03225 74 RRKVGLVFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1190 IAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1256
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
394-619 |
4.97e-43 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 156.89 E-value: 4.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 -IGVVSQEPVLF-STTIAENICYG---RGNVTMDEIKKAVKeanayefiMKLpqkfdTLVGERG------AQLSGGQKQR 540
Cdd:cd03261 78 rMGMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 541 IAIARALVRNPKILLLDEATSALDTESEAEVQA-ALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03261 145 VALARALALDPELLLYDEPTAGLDPIASGVIDDlIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
..
gi 9961250 618 MK 619
Cdd:cd03261 225 RA 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1034-1240 |
7.33e-43 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 165.23 E-value: 7.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQ 1113
Cdd:TIGR02868 335 LELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEV-------TLDGVPVSSLDQD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFDCSIAEN--IAYGDnsrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIA 1191
Cdd:TIGR02868 406 EVRRRVSVCAQDAHLFDTTVRENlrLARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLA 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961250 1192 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRL 1240
Cdd:TIGR02868 482 LARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
394-619 |
1.54e-42 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 156.12 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRA-NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREII 472
Cdd:COG1124 2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVL-----FS--TTIAENI-CYGRGNVtMDEIKKAVKEANayefimkLPqkfDTLVGERGAQLSGGQKQRIAIA 544
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLrIHGLPDR-EERIAELLEQVG-------LP---PSFLDRYPHQLSGGQRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
394-589 |
1.64e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 156.40 E-value: 1.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfnvnyLREII 472
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFS-TTIAENICYGrgnVTMDEIKKAVKEANAYEFImklpqkfdTLVGERGA------QLSGGQKQRIAIAR 545
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALG---LELRGVPKAERRERARELL--------ELVGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
394-608 |
1.91e-42 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 154.61 E-value: 1.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRN--FNVNYLREI 471
Cdd:cd03262 1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFS-TTIAENICYGRgnVTMDEIKKAVKEANAYEFIMK--LPQKFDtlvgERGAQLSGGQKQRIAIARALV 548
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 549 RNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 608
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
395-606 |
3.37e-42 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 151.63 E-value: 3.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 475 VSQepvlfsttiaenicygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd00267 78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 555 LLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFEDG 606
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
116-629 |
4.88e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 169.00 E-value: 4.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 116 YAYYYSGLGAGvLVAAYIQVSFWTLAAG-RQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGM 194
Cdd:PLN03232 952 YIVVYALLGFG-QVAVTFTNSFWLISSSlHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNM 1030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 195 F----FQAVATFFAGFIVGFIRGWkltlvimAISPILGLSAAVWAKILSAFSD-KELAAYAKAGAVAE--EALGAIRTVI 267
Cdd:PLN03232 1031 FmnqlWQLLSTFALIGTVSTISLW-------AIMPLLILFYAAYLYYQSTSREvRRLDSVTRSPIYAQfgEALNGLSSIR 1103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 268 AFGGQNKELERYQKHLENAKEIGIKkAISAN-------ISMGIAFLLIYASYALAFW--------YGSTLVISKEYTIgN 332
Cdd:PLN03232 1104 AYKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAVLRNgnaenqagFASTMGLLLSYTL-N 1181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 333 AMTVFFSILIGAFSVGQAAPCIDAFANARGAAYVIFDIIDNNPKIDSFSERGhkpdSIKgnleFNDVHFSYpsRANVK-I 411
Cdd:PLN03232 1182 ITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG----SIK----FEDVHLRY--RPGLPpV 1251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENI- 490
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNId 1331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 491 CYGRGNVTmdEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAE 570
Cdd:PLN03232 1332 PFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 571 VQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEG-VYFKLVN 629
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVH 1469
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
394-589 |
1.72e-41 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 151.86 E-value: 1.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPS-RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylreiI 472
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFS-TTIAENICYGrgnVTMDEIKKAVKEANAYEFImklpqkfdTLVGERGA------QLSGGQKQRIAIAR 545
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELL--------ELVGLSGFenayphQLSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
394-617 |
2.78e-41 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 156.00 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfnVNYL----R 469
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLppkdR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 470 EIiGVVSQEPVLF-STTIAENICYG---RGnVTMDEIKKAVKEANAyefIMKLpqkfDTLVGERGAQLSGGQKQRIAIAR 545
Cdd:COG3839 76 NI-AMVFQSYALYpHMTVYENIAFPlklRK-VPKAEIDRRVREAAE---LLGL----EDLLDRKPKQLSGGQRQRVALGR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 546 ALVRNPKILLLDEATSALD------TESE-AEVQAALdkareGRTTIVIAH------RLstvrnADVIAGFEDGVIVEQG 612
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQVG 216
|
....*
gi 9961250 613 SHSEL 617
Cdd:COG3839 217 TPEEL 221
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1046-1268 |
2.98e-41 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 152.26 E-value: 2.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1046 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQE 1125
Cdd:COG1124 15 GRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEV-------TFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PIL-------FDCSIAE--NIAYGDNSrvvsQDEIVSAAKAANIHP-FIETLPHkyetrvgdkgtQLSGGQKQRIAIARA 1195
Cdd:COG1124 88 PYAslhprhtVDRILAEplRIHGLPDR----EERIAELLEQVGLPPsFLDRYPH-----------QLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1196 LIRQPQILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:COG1124 153 LILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
85-367 |
3.44e-41 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 153.48 E-value: 3.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 85 FVDTAGNFSFPVnFSLSLLN--PGKILEEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEI 162
Cdd:cd18557 6 LISSAAQLLLPY-LIGRLIDtiIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 163 GWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFS 242
Cdd:cd18557 85 AFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 243 DKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTL 322
Cdd:cd18557 165 KEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 9961250 323 VISKEYTIGNAMT-VFFSILIgAFSVGQAAPCIDAFANARGAAYVI 367
Cdd:cd18557 245 VLSGQLTVGELTSfILYTIMV-ASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1032-1262 |
3.49e-41 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 150.64 E-value: 3.49e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1032 GNITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKL 1110
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKI-------EIDGIDISTI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1111 NVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAakaanihpfietlphkyeTRVGDKGTQLSGGQKQRI 1190
Cdd:cd03369 76 PLEDLRSSLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLL 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1191 AIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1262
Cdd:cd03369 135 CLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
394-621 |
3.62e-41 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 152.51 E-value: 3.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVL-FSTTIAENICYGR-------GNVT---MDEIKKAVKEANAYEFIMKLpqkFDTlvgergaqLSGGQKQRIA 542
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfGRPSaedREAVEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
..
gi 9961250 620 KE 621
Cdd:COG1120 228 PE 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1034-1259 |
1.40e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 149.54 E-value: 1.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEakklnV 1112
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEV-------LVDGEP-----V 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWLRAQLGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIEtlphkyetRVGDKGT------QLSGG 1185
Cdd:cd03293 69 TGPGPDRGYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-----LE--------LVGLSGFenayphQLSGG 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1186 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQN--GRVKE 1259
Cdd:cd03293 136 MRQRVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1045-1261 |
4.57e-40 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 147.67 E-value: 4.57e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQwlRAQLGIVSQ 1124
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILID-------GRDVTGVPPE--RRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 EPILFD-CSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQ 1199
Cdd:cd03259 80 DYALFPhLTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYPH-----------ELSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1200 PQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1261
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1034-1270 |
7.01e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 149.12 E-value: 7.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGQeakklNVQ 1113
Cdd:TIGR04520 1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-GLDTLDEE-----NLW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPilfD----CSIAEN-IAYGDNSRVVSQDEIVS----AAKAANIHPFIETLPHKyetrvgdkgtqLSG 1184
Cdd:TIGR04520 74 EIRKKVGMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1185 GQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1262
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
....*...
gi 9961250 1263 HQQLLAQK 1270
Cdd:TIGR04520 220 PREIFSQV 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1052-1210 |
9.19e-40 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 144.33 E-value: 9.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILF-D 1130
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI-------LLDGQDLTDDERKSLRKEIGYVFQDPQLFpR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 CSIAENIAYGDNSRvvsqdEIVSAAKAANIHPFIETL--PHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:pfam00005 74 LTVRENLRLGLLLK-----GLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
..
gi 9961250 1209 TS 1210
Cdd:pfam00005 149 TA 150
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
394-612 |
9.69e-40 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 148.26 E-value: 9.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD--PD---EGTINIDGQDI--RNFNVN 466
Cdd:COG1117 12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 467 YLREIIGVVSQEPVLFSTTIAENICYG------RGNVTMDEI-----KKA-----VKeanayefimklpqkfDTLvGERG 530
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIveeslRKAalwdeVK---------------DRL-KKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 531 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREgRTTIVI-------AHRLStvrnaDVIAGF 603
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFF 226
|
....*....
gi 9961250 604 EDGVIVEQG 612
Cdd:COG1117 227 YLGELVEFG 235
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
394-617 |
1.05e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 147.90 E-value: 1.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:COG3638 3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 -IGVVSQEPVLFS-TTIAENICYGR-----------GNVTMDEIKKAvkeanayefimklpqkFDTL--VG------ERG 530
Cdd:COG3638 81 rIGMIFQQFNLVPrLSVLTNVLAGRlgrtstwrsllGLFPPEDRERA----------------LEALerVGladkayQRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 531 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGV 607
Cdd:COG3638 145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224
|
250
....*....|
gi 9961250 608 IVEQGSHSEL 617
Cdd:COG3638 225 VVFDGPPAEL 234
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1043-1261 |
1.37e-39 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 146.88 E-value: 1.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1043 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQWL---RAQ 1118
Cdd:cd03257 11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII-------FDGKDLLKLSRRLRkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1119 LGIVSQEPI-----LFdcSIAENIAygdnsrvvsqdEIVSAAKAANIHPFIETLPHKYETRVGDKGT-------QLSGGQ 1186
Cdd:cd03257 84 IQMVFQDPMsslnpRM--TIGEQIA-----------EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvlnryphELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1187 KQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1261
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
394-622 |
1.89e-39 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 146.93 E-value: 1.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIiG 473
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFST-TIAENICY-GRGNvtmdEIKKAVKEANAYEFI--MKLPQKFDTLVGErgaqLSGGQKQRIAIARALVR 549
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRYfAELY----GLFDEELKKRIEELIelLGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEG 622
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
394-610 |
2.90e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.58 E-value: 2.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQD---IRNFNVNYLRE 470
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQE-PVLFSTTIAENICY-----GRgnvTMDEIKKAVKEAnayefIMK--LPQKFDTLVgergAQLSGGQKQRIA 542
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGK---SRKEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRNAD--VIAgFEDGVIVE 610
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1034-1259 |
3.00e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGTVFVDfgfqlldGQEAKK 1109
Cdd:COG1136 5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLID-------GQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 LN----VQWLRAQLGIVSQEPILFDC-SIAENIA----YGDNSRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgt 1180
Cdd:COG1136 75 LSerelARLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1181 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVK 1258
Cdd:COG1136 144 QLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
|
.
gi 9961250 1259 E 1259
Cdd:COG1136 224 S 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1048-1269 |
3.41e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 145.91 E-value: 3.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPLAGTVFVDfGFQLLDgqeaKKLNVQWLRAQLGIVSQ 1124
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVD-GEDLTD----SKKDINKLRRKVGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 EPILF-DCSIAENIAYGdnSRVVSQdeiVSAAKAanihpfiETLPHKYETRVG--DKG----TQLSGGQKQRIAIARALI 1197
Cdd:COG1126 85 QFNLFpHLTVLENVTLA--PIKVKK---MSKAEA-------EERAMELLERVGlaDKAdaypAQLSGGQQQRVAIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1198 RQPQILLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:COG1126 153 MEPKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1034-1269 |
3.94e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 153.52 E-value: 3.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAnVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERfYDPLAGTVFvdfGFQLLDGQEAKKLNVQ 1113
Cdd:COG1123 5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRIS---GEVLLDGRDLLELSEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPI--LFDCSIAENIAYGDNSRVVSQDEI----VSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQK 1187
Cdd:COG1123 80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEArarvLELLEAVGLERRLDRYPH-----------QLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQ 1264
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPE 228
|
....*
gi 9961250 1265 QLLAQ 1269
Cdd:COG1123 229 EILAA 233
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
714-1000 |
6.06e-39 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 146.94 E-value: 6.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 714 GTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVkqqkcNIFSLIFLFLGII---SFFTFFlQGFTFGKAGEILTRRLRSM 790
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLD-----VLNELALILLAIYllqSVFTFV-RYYLFNIAGERIVARLRRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 791 AFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVS 870
Cdd:cd18557 75 LFSSLLRQEIAFFDKHK--TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 871 GIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYF 950
Cdd:cd18557 153 SKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 951 SYAGCFRFGAYLIVNGHMRFRDVI--LVFSAIVfgAVALGHASSFAPDYAKA 1000
Cdd:cd18557 233 SLLLVLWYGGYLVLSGQLTVGELTsfILYTIMV--ASSVGGLSSLLADIMKA 282
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
394-608 |
6.10e-39 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 142.92 E-value: 6.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFST-TIAENIcygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaQLSGGQKQRIAIARALVRNPK 552
Cdd:cd03230 77 YLPEEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 553 ILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 608
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
395-616 |
7.28e-39 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 148.41 E-value: 7.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:PRK11153 3 ELKNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 -IGVVSQE-PVLFSTTIAENICYGR--GNVTMDEIKKAVKE----------ANAYefimklPqkfdtlvgergAQLSGGQ 537
Cdd:PRK11153 83 qIGMIFQHfNLLSSRTVFDNVALPLelAGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIV-IAHRLSTVRN-ADVIAGFEDGVIVEQGSH 614
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQGTV 225
|
..
gi 9961250 615 SE 616
Cdd:PRK11153 226 SE 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1034-1262 |
2.32e-38 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 147.55 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQ 1113
Cdd:COG3842 6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRI-------LLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wlRAQLGIVSQEPILF-DCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQKQ 1188
Cdd:COG3842 76 --KRNVGMVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQ 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1189 RIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVFQNGRVKEHGT 1262
Cdd:COG3842 143 RVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1034-1256 |
3.01e-38 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 142.22 E-value: 3.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRANV--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPLAGTVFVdfgfqlldgqeakk 1109
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSV-------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 lnvqwlRAQLGIVSQEPILFDCSIAENIAYG---DNSRVvsqDEIVsaaKAANIHPFIETLPHKYETRVGDKGTQLSGGQ 1186
Cdd:cd03250 65 ------PGSIAYVSQEPWIQNGTIRENILFGkpfDEERY---EKVI---KACALEPDLEILPDGDLTEIGEKGINLSGGQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1187 KQRIAIARALIRQPQILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVFQNGR 1256
Cdd:cd03250 133 KQRISLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
394-619 |
3.46e-38 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 145.97 E-value: 3.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDP---DEGTINIDGQDIRNFNVNYLR 469
Cdd:COG0444 2 LEVRNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 470 EI----IGVVSQEPvlFS---------TTIAENICYGRGnVTMDEIKKAVKEA-------NAYEFIMKLPQkfdtlvger 529
Cdd:COG0444 82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRIHGG-LSKAEARERAIELlervglpDPERRLDRYPH--------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 530 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIA- 601
Cdd:COG0444 150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
|
250 260
....*....|....*....|
gi 9961250 602 --GfedGVIVEQGSHSELMK 619
Cdd:COG0444 224 myA---GRIVEEGPVEELFE 240
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1034-1267 |
5.69e-38 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 143.26 E-value: 5.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQ 1113
Cdd:COG1120 2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEV-------LLDGRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPIL-FDCSIAENIAYG------DNSRVVSQD-EIVSAA-KAANIHPFIETlphkyetRVgdkgTQLSG 1184
Cdd:COG1120 72 ELARRIAYVPQEPPApFGLTVRELVALGryphlgLFGRPSAEDrEAVEEAlERTGLEHLADR-------PV----DELSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1185 GQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1261
Cdd:COG1120 141 GERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQG 220
|
....*.
gi 9961250 1262 THQQLL 1267
Cdd:COG1120 221 PPEEVL 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1034-1259 |
6.31e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 143.31 E-value: 6.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEakklnV 1112
Cdd:COG1116 8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEV-------LVDGKP-----V 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWLRAQLGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQK 1187
Cdd:COG1116 76 TGPGPDRGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVFQN--GRV 1257
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRI 219
|
..
gi 9961250 1258 KE 1259
Cdd:COG1116 220 VE 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
394-606 |
9.58e-38 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 140.68 E-value: 9.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANV--KILKGLNLKVQSGQTVALVGSSGCGKSTtvqLIQRL---YDPDEGTINIDGQdirnfnvnyl 468
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSS---LLSALlgeLEKLSGSVSVPGS---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 469 reiIGVVSQEPVLFSTTIAENICYGRgnvTMDEIK-KAVKEANAYEFIMK-LPQKFDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03250 68 ---IAYVSQEPWIQNGTIRENILFGK---PFDEERyEKVIKACALEPDLEiLPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEV--QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDG 606
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1034-1269 |
3.85e-37 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 140.02 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGTVFVDfgfqlldGQEAKK 1109
Cdd:cd03258 2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVD-------GTDLTL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 LN---VQWLRAQLGIVSQEPILFDC-SIAENIAYGDNSRVVSQDEIvsaakAANIHPFIET--LPHKYETRVGdkgtQLS 1183
Cdd:cd03258 72 LSgkeLRKARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEI-----EERVLELLELvgLEDKADAYPA----QLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1184 GGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1260
Cdd:cd03258 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEE 222
|
....*....
gi 9961250 1261 GTHQQLLAQ 1269
Cdd:cd03258 223 GTVEEVFAN 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
395-621 |
4.64e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.90 E-value: 4.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:PRK13632 9 KVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 475 VSQEP--VLFSTTIAENICYGRGN--VTMDEIKK----AVKEANAYEFIMKLPQKfdtlvgergaqLSGGQKQRIAIARA 546
Cdd:PRK13632 88 IFQNPdnQFIGATVEDDIAFGLENkkVPPKKMKDiiddLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1034-1269 |
5.39e-37 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 139.81 E-value: 5.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdFGFQLLDGQEAkklnvq 1113
Cdd:COG1131 1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV-LGEDVARDPAE------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wLRAQLGIVSQEPILF-DCSIAENIAYGDNSRVVSQDEIvsaakAANIHPFIET--LPHKYETRVGdkgtQLSGGQKQRI 1190
Cdd:COG1131 71 -VRRRIGYVPQEPALYpDLTVRENLRFFARLYGLPRKEA-----RERIDELLELfgLTDAADRKVG----TLSGGMKQRL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1191 AIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:COG1131 141 GLALALLHDPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
|
.
gi 9961250 1269 Q 1269
Cdd:COG1131 221 R 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
394-617 |
7.00e-37 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 139.63 E-value: 7.00e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-- 471
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 -IGVVSQEPVLFS-TTIAENICYGR-----------GNVTMDEIKKAvkeanayefiMKLPQKF--DTLVGERGAQLSGG 536
Cdd:cd03256 79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRA----------LAALERVglLDKAYQRADQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKARE-GRTTIVIAHRLSTVR-NADVIAGFEDGVIVEQGS 613
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGP 228
|
....
gi 9961250 614 HSEL 617
Cdd:cd03256 229 PAEL 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1034-1269 |
8.40e-37 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.54 E-value: 8.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPtRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQ 1113
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-------GMVLSEETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPilfD-----CSIAENIAYGDNSRVVSQDEIV----SAAKAANIHPFIETLPHKyetrvgdkgtqLSG 1184
Cdd:PRK13635 78 DVRRQVGMVFQNP---DnqfvgATVQDDVAFGLENIGVPREEMVervdQALRQVGMEDFLNREPHR-----------LSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1185 GQKQRIAIARALIRQPQILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1259
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILE 220
|
250
....*....|
gi 9961250 1260 HGTHQQLLAQ 1269
Cdd:PRK13635 221 EGTPEEIFKS 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
394-621 |
1.05e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 139.07 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfnvnyLREIIG 473
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVL---FSTTIAENI---CYGRGNVTM---DEIKKAVKEA----NAYEFImklpqkfDTLVGErgaqLSGGQKQR 540
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsRADREAVDEAlervGLEDLA-------DRPIGE----LSGGQQQR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 541 IAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVR-NADVIAGFEDGVIVEqGSHSELM 618
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226
|
...
gi 9961250 619 KKE 621
Cdd:COG1121 227 TPE 229
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1034-1262 |
1.46e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 141.75 E-value: 1.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGTVFVDfgfqlldGQEAKK 1109
Cdd:COG1135 2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVD-------GVDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 LNVQWLRA---QLGIVSQEPILFD-CSIAENIAY-----GdnsrvVSQDEIvsAAKAAnihpfiETLphkyeTRVG--DK 1178
Cdd:COG1135 72 LSERELRAarrKIGMIFQHFNLLSsRTVAENVALpleiaG-----VPKAEI--RKRVA------ELL-----ELVGlsDK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1179 G----TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVV 1251
Cdd:COG1135 134 AdaypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAV 213
|
250
....*....|.
gi 9961250 1252 FQNGRVKEHGT 1262
Cdd:COG1135 214 LENGRIVEQGP 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
394-617 |
1.75e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 141.82 E-value: 1.75e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--------RNfnv 465
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLftnlppreRR--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 nylreiIGVVSQEPVLF-STTIAENICYG--RGNVTMDEIKKAVKE----------ANAYefimklPqkfdtlvgergAQ 532
Cdd:COG1118 77 ------VGFVFQHYALFpHMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------P-----------SQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdkaRE-----GRTTIVIAH-RLSTVRNADVIAGFEDG 606
Cdd:COG1118 134 LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWL---RRlhdelGGTTVFVTHdQEEALELADRVVVMNQG 210
|
250
....*....|.
gi 9961250 607 VIVEQGSHSEL 617
Cdd:COG1118 211 RIEQVGTPDEV 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
416-618 |
2.66e-36 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 138.93 E-value: 2.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 416 NLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI----IGVVSQEPVLF-STTIAENI 490
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 491 CYG---RGnvtmdeIKKAVKEANAYEFImklpqkfdTLVGERG------AQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:cd03294 124 AFGlevQG------VPRAEREERAAEAL--------ELVGLEGwehkypDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 562 ALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELM 618
Cdd:cd03294 190 ALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
108-364 |
5.03e-36 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 138.84 E-value: 5.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 108 ILEEEMTRYAYYYSGLGAGVLVAA---YIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKI 184
Cdd:cd07346 30 IPAGDLSLLLWIALLLLLLALLRAllsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 185 SEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIR 264
Cdd:cd07346 110 QNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 265 TVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGA 344
Cdd:cd07346 190 VVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIG-ELVAFLAYLGML 268
|
250 260
....*....|....*....|.
gi 9961250 345 FS-VGQAAPCIDAFANARGAA 364
Cdd:cd07346 269 FGpIQRLANLYNQLQQALASL 289
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1272 |
5.29e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 138.20 E-value: 5.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQ 1113
Cdd:PRK13632 8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIK-------IDGITISKENLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPilfD-----CSIAENIAYGDNSRVVSQDE----IVSAAKAANIHPFIETLPHKyetrvgdkgtqLSG 1184
Cdd:PRK13632 80 EIRKKIGIIFQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1185 GQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1262
Cdd:PRK13632 146 GQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
250
....*....|
gi 9961250 1263 HQQLLAQKGI 1272
Cdd:PRK13632 226 PKEILNNKEI 235
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
110-350 |
5.90e-36 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 138.54 E-value: 5.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 110 EEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIG 189
Cdd:cd18780 38 LRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 190 DKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAF 269
Cdd:cd18780 118 VNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSF 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 270 GGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnAMTVFfsiLIGAFSVGQ 349
Cdd:cd18780 198 AKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTG-LLTSF---LLYTLTVAM 273
|
.
gi 9961250 350 A 350
Cdd:cd18780 274 S 274
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
391-627 |
6.79e-36 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 148.94 E-value: 6.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 391 KGNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:TIGR00957 1282 RGRVEFRNYCLRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFSTTIAENIcYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNL-DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRK 1439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYFKL 627
Cdd:TIGR00957 1440 TKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
394-588 |
1.19e-35 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 135.23 E-value: 1.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN---VNYLRE 470
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFST-TIAENICYGR--GNVTMDEIKKAVKEANAyefIMKLPQKFDTLvgerGAQLSGGQKQRIAIARAL 547
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALevTGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA 588
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1032-1277 |
1.30e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 136.58 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1032 GNITFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLN 1111
Cdd:cd03288 18 GEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKI-------VIDGIDISKLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 VQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIA 1191
Cdd:cd03288 90 LHTLRSRLSIILQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1192 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK- 1270
Cdd:cd03288 167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEd 246
|
....*..
gi 9961250 1271 GIYFSMV 1277
Cdd:cd03288 247 GVFASLV 253
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
394-612 |
1.36e-35 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 134.69 E-value: 1.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPsraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfnVNYL----R 469
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD-----VTDLppkdR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 470 EIiGVVSQEPVLF-STTIAENICYG--RGNVTMDEIKKAVKEANAyefIMKLpqkfDTLVGERGAQLSGGQKQRIAIARA 546
Cdd:cd03301 73 DI-AMVFQNYALYpHMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQI----EHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQG 612
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1051-1266 |
1.68e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.93 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--PLA---GTVfvdfgfqLLDGQE--AKKLNVQWLRAQLGIVS 1123
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEI-------LLDGEDiyDPDVDVVELRRRVGMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 QEPILFDCSIAENIAYG-----DNSRVVsQDEIVSAA--KAAnihpfietLPHKYETRVGDKGTQLSGGQKQRIAIARAL 1196
Cdd:COG1117 99 QKPNPFPKSIYDNVAYGlrlhgIKSKSE-LDEIVEESlrKAA--------LWDEVKDRLKKSALGLSGGQQQRLCIARAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1197 IRQPQILLLDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVFQNGRVKEHGTHQQL 1266
Cdd:COG1117 170 AVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
412-629 |
3.40e-35 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 134.39 E-value: 3.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIGVVSQEPVLF-STTIAENI 490
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 491 CYGRGNVTMD--EIKKAVKEANAYEFImklpqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 568
Cdd:cd03299 93 AYGLKKRKVDkkEIERKVLEIAEMLGI-------DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 569 AEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGshselmKKEGVYFKLVN 629
Cdd:cd03299 166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVG------KPEEVFKKPKN 223
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
395-597 |
3.73e-35 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 133.43 E-value: 3.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFnvnylREIIGV 474
Cdd:cd03235 1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 475 VSQEPVL---FSTTIAENI---CYGRGNVTMdEIKKAVKEA--NAYEFiMKLPQKFDTLVGErgaqLSGGQKQRIAIARA 546
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmgLYGHKGLFR-RLSKADKAKvdEALER-VGLSELADRQIGE----LSGGQQQRVLLARA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA 597
Cdd:cd03235 147 LVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1035-1256 |
3.80e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 131.60 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1035 TFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQW 1114
Cdd:cd00267 1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI-------LIDGKDIAKLPLEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1115 LRAQLGIVSQepilfdcsiaeniaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtqLSGGQKQRIAIAR 1194
Cdd:cd00267 71 LRRRIGYVPQ---------------------------------------------------------LSGGQRQRVALAR 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1195 ALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGR 1256
Cdd:cd00267 94 ALLLNPDLLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
111-332 |
3.80e-35 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 136.13 E-value: 3.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 111 EEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGD 190
Cdd:cd18572 33 EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLST 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:cd18572 113 NLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 332
Cdd:cd18572 193 TEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1045-1256 |
5.00e-35 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 131.93 E-value: 5.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLN--VQWLRAQLGIV 1122
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIL-------IDGEDLTDLEdeLPPLRRRIGMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 SQEPILF-DCSIAENIAYGdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtqLSGGQKQRIAIARALIRQPQ 1201
Cdd:cd03229 82 FQDFALFpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1202 ILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1256
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1034-1268 |
5.03e-35 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 133.78 E-value: 5.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGQEAKKLNvq 1113
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLID-GEDISGLSEAELYR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wLRAQLGIVSQEPILFDC-SIAENIAY-----GDNSRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQK 1187
Cdd:cd03261 75 -LRRRMGMLFQSGALFDSlTVFENVAFplrehTRLSEEEIREIVLEKLEAVGLRGAEDLYPA-----------ELSGGMK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQ 1264
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPE 222
|
....
gi 9961250 1265 QLLA 1268
Cdd:cd03261 223 ELRA 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1034-1257 |
5.21e-35 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 133.38 E-value: 5.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNV 1112
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD-------GTDISKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWL----RAQLGIVSQE----PILfdcSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIET--LPHKYETRVGdkgtQL 1182
Cdd:cd03255 74 KELaafrRRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----EL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1183 SGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVFQNGRV 1257
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
711-968 |
7.87e-35 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 135.37 E-value: 7.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDavkQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSM 790
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGD---LSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 791 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVS 870
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 871 GIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYF 950
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250
....*....|....*...
gi 9961250 951 SYAGCFRFGAYLIVNGHM 968
Cdd:cd07346 236 GTALVLLYGGYLVLQGSL 253
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
408-617 |
9.02e-35 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 133.13 E-value: 9.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 408 NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIGVVSQEPVLFS-TTI 486
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENICYG--RGNVTMDEIKKAVKEAnayefiMKLPQkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:cd03300 90 FENIAFGlrLKKLPKAEIKERVAEA------LDLVQ-LEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 565 TESEAEVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03300 163 LKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
392-628 |
2.20e-34 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 133.11 E-value: 2.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYPSraNVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:cd03288 18 GEIKIHDLCVRYEN--NLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFSTTIAENICYGRgNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELM-KKEGVYFKLV 628
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1034-1271 |
2.46e-34 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 132.29 E-value: 2.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNvQ 1113
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI-------LIDGEDVRKEP-R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIvsAAKAANIHPFIEtLPHKYETRVGDkgtqLSGGQKQRIAI 1192
Cdd:COG4555 71 EARRQIGVLPDERGLYDrLTVRENIRYFAELYGLFDEEL--KKRIEELIELLG-LEEFLDRRVGE----LSTGMKKKVAL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1193 ARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:COG4555 144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEI 223
|
.
gi 9961250 1271 G 1271
Cdd:COG4555 224 G 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
401-1278 |
2.72e-34 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 143.90 E-value: 2.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 401 FSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirnfnvnylreiIGVVSQEPV 480
Cdd:TIGR01271 431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 481 LFSTTIAENICYGrgnVTMDEIK--KAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:TIGR01271 498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 559 ATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVY------------- 624
Cdd:TIGR01271 575 PFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdnf 654
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 625 ------------------------------------------------------------FKLVNMQTSGSQIQSEE--- 641
Cdd:TIGR01271 655 saerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVQMGPQKAQATTIEdav 734
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 642 -------FEL---NDEKAATRMAPNGWKSRL--------------------------FRHSTQKNLKNSQMCQKS--LDV 683
Cdd:TIGR01271 735 repserkFSLvpeDEQGEESLPRGNQYHHGLqhqaqrrqsvlqlmthsnrgenrreqLQTSFRKKSSITQQNELAseLDI 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 684 ETDGL------------------------EANVPPV----SFLKVLKLNKTewPYFVVGTVCAIANGGLQPAFSVIFseI 735
Cdd:TIGR01271 815 YSRRLskdsvyeiseeineedlkecfadeRENVFETttwnTYLRYITTNRN--LVFVLIFCLVIFLAEVAASLLGLW--L 890
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 736 IAIFGPGDDAVKQQKCNIFSLIFLFLGII----SFFTF--------------FLQGFTFGKAGEILTRRLRSMAFKAMLR 797
Cdd:TIGR01271 891 ITDNPSAPNYVDQQHANASSPDVQKPVIItptsAYYIFyiyvgtadsvlalgFFRGLPLVHTLLTVSKRLHEQMLHSVLQ 970
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 798 QDMSWFDDHKnsTGALSTRLATDAAQVQGATG-TRLALIAQNIANLGTGIIISFIYGWqltlLLLAVVPIIAVSGIVEMK 876
Cdd:TIGR01271 971 APMAVLNTMK--AGRILNRFTKDMAIIDDMLPlTLFDFIQLTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAY 1044
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 877 LLAGNAKRDKKELEAAGKIATEAIENIR---TVVSLTQERKFESMYveklygpyrnsvQKAhiygITFSISQAFMYFSYA 953
Cdd:TIGR01271 1045 FLRTSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLF------------HKA----LNLHTANWFLYLSTL 1108
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 954 GCFRFGAYLIvnghmrfrdVILVFSAIVFGAVAlghASSFAPDYAKAKLSAAHLFMLFERQPLIDSYSEEGL-------- 1025
Cdd:TIGR01271 1109 RWFQMRIDII---------FVFFFIAVTFIAIG---TNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLmrsvsrvf 1176
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1026 ----------KPDK-----------------------FEGNITFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSG 1072
Cdd:TIGR01271 1177 kfidlpqeepRPSGgggkyqlstvlvienphaqkcwpSGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTG 1255
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1073 CGKSTVVQLLERfydpLAGTVfvdfGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIV 1152
Cdd:TIGR01271 1256 SGKSTLLSALLR----LLSTE----GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIW 1324
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1153 SAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRT 1232
Cdd:TIGR01271 1325 KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCT 1404
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 9961250 1233 CIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVS 1278
Cdd:TIGR01271 1405 VILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAMS 1450
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
406-618 |
3.51e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 134.47 E-value: 3.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI---IGVVSQEPvlF 482
Cdd:COG4608 28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 483 S---------TTIAENICYgRGNVTMDEIKKAVKEA------NAyEFIMKLPQKFdtlvgergaqlSGGQKQRIAIARAL 547
Cdd:COG4608 106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARAL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 548 VRNPKILLLDEATSALDTESEAEV-------QAALdkareGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:COG4608 173 ALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELY 246
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
410-612 |
3.70e-34 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 130.88 E-value: 3.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQ---SGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ---DIR-NFNVNYLREIIGVVSQEPVLF 482
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 483 S-TTIAENICYGRGNVTMDEIKKAVKEANAYefiMKLpqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:cd03297 88 PhLNVRENLAFGLKRKRNREDRISVDELLDL---LGL----DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 562 ALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 612
Cdd:cd03297 161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1050-1268 |
4.07e-34 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 131.64 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNV---QWLRAQLGIVSQEP 1126
Cdd:COG1127 19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-------GQDITGLSEkelYELRRRIGMLFQGG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILFDC-SIAENIAYG-DNSRVVSQDEIVSAA----KAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQP 1200
Cdd:COG1127 92 ALFDSlTVFENVAFPlREHTDLSEAEIRELVleklELVGLPGAADKMPS-----------ELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1201 QILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
392-634 |
1.19e-33 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 141.80 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYpsRANVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFSTTIAENI-CYGRGNVTmdEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLdPFNEHNDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEGVYF-KLV 628
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFsKMV 1471
|
....*.
gi 9961250 629 nmQTSG 634
Cdd:PLN03130 1472 --QSTG 1475
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
394-619 |
1.23e-33 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13635 6 IRVEHISFRYPD-AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDE----IKKAVKEANAYEFIMKLPqkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13635 85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
394-613 |
2.08e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 133.53 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF-----NVNyl 468
Cdd:PRK09452 15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaenrHVN-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 469 reiigVVSQEPVLFS-TTIAENICYG--RGNVTMDEIKKAVKEAnayefiMKLPQkFDTLVGERGAQLSGGQKQRIAIAR 545
Cdd:PRK09452 90 -----TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALdKA--RE-GRTTIVIAH----RLSTvrnADVIAGFEDGVIVEQGS 613
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGT 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1034-1257 |
2.09e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.79 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLN-- 1111
Cdd:COG3638 3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEI-------LVDGQDVTALRgr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 -VQWLRAQLGIVSQEPILFD-CSIAENI---AYGDNS------RVVSQDEIVSAAKAanihpfIET--LPHKYETRVGdk 1178
Cdd:COG3638 74 aLRRLRRRIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERALEA------LERvgLADKAYQRAD-- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1179 gtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNG 1255
Cdd:COG3638 146 --QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDG 223
|
..
gi 9961250 1256 RV 1257
Cdd:COG3638 224 RV 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
394-618 |
2.48e-33 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 129.44 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDV--HFsypsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNyLREI 471
Cdd:PRK09493 2 IEFKNVskHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVD-ERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 ---IGVVSQEPVLFSTTIA-ENICYG----RGnvtmdeIKKAVKEANAYEFIMKlpqkfdtlVG--ERG----AQLSGGQ 537
Cdd:PRK09493 76 rqeAGMVFQQFYLFPHLTAlENVMFGplrvRG------ASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 615
Cdd:PRK09493 142 QQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQ 221
|
...
gi 9961250 616 ELM 618
Cdd:PRK09493 222 VLI 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1034-1269 |
3.16e-33 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 132.19 E-value: 3.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVFVDFGFQLLDGQEAK-KLNV 1112
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRII-------AGLETPDSGRIVLNGRDLFtNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QwlRAQLGIVSQEPILF-DCSIAENIAYGDNSRVVSQDEIvsAAKAA------NIHPFIETLPHkyetrvgdkgtQLSGG 1185
Cdd:COG1118 73 R--ERRVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEI--RARVEellelvQLEGLADRYPS-----------QLSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1186 QKQRIAIARALIRQPQILLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVFQNG 1255
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQG 210
|
250
....*....|....
gi 9961250 1256 RVKEHGTHQQLLAQ 1269
Cdd:COG1118 211 RIEQVGTPDEVYDR 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
395-612 |
3.38e-33 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 126.78 E-value: 3.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:cd03214 1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 475 VSQepvlfsttiaenicygrgnvtmdeikkAVKEANAYEFIMKLpqkFDTLvgergaqlSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03214 78 VPQ---------------------------ALELLGLAHLADRP---FNEL--------SGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 555 LLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 612
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1034-1268 |
4.36e-33 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 128.57 E-value: 4.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAnvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfqllDGQEAKKLNVQ 1113
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFI-------DGEDIREQDPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILF-DCSIAENIAYGDNSRVVSQDEIvsAAKAANIHPFIETLPHKYETRVGDkgtQLSGGQKQRIAI 1192
Cdd:cd03295 72 ELRRKIGYVIQQIGLFpHMTVEENIALVPKLLKWPKEKI--RERADELLALVGLDPAEFADRYPH---ELSGGQQQRVGV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1193 ARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1051-1257 |
6.41e-33 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 127.26 E-value: 6.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDgqeaKKLNVQWLRAQLGIVSQEPILF- 1129
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID-GLKLTD----DKKNINELRQKVGMVFQQFNLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGD-NSRVVSQDEIVSAAKaanihpfietlphKYETRVG--DKGT----QLSGGQKQRIAIARALIRQPQI 1202
Cdd:cd03262 90 HLTVLENITLAPiKVKGMSKAEAEERAL-------------ELLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1203 LLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:cd03262 157 MLFDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
411-617 |
1.07e-32 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.94 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI---RNFN-----VNYLREIIGVVSQEPVLF 482
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 483 S-TTIAENICygRGNVTMDEIKKAVKEANAYEFIMKLpqkfdTLVGERGA---QLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK11264 98 PhRTVLENII--EGPVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 559 ATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK11264 171 PTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1034-1261 |
1.23e-32 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 126.71 E-value: 1.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLN-- 1111
Cdd:COG2884 2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVN-------GQDLSRLKrr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 -VQWLRAQLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSQDEIVSAAKAAnihpfIET--LPHKYETRVGdkgtQL 1182
Cdd:COG2884 73 eIPYLRRRIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREV-----LDLvgLSDKAKALPH----EL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1183 SGGQKQRIAIARALIRQPQILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVFQNGRVKE 1259
Cdd:COG2884 139 SGGEQQRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
..
gi 9961250 1260 HG 1261
Cdd:COG2884 218 DE 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
394-617 |
2.58e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.83 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-I 472
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFST-TIAENICYGR---GNVTMDEiKKAVKEANAyefIMK---LPQKFDTLVGErgaqLSGGQKQRIAIAR 545
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGReprRGGLIDW-RAMRRRARE---LLArlgLDIDPDTPVGD----LSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 546 ALVRNPKILLLDEATSALdteSEAEVQAALD-----KAReGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG1129 154 ALSRDARVLILDEPTASL---TEREVERLFRiirrlKAQ-GVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
394-618 |
3.72e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 125.24 E-value: 3.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNY-LREII 472
Cdd:cd03224 1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFST-TIAENICYGRGNVTMDEIKKAVKEAnaYEFIMKLPQKFDTLVGergaQLSGGQKQRIAIARALVRNP 551
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVI----AHRLSTVrnADVIAGFEDGVIVEQGSHSELM 618
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELL 220
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
394-617 |
1.07e-31 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 124.89 E-value: 1.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD--PD---EGTINIDGQDIRNFNVNY- 467
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 468 -LREIIGVVSQEPVLFSTTIAENICYG------RGNVTMDE-IKKAVKEANAYEFIMKlpQKFDTLVGergaqLSGGQKQ 539
Cdd:PRK14239 83 dLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
412-617 |
1.91e-31 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 123.99 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIGVVSQEPVLFS-TTIAENI 490
Cdd:cd03296 18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 491 CYG------RGNVTMDEIKKAVKEanayefIMKLPQkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:cd03296 96 AFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 565 TESEAEVQAALDKARE--GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03296 169 AKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
394-618 |
2.08e-31 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 130.57 E-value: 2.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN--------VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLyDPDEGTINIDGQDIRNFNV 465
Cdd:COG4172 276 LEARDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 NYLREI---IGVVSQEPvlFST-----TIAENICYG----RGNVTMDEIKKAVKEA-----------NAY--EFimklpq 520
Cdd:COG4172 355 RALRPLrrrMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRYphEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 521 kfdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEVQAA-LD-----KAREGRTTIVIAHRLSTV 594
Cdd:COG4172 427 -------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVV 489
|
250 260
....*....|....*....|....*
gi 9961250 595 RN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:COG4172 490 RAlAHRVMVMKDGKVVEQGPTEQVF 514
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
393-621 |
2.20e-31 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 123.33 E-value: 2.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 393 NLEFNDVHFSYPSRAnvkilKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVnYLREIi 472
Cdd:COG3840 1 MLRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFS-TTIAENICYG---RGNVTMDEiKKAVKEANA----YEFIMKLPqkfdtlvgergAQLSGGQKQRIAIA 544
Cdd:COG3840 74 SMLFQENNLFPhLTVAQNIGLGlrpGLKLTAEQ-RAQVEQALErvglAGLLDRLP-----------GQLSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1034-1266 |
3.40e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 126.34 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGfQLLDGQEAKKLNVq 1113
Cdd:COG3839 4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIG-G-RDVTDLPPKDRNI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wlraqlGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEI----VSAAKAANIHPFIETLPhkyetrvgdkgTQLSGGQKQ 1188
Cdd:COG3839 78 ------AMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIdrrvREAAELLGLEDLLDRKP-----------KQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1189 RIAIARALIRQPQILLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVFQNGRVK 1258
Cdd:COG3839 141 RVALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQ 213
|
....*...
gi 9961250 1259 EHGTHQQL 1266
Cdd:COG3839 214 QVGTPEEL 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
394-617 |
3.69e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 124.03 E-value: 3.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL--REI 471
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEP--VLFSTTIAENICYGRGNV--TMDEIKKAVKEA------NAYEfiMKLPQkfdtlvgergaQLSGGQKQRI 541
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavgmEGFE--NKPPH-----------HLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 542 AIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
410-619 |
4.23e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 124.39 E-value: 4.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--RNFNVNYLREIIGVVSQEP--VLFSTT 485
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEET 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 486 IAENICYGRGNVTM--DEIKKAVKEANAyefIMKLPqkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 563
Cdd:PRK13637 101 IEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 564 DTESEAEVQAALDKARE--GRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:PRK13637 176 DPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFK 234
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1051-1267 |
4.42e-31 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 122.44 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQwlRAQLGIVSQEPILF- 1129
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKI-------LLNGKDITNLPPE--KRDISYVPQNYALFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRVVSQDEIvsAAKAANIHPF--IETLPHKYETRvgdkgtqLSGGQKQRIAIARALIRQPQILLLDE 1207
Cdd:cd03299 85 HMTVYKNIAYGLKKRKVDKKEI--ERKVLEIAEMlgIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1208 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1267
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
712-968 |
7.17e-31 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 123.90 E-value: 7.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 712 VVGTVCAIAnggLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFfLQGFTFGKAGEILTRRLRSMA 791
Cdd:cd18780 6 LVSSGTNLA---LPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATF-LRSWLFTLAGERVVARLRKRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 792 FKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSG 871
Cdd:cd18780 82 FSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 872 IVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFS 951
Cdd:cd18780 160 VIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLA 239
|
250
....*....|....*..
gi 9961250 952 YAGCFRFGAYLIVNGHM 968
Cdd:cd18780 240 IVLVLWYGGRLVIDGEL 256
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1034-1257 |
7.68e-31 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 119.81 E-value: 7.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQ 1113
Cdd:cd03230 1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVL-------GKDIKKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wLRAQLGIVSQEPILF-DCSIAENIaygdnsrvvsqdeivsaakaanihpfietlphkyetrvgdkgtQLSGGQKQRIAI 1192
Cdd:cd03230 71 -VKRRIGYLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLAL 106
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1193 ARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:cd03230 107 AQALLHDPELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
394-600 |
8.50e-31 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 120.66 E-value: 8.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYlREIIG 473
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFST-TIAENIC-----YGRgNVTMDEIKKAVKEanayefiMKLPQKFDTLVGergaQLSGGQKQRIAIARAL 547
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRNADVI 600
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
398-589 |
1.06e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 120.44 E-value: 1.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 398 DVHFSYpsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqdiRNFNVNYLREIIGVVSQ 477
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 478 EP--VLFSTTIAENICYGRGNVTMD--EIKKAVKEANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961250 554 LLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH 589
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1052-1257 |
1.17e-30 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 120.86 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGQeaKKLNVQWLRAQLGIVSQEPIL 1128
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLN-GTVLFDSR--KKINLPPQQRKIGLVFQQYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1129 F-DCSIAENIAYG-----DNSRVVSQDEIVSAAkaaNIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQI 1202
Cdd:cd03297 87 FpHLNVRENLAFGlkrkrNREDRISVDELLDLL---GLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1203 LLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
394-617 |
1.24e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.53 E-value: 1.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPqkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1043-1269 |
1.32e-30 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 123.62 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1043 YPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA---GTVfvdfgfqLLDGQEAKKLNVQWLRA- 1117
Cdd:COG0444 11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEI-------LFDGEDLLKLSEKELRKi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1118 ---QLGIVSQEP---------ILFdcSIAENI-AYGDNSRVVSQDEIVSAAKAANIHPFIETL---PHkyetrvgdkgtQ 1181
Cdd:COG0444 84 rgrEIQMIFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPDPERRLdryPH-----------E 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1182 LSGGQKQRIAIARALIRQPQILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVFQN 1254
Cdd:COG0444 151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYA 226
|
250
....*....|....*
gi 9961250 1255 GRVKEHGTHQQLLAQ 1269
Cdd:COG0444 227 GRIVEEGPVEELFEN 241
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1034-1257 |
1.32e-30 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 121.52 E-value: 1.32e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqLLDGQEAKKLNVQ 1113
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLID----GTDINKLKGKALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFD-CSIAENIAYGDNSRV---------VSQDEIVSAAKAanihpfIET--LPHKYETRVGdkgtQ 1181
Cdd:cd03256 75 QLRRQIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQRALAA------LERvgLLDKAYQRAD----Q 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1182 LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVFQNGRV 1257
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
394-617 |
1.41e-30 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 120.69 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFST-TIAENICY-----GRGNVTMDEikkavkEANAYEFIMKLPQKFDTLVGergaQLSGGQKQRIAIARAL 547
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1049-1269 |
1.85e-30 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 121.98 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQWLRA----QLGIVSQ 1124
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID-------GQDIAAMSRKELRElrrkKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 EPILF-DCSIAENIAYGDNSRVVSQDEIVSAA----KAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQ 1199
Cdd:cd03294 110 SFALLpHRTVLENVAFGLEVQGVPRAEREERAaealELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1200 PQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:cd03294 179 PDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1048-1266 |
2.01e-30 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 120.42 E-value: 2.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAkkLNVQWLRAQLGIVSQEPI 1127
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI-------LLDGKDI--TNLPPHKRPVNTVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:cd03300 83 LFpHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1207 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1266
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1045-1251 |
2.14e-30 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 119.51 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWlRAQLGIVSQ 1124
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEV-------LWNGEPIRDAREDY-RRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 EPILF-DCSIAENIA-----YGdnsRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIR 1198
Cdd:COG4133 83 ADGLKpELTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLS 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1199 QPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1251
Cdd:COG4133 149 PAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
85-331 |
2.28e-30 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 122.24 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 85 FVDTAGNFSFPVNF--SLSLLNPGKILEEEMTRYAYYYSGLGAGVLV----AAYIQVSFWTLAAGRQIRKIRQKFFHAIL 158
Cdd:cd18573 6 LVSSAVTMSVPFAIgkLIDVASKESGDIEIFGLSLKTFALALLGVFVvgaaANFGRVYLLRIAGERIVARLRKRLFKSIL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 159 RQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKIL 238
Cdd:cd18573 86 RQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 239 SAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWY 318
Cdd:cd18573 166 RKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYY 245
|
250
....*....|...
gi 9961250 319 GSTLVISKEYTIG 331
Cdd:cd18573 246 GGSLVASGELTVG 258
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1034-1269 |
3.17e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.58 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLnvq 1113
Cdd:COG1121 7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLF-------GKPPRRA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wlRAQLGIVSQE-------PIlfdcSIAENIAYGDNSRV-------VSQDEIVSAA-KAANIHPFIETlphkyetRVGdk 1178
Cdd:COG1121 74 --RRRIGYVPQRaevdwdfPI----TVRDVVLMGRYGRRglfrrpsRADREAVDEAlERVGLEDLADR-------PIG-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1179 gtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFqNGR 1256
Cdd:COG1121 139 --ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRG 215
|
250
....*....|...
gi 9961250 1257 VKEHGTHQQLLAQ 1269
Cdd:COG1121 216 LVAHGPPEEVLTP 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
410-1277 |
3.82e-30 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 130.28 E-value: 3.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTInidgqdirnfnvnYLREIIGVVSQEPVLFSTTIAEN 489
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 490 ICYgrgnvtMDE-----IKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:PTZ00243 741 ILF------FDEedaarLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 565 TE-SEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKEgVYFKL-----VNMQTSGSQIQ 638
Cdd:PTZ00243 815 AHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLaaelkENKDSKEGDAD 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 639 SEEFELNDEKAATRMaPNGWKSRLFRHSTQKNLKNSQMCQKSLDVETDGLEANVPPVSFLKVLKLnktewpyfvVGTVCA 718
Cdd:PTZ00243 894 AEVAEVDAAPGGAVD-HEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRF---------CGGLHA 963
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 719 IanGGLQPAFSVifSEIIAI-------------FGPGDDavkqqkcnIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTR 785
Cdd:PTZ00243 964 A--GFVLATFAV--TELVTVssgvwlsmwstrsFKLSAA--------TYLYVYLGIVLLGTFSVPLRFFLSYEAMRRGSR 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 786 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFiygWQLTLLLLAVVP 865
Cdd:PTZ00243 1032 NMHRDLLRSVSRGTMSFFD--TTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTS---ASQPFVLVALVP 1106
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 866 IiavsGIVEMKLLA--GNAKRDKKELEAAGK-----IATEAIENIRTVVSltqerkfesmyveklYGPYRNSVQKA-HIY 937
Cdd:PTZ00243 1107 C----GYLYYRLMQfyNSANREIRRIKSVAKspvftLLEEALQGSATITA---------------YGKAHLVMQEAlRRL 1167
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 938 GITFSISqafmyfsyagcfrfgayLIVNGHMRFRDVILVF-SAIVFGAVAL-------GHASSfaPDYAKAKLSAAHLFM 1009
Cdd:PTZ00243 1168 DVVYSCS-----------------YLENVANRWLGVRVEFlSNIVVTVIALigvigtmLRATS--QEIGLVSLSLTMAMQ 1228
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1010 LFE------RQ--------------------------PLIDSY-----SEEGLKPDKF-------------------EGN 1033
Cdd:PTZ00243 1229 TTAtlnwlvRQvatveadmnsverllyytdevphedmPELDEEvdaleRRTGMAADVTgtvviepasptsaaphpvqAGS 1308
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptRANVP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNV 1112
Cdd:PTZ00243 1309 LVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVN-------GREIGAYGL 1379
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWLRAQLGIVSQEPILFDCSIAENIaygDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAI 1192
Cdd:PTZ00243 1380 RELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCM 1456
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1193 ARALI-RQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL-LAQK 1270
Cdd:PTZ00243 1457 ARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQ 1536
|
....*..
gi 9961250 1271 GIYFSMV 1277
Cdd:PTZ00243 1537 SIFHSMV 1543
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
756-968 |
5.40e-30 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 121.11 E-value: 5.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 756 LIFLFLGIIS-FFTFfLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLAL 834
Cdd:cd18572 40 LLLLLLSVLSgLFSG-LRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATK--TGELTSRLTSDCQKVSDPLSTNLNV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 835 IAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERK 914
Cdd:cd18572 117 FLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEER 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 915 FESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18572 197 EARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
394-617 |
1.02e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 120.20 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPqkfdtlvgergAQLSGGQKQRIAIAR 545
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1034-1269 |
1.12e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.84 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQ 1113
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID-------GDLLTEENVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPhkyetrvgdkgTQLSGGQK 1187
Cdd:PRK13650 78 DIRHKIGMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQ 1265
Cdd:PRK13650 147 QRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRE 226
|
....
gi 9961250 1266 LLAQ 1269
Cdd:PRK13650 227 LFSR 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1049-1257 |
1.21e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 124.75 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQwlRAQ-LGI--VSQE 1125
Cdd:COG1129 17 VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIL-------LDGEPVRFRSPR--DAQaAGIaiIHQE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILF-DCSIAENIAYGD---NSRVVSQDEIVSAAKAA------NIHPfietlphkyETRVGDkgtqLSGGQKQRIAIARA 1195
Cdd:COG1129 88 LNLVpNLSVAENIFLGReprRGGLIDWRAMRRRARELlarlglDIDP---------DTPVGD----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1196 LIRQPQILLLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:COG1129 155 LSRDARVLILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1045-1266 |
1.48e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 120.99 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLN---VQWLRAQLGI 1121
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEI-------LFDGQDITGLSgreLRPLRRRMQM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 VSQEPilFDC-----SIAENIAYG-DNSRVVSQDEIvsAAKAANI-------HPFIETLPHkyetrvgdkgtQLSGGQKQ 1188
Cdd:COG4608 100 VFQDP--YASlnprmTVGDIIAEPlRIHGLASKAER--RERVAELlelvglrPEHADRYPH-----------EFSGGQRQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1189 RIAIARALIRQPQILLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKE 1259
Cdd:COG4608 165 RIGIARALALNPKLIVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVE 238
|
....*..
gi 9961250 1260 HGTHQQL 1266
Cdd:COG4608 239 IAPRDEL 245
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
394-609 |
1.52e-29 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 115.60 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPsraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-I 472
Cdd:cd03216 1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQepvlfsttiaenicygrgnvtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPK 552
Cdd:cd03216 78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 553 ILLLDEATSALdteSEAEVQAALD----KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIV 609
Cdd:cd03216 103 LLILDEPTAAL---TPAEVERLFKvirrLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
394-604 |
2.03e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 118.60 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD-----EGTINIDGQDI--RNFNVN 466
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 467 YLREIIGVVSQEPVLFSTTIAENICYG------RGNVTMDEI-KKAVKEANAYEFIMKLPQKfdtlvgeRGAQLSGGQKQ 539
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFE 604
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFK 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
394-621 |
2.04e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.13 E-value: 2.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDE---GTINIDGQDIRNFNVNYLRE 470
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEANA----YEFIMKLPQkfdtlvgergaQLSGGQKQRIA 542
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEPA-----------NLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
.
gi 9961250 621 E 621
Cdd:PRK13640 234 V 234
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1041-1278 |
2.99e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 118.68 E-value: 2.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1041 FNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQWLRAQ 1118
Cdd:PRK13647 12 FRYKdgTKA----LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVM-------GREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1119 LGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVS----AAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAI 1192
Cdd:PRK13647 81 VGLVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERrveeALKAVRMWDFRDKPPY-----------HLSYGQKKRVAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1193 ARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG-----THQQ 1265
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDED 229
|
250
....*....|...
gi 9961250 1266 LLAQKGIYFSMVS 1278
Cdd:PRK13647 230 IVEQAGLRLPLVA 242
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
752-968 |
3.26e-29 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 119.16 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTR 831
Cdd:cd18573 41 KTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 832 LALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQ 911
Cdd:cd18573 119 LSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAA 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 912 ERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18573 199 ERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGEL 255
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1045-1269 |
4.67e-29 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 123.64 E-value: 4.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPLAGTVFvdFGFQLLDGQEAKKLnvQWLRAQLGIVSQ 1124
Cdd:COG4172 295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIR--FDGQDLDGLSRRAL--RPLRRRMQVVFQ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 EPilFDC-----SIAENIAYG------DNSRVVSQDEIVSAAKAANIHPfiETL---PHkyetrvgdkgtQLSGGQKQRI 1190
Cdd:COG4172 370 DP--FGSlsprmTVGQIIAEGlrvhgpGLSAAERRARVAEALEEVGLDP--AARhryPH-----------EFSGGQRQRI 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1191 AIARALIRQPQILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTH 1263
Cdd:COG4172 435 AIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPT 510
|
....*.
gi 9961250 1264 QQLLAQ 1269
Cdd:COG4172 511 EQVFDA 516
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1039-1261 |
5.56e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 114.84 E-value: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1039 VVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQ 1118
Cdd:cd03214 5 LSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEI-------LLDGKDLASLSPKELARK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1119 LGIVSQepilfdcsiaeniaygdnsrvvsqdeivsAAKAANIHPFIetlphkyetrvgDKG-TQLSGGQKQRIAIARALI 1197
Cdd:cd03214 75 IAYVPQ-----------------------------ALELLGLAHLA------------DRPfNELSGGERQRVLLARALA 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1198 RQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1261
Cdd:cd03214 114 QEPPILLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1036-1261 |
5.70e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 115.71 E-value: 5.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1036 FNEVVFNYPtraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLnvqwl 1115
Cdd:cd03235 2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVF-------GKPLEKE----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1116 RAQLGIVSQEPIL---FDCSIAENIAYGDNSRVVSQdEIVSAAKAANIHPFIET--LPHKYETRVGdkgtQLSGGQKQRI 1190
Cdd:cd03235 67 RKRIGYVPQRRSIdrdFPISVRDVVLMGLYGHKGLF-RRLSKADKAKVDEALERvgLSELADRQIG----ELSGGQQQRV 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1191 AIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFqNGRVKEHG 1261
Cdd:cd03235 142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1048-1266 |
5.75e-29 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 116.67 E-value: 5.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQwlRAQLGIVSQEPI 1127
Cdd:cd03296 14 DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIL-------FGGEDATDVPVQ--ERNVGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIAYG----DNSRVVSQDEIvsAAKAANIHPFI--ETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQP 1200
Cdd:cd03296 85 LFrHMTVFDNVAFGlrvkPRSERPPEAEI--RAKVHELLKLVqlDWLADRYPA-------QLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1201 QILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1266
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
394-623 |
5.89e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 116.62 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPsraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylrEI-- 471
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH---RIar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 --IGVVSQEPVLFST-TIAENI---CYGRGNvtmdeiKKAVKEAnaYEFIMKLpqkFDTLvGER----GAQLSGGQKQRI 541
Cdd:COG0410 78 lgIGYVPEGRRIFPSlTVEENLllgAYARRD------RAEVRAD--LERVYEL---FPRL-KERrrqrAGTLSGGEQQML 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 542 AIARALVRNPKILLLDEATSALdteseA-----EVQAALDKAREGRTTIVI----AHRLSTVrnADVIAGFEDGVIVEQG 612
Cdd:COG0410 146 AIGRALMSRPKLLLLDEPSLGL-----ApliveEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEG 218
|
250
....*....|.
gi 9961250 613 SHSELMKKEGV 623
Cdd:COG0410 219 TAAELLADPEV 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1021-1285 |
6.22e-29 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 126.21 E-value: 6.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1021 SEEGLKPDKFE--------GN-ITFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG 1091
Cdd:TIGR00957 615 SHEELEPDSIErrtikpgeGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1092 TVFvdfgfqlldgqeakklnvqwLRAQLGIVSQEPILFDCSIAENIAYGdnsRVVSQDEIVSAAKAANIHPFIETLPHKY 1171
Cdd:TIGR00957 694 HVH--------------------MKGSVAYVPQQAWIQNDSLRENILFG---KALNEKYYQQVLEACALLPDLEILPSGD 750
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1172 ETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADL 1248
Cdd:TIGR00957 751 RTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDV 830
|
250 260 270
....*....|....*....|....*....|....*..
gi 9961250 1249 IVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGTQN 1285
Cdd:TIGR00957 831 IIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
394-623 |
6.59e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 117.53 E-value: 6.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIAR 545
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEGV 623
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1050-1262 |
7.51e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.05 E-value: 7.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQwlRAQLGIVSQEPILF 1129
Cdd:PRK09452 28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM-------LDGQDITHVPAE--NRHVNTVFQSYALF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 -DCSIAENIAYGDNSRVVSQDEIVS----AAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILL 1204
Cdd:PRK09452 99 pHMTVFENVAFGLRMQKTPAAEITPrvmeALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1205 LDEATSALDTESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHGT 1262
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1034-1262 |
8.16e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.14 E-value: 8.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAN-VPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPLAGTVFVDfgfqlldGQEAKK 1109
Cdd:PRK11153 2 IELKNISKVFPQGGRtIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVD-------GQDLTA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 LNVQWLRA---QLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSQDEIvsaakAANIHPFIEtlphkyetRVG--DK 1178
Cdd:PRK11153 72 LSEKELRKarrQIGMIFQHfNLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1179 G----TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVV 1251
Cdd:PRK11153 134 AdrypAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAV 213
|
250
....*....|.
gi 9961250 1252 FQNGRVKEHGT 1262
Cdd:PRK11153 214 IDAGRLVEQGT 224
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
394-621 |
1.09e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 116.77 E-value: 1.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVKiLKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13648 8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIAR 545
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
714-986 |
1.18e-28 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 117.20 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 714 GTVCAIANGGLQPAFSVIFSEII-AIFGPGDDAvkqqkcNIFSLIFLFLGII---SFFTFFlQGFTFGKAGEILTRRLRS 789
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIdAALGGGDTA------SLNQIALLLLGLFllqAVFSFF-RIYLFARVGERVVADLRK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 790 MAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAV 869
Cdd:cd18576 74 DLYRHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 870 SGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERkFESM-YVEKLYGPYRNSVQKAHIYGITFSISQAFM 948
Cdd:cd18576 152 VAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 9961250 949 YFSYAGCFRFGAYLIVNGHMRFRDVI--LVFSAIVFGAVA 986
Cdd:cd18576 231 FGAIVAVLWYGGRLVLAGELTAGDLVafLLYTLFIAGSIG 270
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
394-621 |
2.26e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 115.18 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEG-TINIDGQDIRNFNVNYLREII 472
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVS---QEPVLFSTTIAENICYGR-------GNVTMDEIKKAVKEANAYEFimklpqkfDTLVGERGAQLSGGQKQRIA 542
Cdd:COG1119 81 GLVSpalQLRFPRDETVLDVVLSGFfdsiglyREPTDEQRERARELLELLGL--------AHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStvrnaDVIAGF------EDGVIVEQGSH 614
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIthvlllKDGRVVAAGPK 227
|
....*..
gi 9961250 615 SELMKKE 621
Cdd:COG1119 228 EEVLTSE 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
410-618 |
2.50e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 115.45 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIR-------------NFNVNYLREIIGVVS 476
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 477 QEPVLFS-TTIAENICygRGNVTMDEIKKAVKEANAYEFIMKLPQKfDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 555
Cdd:PRK10619 99 QHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 556 LDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNADVIAGF-EDGVIVEQGSHSELM 618
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
394-610 |
2.97e-28 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 114.45 E-value: 2.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL---- 468
Cdd:COG4181 9 IELRGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 469 REIIGVVSQ-EPVLFSTTIAENicygrgnVTM--------DEIKKAVKEANAYEfimklpqkfdtlVGERG----AQLSG 535
Cdd:COG4181 89 ARHVGFVFQsFQLLPTLTALEN-------VMLplelagrrDARARARALLERVG------------LGHRLdhypAQLSG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 536 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA-HRLSTVRNADVIAGFEDGVIVE 610
Cdd:COG4181 150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
125-364 |
3.49e-28 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 115.66 E-value: 3.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 125 AGVLVA----AYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVA 200
Cdd:cd18576 43 LGLFLLqavfSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 201 TFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQ 280
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 281 KHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMT-VFFSILIGAfSVGQAAPCIDAFAN 359
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQK 281
|
....*
gi 9961250 360 ARGAA 364
Cdd:cd18576 282 ALGAS 286
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1049-1268 |
4.41e-28 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 113.68 E-value: 4.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQwLRAQLGI--VSQEP 1126
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI-------RFDGRDITGLPPH-ERARAGIgyVPEGR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILF-DCSIAENIaygdnsrvvsqdeiVSAAKAANIHPFIETLPHKYE------TRVGDKGTQLSGGQKQRIAIARALIRQ 1199
Cdd:cd03224 85 RIFpELTVEENL--------------LLGAYARRRAKRKARLERVYElfprlkERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1200 PQILLLDEATSALdteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVFQNGRVKEHGTHQQLLA 1268
Cdd:cd03224 151 PKLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-591 |
4.87e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 114.80 E-value: 4.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVH--FsYPSRAN-VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfnVNYLRE 470
Cdd:COG1101 2 LELKNLSktF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-----VTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 -----IIGVVSQEPVL---FSTTIAEN--ICYGRGN-------VT---MDEIKKAVKEANayefiMKLPQKFDTLVGerg 530
Cdd:COG1101 76 ykrakYIGRVFQDPMMgtaPSMTIEENlaLAYRRGKrrglrrgLTkkrRELFRELLATLG-----LGLENRLDTKVG--- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 531 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRL 591
Cdd:COG1101 148 -LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
394-609 |
4.95e-28 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 121.37 E-value: 4.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPS-RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL---- 468
Cdd:PRK10535 5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 469 REIIGVVSQEPVLFSTTIAENicygrgNVTMDEI----KKAVKEANAYEFIMKLpqKFDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PRK10535 85 REHFGFIFQRYHLLSHLTAAQ------NVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFEDGVIV 609
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1034-1267 |
6.81e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.36 E-value: 6.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpLAGTVFVDFGFQLLdGQE--AKKLN 1111
Cdd:PRK14258 8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFF-NQNiyERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 VQWLRAQLGIVSQEPILFDCSIAENIAYGDN----SRVVSQDEIV-SAAKAANIHPFIETLPHKyetrvgdKGTQLSGGQ 1186
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVeSALKDADLWDEIKHKIHK-------SALDLSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1187 KQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQN-----GRVK 1258
Cdd:PRK14258 156 QQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLV 235
|
....*....
gi 9961250 1259 EHGTHQQLL 1267
Cdd:PRK14258 236 EFGLTKKIF 244
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1047-1255 |
7.27e-28 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 112.81 E-value: 7.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1047 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfQLLDGQEAKKLNVQWLRAQLGIVSQEP 1126
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWS---NKNESEPSFEATRSRNRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILFDCSIAENIAYGDNsrvVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:cd03290 89 WLLNATVEENITFGSP---FNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1207 EATSALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNG 1255
Cdd:cd03290 166 DPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1034-1237 |
1.20e-27 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 112.12 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLN-- 1111
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN-------GQDVSDLRgr 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 -VQWLRAQLGIVSQE-PILFDCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIETLPHKYETRvgDKGTQLSGGQKQR 1189
Cdd:cd03292 72 aIPYLRRKIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAA-----LELVGLSHKHR--ALPAELSGGEQQR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961250 1190 IAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA 1237
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
393-615 |
1.60e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 112.41 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 393 NLEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrNFN-------V 465
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSqkpsekaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 NYLREIIGVVSQE----PVLfstTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLvgerGAQLSGGQKQRI 541
Cdd:COG4161 78 RLLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 542 AIARALVRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 615
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQvVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
267-590 |
1.76e-27 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 119.14 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 267 IAF-GGQNKELERYQKHLENAKEIgIKKAISANISMGiAFLLIYASYALAFWY--GSTLVISKEYTIGNAMTV--FFSIL 341
Cdd:COG4178 234 IALyRGEAAERRRLRRRFDAVIAN-WRRLIRRQRNLT-FFTTGYGQLAVIFPIlvAAPRYFAGEITLGGLMQAasAFGQV 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 342 IGAFSVgqaapCIDAFAN-ARGAAYVI-----FDIIDNNPKIDSFSERGHKPDSikGNLEFNDVHFSYPSRAnvKILKGL 415
Cdd:COG4178 312 QGALSW-----FVDNYQSlAEWRATVDrlagfEEALEAADALPEAASRIETSED--GALALEDLTLRTPDGR--PLLEDL 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 416 NLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINI-DGQDIrnfnvnyLreiigVVSQEPVLFSTTIAENICY-- 492
Cdd:COG4178 383 SLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-----FLPQRPYLPLGTLREALLYpa 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 493 GRGNVTMDEIKKAVKEANayefIMKLPQKFDTlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQ 572
Cdd:COG4178 451 TAEAFSDAELREALEAVG----LGHLAERLDE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALY 525
|
330
....*....|....*...
gi 9961250 573 AALDKAREGRTTIVIAHR 590
Cdd:COG4178 526 QLLREELPGTTVISVGHR 543
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
394-620 |
2.00e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 113.72 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRA--NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN-YLRE 470
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 I---IGVVSQ--EPVLFSTTIAENICYGRGNVTMDeikkaVKEANAYEFIMKLPQKFDTLVGERGA-QLSGGQKQRIAIA 544
Cdd:PRK13646 83 VrkrIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-----LDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKAR--EGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1048-1261 |
2.55e-27 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 111.19 E-value: 2.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfGFQLLDGQEAKKLNVqwlraqlGIVSQEPI 1127
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYI--GGRDVTDLPPKDRDI-------AMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIAYGDNSRVVSQDEIV----SAAKAANIhpfiETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQI 1202
Cdd:cd03301 83 LYpHMTVYDNIAFGLKLRKVPKDEIDervrEVAELLQI----EHLLDRKPK-------QLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1203 LLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHG 1261
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1052-1262 |
2.98e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.22 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDgqeaKKLNVQWLRAQLGIVSQEP--ILF 1129
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-GVDITD----KKVKLSDIRKKVGLVFQYPeyQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIETLPHKYETrVGDKGT-QLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:PRK13637 98 EETIEKDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1209 TSALDTeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1262
Cdd:PRK13637 172 TAGLDP---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
394-612 |
4.35e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 109.56 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHF---SYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI--QRLYDPDEGTINIDGQDIRNFNvnyL 468
Cdd:cd03213 4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 469 REIIGVVSQEPVLFST-TIAENIcygrgnvtmdeikkavkeanayEFIMKLpqkfdtlvgeRGaqLSGGQKQRIAIARAL 547
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTvrnaDVIAGFEDGVIVEQG 612
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQG 188
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
415-620 |
4.76e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 4.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 415 LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYlREIIgVVSQEPVLFS-TTIAENICYG 493
Cdd:PRK11432 25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RDIC-MVFQSYALFPhMSLGENVGYG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 494 RG--NVTMDEIKKAVKEANAyefIMKLPQKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAEV 571
Cdd:PRK11432 103 LKmlGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALILKPKVLLFDEPLSNLD----ANL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 572 QAAL-DKARE-----GRTTIVIAHRLS---TVrnADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:PRK11432 172 RRSMrEKIRElqqqfNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
394-617 |
5.72e-27 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 117.09 E-value: 5.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD----EGTINIDGQDIRNFNVNYL 468
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVeAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 469 REI----IGVVSQEPV-----LFS--TTIAENIcygrgnvtmdEIKKAVKEANAYEFIMKLPQkfdtLVGERGA------ 531
Cdd:COG4172 87 RRIrgnrIAMIFQEPMtslnpLHTigKQIAEVL----------RLHRGLSGAAARARALELLE----RVGIPDPerrlda 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 532 ---QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFED 605
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITHDLGVVRRfADRVAVMRQ 232
|
250
....*....|..
gi 9961250 606 GVIVEQGSHSEL 617
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1048-1257 |
5.92e-27 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 108.28 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQwlRAQ-LGIvsqep 1126
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-------GKEVSFASPR--DARrAGI----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ilfdcsiaeniaygdnsrvvsqdeivsaakaANIHpfietlphkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:cd03216 78 -------------------------------AMVY-------------------QLSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1207 EATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:cd03216 108 EPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
409-623 |
5.99e-27 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 110.60 E-value: 5.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylrEI----IGVVSQEPVLFST 484
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIarlgIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 485 -TIAENI-----CYGRGNVTMDEIKKAVKEAN--AYEFI--MKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03219 90 lTVLENVmvaaqARTGSGLLLARARREEREARerAEELLerVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 555 LLDEATSALdteSEAEVQAALDK----AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEGV 623
Cdd:cd03219 166 LLDEPAAGL---NPEETEELAELirelRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1051-1268 |
7.58e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 111.00 E-value: 7.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfGFQLLDGQE---AKKLNVQWLRAQLGIVSQEPI 1127
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--GDITIDTARslsQQKGLIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LFDC-SIAENIAYGDnsrVVSQDEIVSAAKAanihpfietLPHKYETRVGDKGTQ------LSGGQKQRIAIARALIRQP 1200
Cdd:PRK11264 96 LFPHrTVLENIIEGP---VIVKGEPKEEATA---------RARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1201 QILLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:PRK11264 164 EVILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
387-623 |
8.32e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.86 E-value: 8.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 387 PDSIkgnLEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ--DIRNFN 464
Cdd:PRK13636 2 EDYI---LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 465 VNYLREIIGVVSQEP--VLFSTTIAENICYGRGNVTM--DEIKKAVKEANAYEFIMKLPQKfdtlvgeRGAQLSGGQKQR 540
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 541 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIA-HRLSTVR-NADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
....*.
gi 9961250 618 MKKEGV 623
Cdd:PRK13636 230 FAEKEM 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1034-1267 |
8.97e-27 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 110.18 E-value: 8.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGqeakKLNVQ 1113
Cdd:PRK09493 2 IEFKNVSKHF---GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD-GLKVNDP----KVDER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFDCSIA-ENIAYGDNSrvvsqdeiVSAAKAANIHPFIETLPHK--YETRVGDKGTQLSGGQKQRI 1190
Cdd:PRK09493 74 LIRQEAGMVFQQFYLFPHLTAlENVMFGPLR--------VRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1191 AIARALIRQPQILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVF-QNGRVKEHGTHQQLL 1267
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFiDKGRIAEDGDPQVLI 224
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
411-610 |
9.90e-27 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 110.93 E-value: 9.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN---VNYLREIIGVVSQEPV------- 480
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSIsavnprk 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 481 LFSTTIAENIcygRGNVTMDEikkAVKEANAYEFI--MKLPqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK10419 107 TVREIIREPL---RHLLSLDK---AERLARASEMLraVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 559 ATSALDTESEAEVQAALDKAREGRTT--IVIAHRLSTV-RNADVIAGFEDGVIVE 610
Cdd:PRK10419 178 AVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1051-1262 |
1.02e-26 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 109.83 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQwLRAQLGIVS--QEPIL 1128
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-------LFDGEDITGLPPH-EIARLGIGRtfQIPRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1129 F-DCSIAENIA--------YGDNSRVVSQDEIVSAAKAANIhpfIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALI 1197
Cdd:cd03219 87 FpELTVLENVMvaaqartgSGLLLARARREEREARERAEEL---LERvgLADLADRPAGE----LSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1198 RQPQILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1262
Cdd:cd03219 160 TDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1034-1268 |
1.14e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 111.23 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfQLLDGQEAKKLnvQ 1113
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV----SGIDTGDFSKL--Q 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpFIETLPHKYETRvgdKGTQLSGGQKQRIA 1191
Cdd:PRK13644 74 GIRKLVGIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1192 IARALIRQPQILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
394-620 |
1.17e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANV--KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI----RNFNVNY 467
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 468 LREIIGVVSQ--EPVLFSTTIAENICYGRGN--VTMDEIKKAVKEANAY-----EFIMKLPqkFDtlvgergaqLSGGQK 538
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIELvglpeELLARSP--FE---------LSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 539 QRIAIARALVRNPKILLLDEATSALDTESEAEVQ---AALDKaREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSH 614
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
....*.
gi 9961250 615 SELMKK 620
Cdd:PRK13634 231 REIFAD 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
394-612 |
1.19e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 109.12 E-value: 1.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkilKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIG 473
Cdd:cd03298 1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFS-TTIAENICYGRG------NVTMDEIKKAVKEANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIARA 546
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSpglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1052-1269 |
1.24e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 110.64 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGtvFVDFGFQLLDGQE--AKKLNVQWLRAQLGIVSQEPILF 1129
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG--FRVEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGD--NSRVVSQDEIV--SAAKAAnihpfietLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLL 1205
Cdd:PRK14243 104 PKSIYDNIAYGAriNGYKGDMDELVerSLRQAA--------LWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1206 DEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
408-617 |
1.36e-26 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 110.00 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 408 NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD--PD---EGTINIDGQDIRNFNVNYLREIIGVVSQEPVLF 482
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 483 ST-TIAENICYG----RGNVTMDEIKKAVKEAnayefiMKLPQKFDTL---VGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:PRK14247 95 PNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 555 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
394-612 |
1.42e-26 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 108.82 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTvALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAEN----ICYGRGnVTMDEIKKAVKEAnayefiMKLPQKFDTLvGERGAQLSGGQKQRIAIARALVR 549
Cdd:cd03264 76 YLPQEFGVYPNFTVREfldyIAWLKG-IPSKEVKARVDEV------LELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
406-611 |
1.52e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 110.28 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN----YLREIIGVVSQEPVL 481
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKqrraFRRDVQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 482 FS--TTIAENICYGRGNVTmdEIKKAVKEANAYEFI--MKLPqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:TIGR02769 101 VNprMTVRQIIGEPLRHLT--SLDESEQKARIAELLdmVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 558 EATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQ 611
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
394-564 |
1.74e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.03 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFSTTIAENICYGRgnvtmdEIKKAVKEANAY-EFIMK--LPqkfDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
|
170
....*....|....
gi 9961250 551 PKILLLDEATSALD 564
Cdd:PRK10247 156 PKVLLLDEITSALD 169
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
394-589 |
1.85e-26 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.95 E-value: 1.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYP-SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylReii 472
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFS-TTIAENICYG---RGnvtmdeIKKAVKEANAYEFImklpqkfdTLVGERGA------QLSGGQKQRIA 542
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAFGlrlRG------VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVG 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
426-618 |
2.28e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 112.12 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 426 ALVGSSGCGKSTTVQLIQRLYDPDEGTINIDG---QDIRNfNVN---YLREIiGVVSQEPVLFST-TIAENICYGRgnvt 498
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSAR-GIFlppHRRRI-GYVFQEARLFPHlSVRGNLLYGR---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 499 mdeiKKAVKEANAYEFimklpqkfDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 569
Cdd:COG4148 103 ----KRAPRAERRISF--------DEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 570 EVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGSHSELM 618
Cdd:COG4148 171 EILPYLERlRDELDIPILyVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
394-622 |
2.36e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 110.18 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVK---ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF-NVNYLR 469
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 470 EIIGVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEA----NAYEFIMKLPQkfdtlvgergaQLSGGQKQRI 541
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 542 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQG------S 613
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGtpkeifK 233
|
....*....
gi 9961250 614 HSELMKKEG 622
Cdd:PRK13633 234 EVEMMKKIG 242
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
407-621 |
2.76e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 109.33 E-value: 2.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 407 ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVL-FSTT 485
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 486 IAENICYGR-------GNVTMDEiKKAVKEAnayefiMKLPQkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK11231 93 VRELVAYGRspwlslwGRLSAED-NARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 559 ATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1051-1258 |
2.99e-26 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 107.73 E-value: 2.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldgqeAKKLNVQWLRAQLGIVSQEP--IL 1128
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLN----------GKPIKAKERRKSIGYVMQDVdyQL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1129 FDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:cd03226 85 FTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLIFDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1209 TSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK 1258
Cdd:cd03226 154 TSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
394-619 |
3.22e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 109.92 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYP--SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIR----NFNVNY 467
Cdd:PRK13641 3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 468 LREIIGVVSQ--EPVLFSTTIAENICYGRGN--VTMDEIKKAvkeanAYEFIMKLPQKfDTLVGERGAQLSGGQKQRIAI 543
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEK-----ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 544 ARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHrlstvrNADVIAGFEDGVIVEQgsHSELMK 619
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVLE--HGKLIK 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1034-1269 |
4.01e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.79 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNY---PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKL 1110
Cdd:PRK13633 5 IKCKNVSYKYesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD-------GLDTSDE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1111 NVQW-LRAQLGIVSQEPilfDCSIA-----ENIAYGDNSRVVSQDEIVS----AAKAANIHPFIETLPHkyetrvgdkgt 1180
Cdd:PRK13633 78 ENLWdIRNKAGMVFQNP---DNQIVativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH----------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1181 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVK 1258
Cdd:PRK13633 144 LLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
|
250
....*....|.
gi 9961250 1259 EHGTHQQLLAQ 1269
Cdd:PRK13633 224 MEGTPKEIFKE 234
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1052-1269 |
4.22e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 111.35 E-value: 4.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPLAGTVFVDfGFQLLDGqeAKKLNVQWLRAQLGIVS 1123
Cdd:COG4148 11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLG-GEVLQDS--ARGIFLPPHRRRIGYVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 QEPILFD-CSIAENIAYG-----DNSRVVSQDEIVsaaKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALI 1197
Cdd:COG4148 84 QEARLFPhLSVRGNLLYGrkrapRAERRISFDEVV---ELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1198 RQPQILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAH------RLstiqnADLIVVFQNGRVKEHGTHQQL 1266
Cdd:COG4148 150 SSPRLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEV 221
|
...
gi 9961250 1267 LAQ 1269
Cdd:COG4148 222 LSR 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1033-1269 |
4.88e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.92 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NITFNEVVFNYPTRAnvpvLQgLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNV 1112
Cdd:COG3840 1 MLRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRIL-------WNGQDLTALPP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 qwlrAQ--LGIVSQEPILFD-CSIAENIAYGDNSR----VVSQDEIVSAAKAANIHPFIETLPhkyetrvgdkgTQLSGG 1185
Cdd:COG3840 69 ----AErpVSMLFQENNLFPhLTVAQNIGLGLRPGlkltAEQRAQVEQALERVGLAGLLDRLP-----------GQLSGG 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1186 QKQRIAIARALIRQPQILLLDEATSALD----TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1260
Cdd:COG3840 134 QRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAAD 211
|
....*....
gi 9961250 1261 GTHQQLLAQ 1269
Cdd:COG3840 212 GPTAALLDG 220
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1045-1215 |
7.65e-26 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.80 E-value: 7.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTvvqLLerfyDPLAGTVFVDFGFQ---LLDGQEAKKLNVQwlRAQLGI 1121
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKST---LL----AAIAGTLSPAFSASgevLLNGRRLTALPAE--QRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 VSQEPILFD-CSIAENIAYG---DNSRVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALI 1197
Cdd:COG4136 81 LFQDDLLFPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALL 149
|
170
....*....|....*...
gi 9961250 1198 RQPQILLLDEATSALDTE 1215
Cdd:COG4136 150 AEPRALLLDEPFSKLDAA 167
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
394-624 |
1.08e-25 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 109.80 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFND--VHFSYPSR--------ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF 463
Cdd:PRK15079 9 LEVADlkVHFDIKDGkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 464 NVNYLREI---IGVVSQEPvLFSTT--------IAENICYGRGNVTMDEIKKAVKEanayeFIMK---LPQkfdtLVGER 529
Cdd:PRK15079 89 KDDEWRAVrsdIQMIFQDP-LASLNprmtigeiIAEPLRTYHPKLSRQEVKDRVKA-----MMLKvglLPN----LINRY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 530 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLSTVRNadviagFEDGV 607
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKH------ISDRV 232
|
250
....*....|....*...
gi 9961250 608 IVEQGSHS-ELMKKEGVY 624
Cdd:PRK15079 233 LVMYLGHAvELGTYDEVY 250
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
393-564 |
1.19e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.93 E-value: 1.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 393 NLEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfnVNYL---- 468
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV-----VNELepad 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 469 REIiGVVSQEPVLFS-TTIAENICYG---RGnVTMDEIKKAVKEANAyefIMKLpqkfDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PRK11650 76 RDI-AMVFQNYALYPhMSVRENMAYGlkiRG-MPKAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMG 146
|
170 180
....*....|....*....|
gi 9961250 545 RALVRNPKILLLDEATSALD 564
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLD 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1050-1255 |
1.22e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 113.36 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLLdgqeakklnvqwlraqlgIVSQEPILF 1129
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVL------------------FLPQRPYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLphkyeTRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEAT 1209
Cdd:COG4178 439 LGTLREALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961250 1210 SALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNG 1255
Cdd:COG4178 514 SALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
395-621 |
1.47e-25 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 107.09 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGV 474
Cdd:COG4604 3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 475 VSQEPVLFST-TIAENICYGR-----GNVTmDEIKKAVKEANAYEFIMKLPQKF-DtlvgergaQLSGGQKQRIAIARAL 547
Cdd:COG4604 80 LRQENHINSRlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLstvrN-----ADVIAGFEDGVIVEQGSHSELMKK 620
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEIITP 226
|
.
gi 9961250 621 E 621
Cdd:COG4604 227 E 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1055-1270 |
1.66e-25 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 109.82 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1055 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGqeAKKLNVQWLRAQLGIVSQEPILF-DCSI 1133
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-GRTLFDS--RKGIFLPPEKRRIGYVFQEARLFpHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1134 AENIAYG-----DNSRVVSQDEIVsaaKAANIHPFIETLPHKyetrvgdkgtqLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:TIGR02142 93 RGNLRYGmkrarPSERRISFERVI---ELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1209 TSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
412-603 |
2.07e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 107.18 E-value: 2.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD-----PDEGTINIDGQDIRNFNVN--YLREIIGVVSQEPVLFST 484
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 485 TIAENICYG------RGNvtMDE-IKKAVKEANAY-EFIMKLPQKfdtlvgerGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK14243 106 SIYDNIAYGaringyKGD--MDElVERSLRQAALWdEVKDKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961250 557 DEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGF 603
Cdd:PRK14243 176 DEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFF 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
394-615 |
2.34e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.25 E-value: 2.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirNFN--------- 464
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDfsktpsdka 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 465 VNYLREIIGVVSQEPVLFS-TTIAENI----CYGRGnvtMDEiKKAVKEANAYEFIMKLPQKFDTLvgerGAQLSGGQKQ 539
Cdd:PRK11124 77 IRELRRNVGMVFQQYNLWPhLTVQQNLieapCRVLG---LSK-DQALARAEKLLERLRLKPYADRF----PLHLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHS 615
Cdd:PRK11124 149 RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
397-617 |
2.74e-25 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 107.25 E-value: 2.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 397 NDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirnfnvnylreiIGVVS 476
Cdd:cd03291 38 NNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 477 QEPVLFSTTIAENICYGrgnVTMDEI--KKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:cd03291 105 QFSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLY 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 555 LLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03291 182 LLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1049-1256 |
3.32e-25 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 105.59 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLLDGQEAKKLNVQWLRAQ-LGIVSQ--- 1124
Cdd:COG4778 24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPREILALRRRtIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 ------------EPILfdcsiaeniaygdnSRVVSQDEivSAAKAA------NIHpfiETLPHKYETrvgdkgTqLSGGQ 1186
Cdd:COG4778 104 viprvsaldvvaEPLL--------------ERGVDREE--ARARARellarlNLP---ERLWDLPPA------T-FSGGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1187 KQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGR 1256
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
394-595 |
3.52e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.27 E-value: 3.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPS-RANVKIlkglNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ--DIRNFNVNyLRE 470
Cdd:COG3845 6 LELRGITKRFGGvVANDDV----SLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDA-IAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFST-TIAENICYGR-----GNVTMDEIKKAVKE-ANAYEFIMKLpqkfDTLVGergaQLSGGQKQRIAI 543
Cdd:COG3845 81 GIGMVHQHFMLVPNlTVAENIVLGLeptkgGRLDRKAARARIRElSERYGLDVDP----DAKVE----DLSVGEQQRVEI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 544 ARALVRNPKILLLDEATSALdTESEA-EVQAALDK-AREGRTTIVIAHRLSTVR 595
Cdd:COG3845 153 LKALYRGARILILDEPTAVL-TPQEAdELFEILRRlAAEGKSIIFITHKLREVM 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1046-1270 |
3.87e-25 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 106.43 E-value: 3.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1046 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgFQlldGQEAKKLNVQWLRA---QLGIV 1122
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS----FR---GQDLYQLDRKQRRAfrrDVQLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 SQepilfDC--------SIAENIayGDNSR-VVSQDEIVSAAKAANIHPFIETLPHKYETRvgdkGTQLSGGQKQRIAIA 1193
Cdd:TIGR02769 94 FQ-----DSpsavnprmTVRQII--GEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKL----PRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1266 |
5.22e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.99 E-value: 5.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRANVpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdFGFQLLDGQeakklNVQ 1113
Cdd:PRK13648 8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF--YNNQAITDD-----NFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPI-LFDCSIAE-NIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPHkyetrvgdkgtQLSGGQK 1187
Cdd:PRK13648 80 KLRKHIGIVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQ 1265
Cdd:PRK13648 149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTE 228
|
.
gi 9961250 1266 L 1266
Cdd:PRK13648 229 I 229
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
393-612 |
5.74e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 104.66 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 393 NLEFNDVhFSYPSRAN--VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDE---GTINIDGQDIRNFNVny 467
Cdd:cd03234 3 VLPWWDV-GLKAKNWNkyARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQF-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 468 lREIIGVVSQEPVLFST-TIAENICYG---RGNVTM-DEIKKAVKEanayefIMKLPQKFDTLVG-ERGAQLSGGQKQRI 541
Cdd:cd03234 80 -QKCVAYVRQDDILLPGlTVRETLTYTailRLPRKSsDAIRKKRVE------DVLLRDLALTRIGgNLVKGISGGERRRV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 542 AIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQG 612
Cdd:cd03234 153 SIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLsQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
392-629 |
6.01e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 113.34 E-value: 6.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYpsRANVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLRE 470
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFSTTIaenicygRGNV------TMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTV-------RQNVdpfleaSSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMA 1457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 545 RALV-RNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGSHSEL-MKKEG 622
Cdd:PTZ00243 1458 RALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQS 1537
|
....*..
gi 9961250 623 VYFKLVN 629
Cdd:PTZ00243 1538 IFHSMVE 1544
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1040-1273 |
6.10e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 107.24 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1040 VFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFV---------DFGFQLLDGQEAKKL 1110
Cdd:PRK13631 30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNPYSKKIK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1111 NVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEivsAAKAANIH--------PFIETLPHkyetrvgdkgt 1180
Cdd:PRK13631 110 NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYlnkmglddSYLERSPF----------- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1181 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVK 1258
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKIL 255
|
250
....*....|....*
gi 9961250 1259 EHGTHQQLLAQKGIY 1273
Cdd:PRK13631 256 KTGTPYEIFTDQHII 270
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
411-617 |
6.44e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 105.51 E-value: 6.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ------DIRNFNVNYLREIIGVVSQEPVLFS- 483
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 484 TTIAENICY---GRGNVTMDEIKKAVKEANAYEFIMKlpQKFDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK14246 105 LSIYDNIAYplkSHGIKEKREIKKIVEECLRKVGLWK--EVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 561 SALDTESEAEVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1047-1269 |
6.70e-25 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 107.36 E-value: 6.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1047 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLN---VQWLRAQLGIVS 1123
Cdd:PRK11308 26 RLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELY-------YQGQDLLKADpeaQKLLRQKIQIVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 QEPilfdcsiaeniaYGD-NSR-VVSQ---------DEIVSAAKAANIHPFIETL----------PHKYetrvgdkgtql 1182
Cdd:PRK11308 99 QNP------------YGSlNPRkKVGQileepllinTSLSAAERREKALAMMAKVglrpehydryPHMF----------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1183 SGGQKQRIAIARALIRQPQILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKE 1259
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVE 235
|
250
....*....|
gi 9961250 1260 HGTHQQLLAQ 1269
Cdd:PRK11308 236 KGTKEQIFNN 245
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
393-580 |
7.54e-25 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 107.86 E-value: 7.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 393 NLEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLReiI 472
Cdd:PRK10851 2 SIEIANIKKSF---GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFS-TTIAENICYG------RGNVTMDEIKKAVkeanayefiMKLPQ--KFDTLVGERGAQLSGGQKQRIAI 543
Cdd:PRK10851 77 GFVFQHYALFRhMTVFDNIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961250 544 ARALVRNPKILLLDEATSALDTESEAEVQAALDKARE 580
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHE 184
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
396-589 |
9.21e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.15 E-value: 9.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 396 FNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqDIRnfnvnylreiIGVV 475
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 476 SQEPVLFST-TIAENICYGRGNV--TMDEIKKAVK--------------------EANAYEF------IMK---LPQK-F 522
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGDAELraLEAELEELEAklaepdedlerlaelqeefeALGGWEAearaeeILSglgFPEEdL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 523 DTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAEVqaaldKAREGrTTIVIAH 589
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1051-1269 |
1.15e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 107.11 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQwlRAQLGIVSQEPILF- 1129
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFID-------GEDVTHRSIQ--QRDICMVFQSYALFp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIETLP-HKYETRVGDkgtQLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:PRK11432 92 HMSLGENVGYGLKMLGVPKEERKQRVKEA-----LELVDlAGFEDRYVD---QISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1209 TSALDTESEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:PRK11432 164 LSNLDANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
415-618 |
1.20e-24 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 107.12 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 415 LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDG---QDIR-NFNVNYLREIIGVVSQEPVLFS-TTIAEN 489
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRkGIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 490 ICYGRGNVTMDEikKAVKEANAYEFImklpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 569
Cdd:TIGR02142 96 LRYGMKRARPSE--RRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 570 EVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGSHSELM 618
Cdd:TIGR02142 169 EILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1049-1269 |
1.21e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 109.77 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRA----QLG 1120
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSI-------LFDGQDLLGLSERELRRirgnRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1121 IVSQEPI-----LFdcSIAENIAygdnsrvvsqdEIVS--------AAKAANIHPFIET-LPHKyETRVGDKGTQLSGGQ 1186
Cdd:COG4172 96 MIFQEPMtslnpLH--TIGKQIA-----------EVLRlhrglsgaAARARALELLERVgIPDP-ERRLDAYPHQLSGGQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1187 KQRIAIARALIRQPQILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKE 1259
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVE 237
|
250
....*....|
gi 9961250 1260 HGTHQQLLAQ 1269
Cdd:COG4172 238 QGPTAELFAA 247
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1270 |
1.61e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYP--TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdFGFQLLDGQEAKKLN 1111
Cdd:PRK13636 6 LKVEELNYNYSdgTHA----LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL--FDGKPIDYSRKGLMK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 vqwLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKyetrvgdKGTQLSGGQKQR 1189
Cdd:PRK13636 80 ---LRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1190 IAIARALIRQPQILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVFQNGRVKEHGTHQ 1264
Cdd:PRK13636 150 VAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPK 227
|
....*.
gi 9961250 1265 QLLAQK 1270
Cdd:PRK13636 228 EVFAEK 233
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
394-624 |
1.87e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 105.82 E-value: 1.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSR-------ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN-- 464
Cdd:PRK11308 6 LQAIDLKKHYPVKrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 465 -VNYLREIIGVVSQEPvlfsttiaenicYG----RGNV--TMDE-------IKKAVKEANAYEFIMKlpqkfdtlVGERG 530
Cdd:PRK11308 86 aQKLLRQKIQIVFQNP------------YGslnpRKKVgqILEEpllintsLSAAERREKALAMMAK--------VGLRP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 531 AQ-------LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIV-IAHRLSTVRN-ADVI 600
Cdd:PRK11308 146 EHydryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVfISHDLSVVEHiADEV 225
|
250 260
....*....|....*....|....
gi 9961250 601 AGFEDGVIVEQGShselmkKEGVY 624
Cdd:PRK11308 226 MVMYLGRCVEKGT------KEQIF 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1039-1268 |
1.94e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1039 VVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfqllDGQEAKKLNVQWLRAQ 1118
Cdd:PRK13642 10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-------DGELLTAENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1119 LGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIV----SAAKAANIHPFIETLPhkyetrvgdkgTQLSGGQKQRIAI 1192
Cdd:PRK13642 83 IGMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIkrvdEALLAVNMLDFKTREP-----------ARLSGGQKQRVAV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1193 ARALIRQPQILLLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:PRK13642 152 AGIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
394-612 |
1.96e-24 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 102.83 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSY-PSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrNFNVNYLREII 472
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFS-TTIAENICY--GRGNVTMDEIKKAVKEanayefimkLPQKFDT--LVGERGAQLSGGQKQRIAIARAL 547
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYfaGLYGLKGDELTARLEE---------LADRLGMeeLLDRRVGGFSTGMRQKVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFEDGVIVEQG 612
Cdd:cd03266 152 VHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1034-1268 |
2.14e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.72 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfGFQLLD-GQEAK 1108
Cdd:PRK13634 3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI--GERVITaGKKNK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1109 KLNVqwLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfIET--LPHKYETRvgdKGTQLSG 1184
Cdd:PRK13634 79 KLKP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IELvgLPEELLAR---SPFELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1185 GQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1260
Cdd:PRK13634 149 GQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQ 227
|
....*...
gi 9961250 1261 GTHQQLLA 1268
Cdd:PRK13634 228 GTPREIFA 235
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1050-1238 |
2.27e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 106.84 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKklNVQWLRAQLGIVSQEPILF 1129
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQI-------MLDGVDLS--HVPPYQRPINMMFQSYALF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 -DCSIAENIAYGdnsrvVSQDEIVSAAKAANIHPFIeTLPHKYETrVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:PRK11607 104 pHMTVEQNIAFG-----LKQDKLPKAEIASRVNEML-GLVHMQEF-AKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|..
gi 9961250 1209 TSALDTESEKVVQ-EALD-KAREGRTCIVIAH 1238
Cdd:PRK11607 177 MGALDKKLRDRMQlEVVDiLERVGVTCVMVTH 208
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1033-1263 |
2.62e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFV---DFGFQlldgQEAKK 1109
Cdd:COG4161 2 SIQLKNINCFY---GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaghQFDFS----QKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 LNVQWLRAQLGIVSQE----PILfdcSIAENIAYGDnSRVVSQDEIVSAAKAANIhpfIETLphkyetRVGDKGT----Q 1181
Cdd:COG4161 75 KAIRLLRQKVGMVFQQynlwPHL---TVMENLIEAP-CKVLGLSKEQAREKAMKL---LARL------RLTDKADrfplH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1182 LSGGQKQRIAIARALIRQPQILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKE 1259
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIE 221
|
....
gi 9961250 1260 HGTH 1263
Cdd:COG4161 222 QGDA 225
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1052-1266 |
2.84e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 103.32 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpLAGTVFVDfGFQLLDGQE--AKKLNVQWLRAQLGIVSQEPILF 1129
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMND-LNPEVTIT-GSIVYNGHNiySPRTDTVDLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRVVSQDEIVSAA-----KAANIhpFIETLPHKYETRVGdkgtqLSGGQKQRIAIARALIRQPQILL 1204
Cdd:PRK14239 99 PMSIYENVVYGLRLKGIKDKQVLDEAvekslKGASI--WDEVKDRLHDSALG-----LSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1205 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRL---STIqnADLIVVFQNGRVKEHGTHQQL 1266
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
394-621 |
3.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 104.11 E-value: 3.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEP--VLFSTTIAENICYGRGNVTMDE------IKKAVKEANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIAR 545
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1043-1266 |
3.27e-24 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 102.20 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1043 YPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGQEAkklnvqwLRAQLGIV 1122
Cdd:cd03263 10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN-GYSIRTDRKA-------ARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 SQEPILFD-CSIAENIAYgdNSRV--VSQDEIvsaakAANIHPFIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALI 1197
Cdd:cd03263 81 PQFDALFDeLTVREHLRF--YARLkgLPKSEI-----KEEVELLLRVlgLTDKANKRART----LSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1198 RQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1266
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
411-612 |
3.27e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 103.38 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD-----EGTINIDGQDIRNFNVN--YLREIIGVVSQEPVLFS 483
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 484 -TTIAENICYG-------RGNVTMDE-IKKAVKEANAYEFIMklpqkfDTLvGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:PRK14267 99 hLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWDEVK------DRL-NDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 555 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHR-LSTVRNADVIAGFEDGVIVEQG 612
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
394-620 |
3.89e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 103.67 E-value: 3.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPS------RAnvkiLKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN- 466
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegRA----LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 467 ---YLREIIGVVSQ--EPVLFSTTIAENICYGRGN--VTMDEIKKAVKEANAYEFIMklpqkfDTLVGERGAQLSGGQKQ 539
Cdd:PRK13649 79 dikQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 540 RIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGKPKDI 232
|
...
gi 9961250 618 MKK 620
Cdd:PRK13649 233 FQD 235
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
394-623 |
3.95e-24 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 102.24 E-value: 3.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNY-LREII 472
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLF-STTIAENIcygrgnvtmdeikKAVKEanayefIMKLP-----QKFDTLVGE---------RGAQLSGGQ 537
Cdd:cd03218 78 GYLPQEASIFrKLTVEENI-------------LAVLE------IRGLSkkereEKLEELLEEfhithlrksKASSLSGGE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIA-HR----LSTVRNADVIAgfeDGVIVEQG 612
Cdd:cd03218 139 RRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYIIY---EGKVLAEG 215
|
250
....*....|.
gi 9961250 613 SHSELMKKEGV 623
Cdd:cd03218 216 TPEEIAANELV 226
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
412-617 |
4.23e-24 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 102.06 E-value: 4.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNyLREIIGVVSQEPvlfsttIAENIC 491
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVFQDL------SVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 492 YGRGNVTM---------DEIKKAVKEANAYefiMKLPQKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:cd03265 89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 563 LDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:cd03265 162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
394-606 |
5.06e-24 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 101.64 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKST----TVQLIQRL------YDPDEGTINIDGQDIRNf 463
Cdd:cd03290 1 VQVTNGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSlllaILGEMQTLegkvhwSNKNESEPSFEATRSRN- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 464 nvnylREIIGVVSQEPVLFSTTIAENICYGrgNVTMDEIKKAVKEANAYE-FIMKLPQKFDTLVGERGAQLSGGQKQRIA 542
Cdd:cd03290 78 -----RYSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRIC 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 543 IARALVRNPKILLLDEATSALDTE-SEAEVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFEDG 606
Cdd:cd03290 151 VARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
412-589 |
5.45e-24 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 102.16 E-value: 5.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLreiigVVSQEPVLFS-TTIAENI 490
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 491 CYGRGNVtMDEIKKAVKEANAYEFImklpqkfdTLVG------ERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:TIGR01184 76 ALAVDRV-LPDLSKSERRAIVEEHI--------ALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*..
gi 9961250 565 TESEAEVQAALDKARE--GRTTIVIAH 589
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEehRVTVLMVTH 173
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
394-621 |
8.06e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 107.06 E-value: 8.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-I 472
Cdd:PRK15439 12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLF-STTIAENICYG--RGNVTMDEIKKAVKEANAYefiMKLPQKFDTL-VGERgaqlsggqkQRIAIARALV 548
Cdd:PRK15439 89 YLVPQEPLLFpNLSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 549 RNPKILLLDEATSALdTESEAE-----VQAALDKareGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK15439 157 RDSRILILDEPTASL-TPAETErlfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDD 231
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1048-1268 |
8.44e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 101.60 E-value: 8.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVqWLRAQLGI--VSQE 1125
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI-------RFDGEDITGLPP-HRIARLGIgyVPEG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILF-DCSIAENIaygdnsrvvsqdeIVSAAKAANIHPFIETLPHKYET------RVGDKGTQLSGGQKQRIAIARALIR 1198
Cdd:COG0410 87 RRIFpSLTVEENL-------------LLGAYARRDRAEVRADLERVYELfprlkeRRRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1199 QPQILLLDEATSALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:COG0410 154 RPKLLLLDEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
129-347 |
1.02e-23 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 102.89 E-value: 1.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 129 VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIV 208
Cdd:cd18552 54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 209 GFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKE 288
Cdd:cd18552 134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 289 IGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSV 347
Cdd:cd18552 214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1034-1267 |
1.23e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 101.31 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG-TVFVdFGFQLldGQEakklNV 1112
Cdd:COG1119 4 LELRNVTVRRGGK---TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRL-FGERR--GGE----DV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWLRAQLGIVSQEpilfdcsIAENIAYGDNSR--VVS------------QDEIVSAAKAAnihpfIETL--PHKYETRVG 1176
Cdd:COG1119 74 WELRKRIGLVSPA-------LQLRFPRDETVLdvVLSgffdsiglyrepTDEQRERAREL-----LELLglAHLADRPFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1177 dkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliV 1250
Cdd:COG1119 142 ----TLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---L 214
|
250
....*....|....*..
gi 9961250 1251 VFQNGRVKEHGTHQQLL 1267
Cdd:COG1119 215 LLKDGRVVAAGPKEEVL 231
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
111-364 |
1.31e-23 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 102.56 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 111 EEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGD 190
Cdd:cd18575 33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:cd18575 113 SLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFT 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-AMTVFFSILIgAFSVGQ 349
Cdd:cd18575 193 REDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGElSQFVFYAVLA-AGSVGA 271
|
250
....*....|....*
gi 9961250 350 AAPCIDAFANARGAA 364
Cdd:cd18575 272 LSEVWGDLQRAAGAA 286
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1034-1262 |
1.41e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.19 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAGTVFVdfgfqlLDGQEAKKLN 1111
Cdd:PRK13640 6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpDDNPNSKIT------VDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 VQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAA----NIHPFIETLPhkyetrvgdkgTQLSGG 1185
Cdd:PRK13640 79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVladvGMLDYIDSEP-----------ANLSGG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1186 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1262
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
416-618 |
1.94e-23 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.43 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 416 NLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylREIIGVVSQEPVLFS-TTIAENICYG- 493
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 494 ----RGNV----TMDEIKKAVKEANayeFIMKLPqkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:PRK10771 97 npglKLNAaqreKLHAIARQMGIED---LLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 566 ESEAEVQAALDKAREGR--TTIVIAHRLS-TVRNAD---VIAgfeDGVIVEQGSHSELM 618
Cdd:PRK10771 163 ALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1051-1269 |
2.18e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 101.20 E-value: 2.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLL----DGQ--EAKKLNVQWLRAQLGIVSQ 1124
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkDGQlkVADKNQLRLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 EPILFD-CSIAENIAYGDnSRVVSQDEIVSAAKAAnihpfietlphKYETRVG-DKGTQ------LSGGQKQRIAIARAL 1196
Cdd:PRK10619 100 HFNLWShMTVLENVMEAP-IQVLGLSKQEARERAV-----------KYLAKVGiDERAQgkypvhLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1197 IRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIVVF-QNGRVKEHGTHQQLLAQ 1269
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLFGN 242
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1034-1238 |
3.05e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYP-TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEakklnV 1112
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEI-------TLDGVP-----V 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWLRAQLGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVSAAkaanihpfietlpHKYETRVGDKGT------QLSGG 1185
Cdd:COG4525 72 TGPGADRGVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARA-------------EELLALVGLADFarrriwQLSGG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1186 QKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1238
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
394-612 |
3.35e-23 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 98.83 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIiG 473
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRI-G 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFST-TIAENICYGRgnVTMDEIKKAVKEANAYefimklpqkfdtlVGERGA------QLSGGQKQRIAIARA 546
Cdd:cd03268 76 ALIEAPGFYPNlTARENLRLLA--RLLGIRKKRIDEVLDV-------------VGLKDSakkkvkGFSLGMKQRLGIALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
403-617 |
3.60e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.19 E-value: 3.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 403 YPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdiRNFNVNYLREIIGVVSQEPVLF 482
Cdd:PRK11000 10 TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 483 S-TTIAENICYGR--GNVTMDEIKKAVKEANAyefIMKLpqkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 559
Cdd:PRK11000 88 PhLSVAENMSFGLklAGAKKEEINQRVNQVAE---VLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 560 TSALDTESEAEVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK11000 161 LSNLDAALRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
409-624 |
4.34e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 4.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINID----GQD--------------IRNFNvnYLRE 470
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKknnhelitnpyskkIKNFK--ELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEP--VLFSTTIAENICYGrgNVTMDEIKKAVKEANAYeFIMKLPQKFDTLvgERGA-QLSGGQKQRIAIARAL 547
Cdd:PRK13631 117 RVSMVFQFPeyQLFKDTIEKDIMFG--PVALGVKKSEAKKLAKF-YLNKMGLDDSYL--ERSPfGLSGGQKRRVAIAGIL 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 548 VRNPKILLLDEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEGVY 624
Cdd:PRK13631 192 AIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1044-1261 |
4.60e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 98.98 E-value: 4.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1044 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVFVDFGFQLLDGQEAKKlNVQWLRAQLGIVS 1123
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRML-------AGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 QEPILFD-CSIAENIAYGDNSRVVSQDEIVSA----AKAANIHPFIETlphkyetRVGDkgtqLSGGQKQRIAIARALIR 1198
Cdd:cd03266 85 DSTGLYDrLTARENLEYFAGLYGLKGDELTARleelADRLGMEELLDR-------RVGG----FSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1199 QPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGRVKEHG 1261
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
394-623 |
6.22e-23 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 98.75 E-value: 6.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL-REII 472
Cdd:TIGR03410 1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFST-TIAENICYGrgnvtMDEIKKAVKE--ANAYEFimkLPQKFDTLvGERGAQLSGGQKQRIAIARALVR 549
Cdd:TIGR03410 78 AYVPQGREIFPRlTVEENLLTG-----LAALPRRSRKipDEIYEL---FPVLKEML-GRRGGDLSGGQQQQLAIARALVT 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSElMKKEGV 623
Cdd:TIGR03410 149 RPKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDE-LDEDKV 224
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
100-339 |
8.21e-23 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 100.20 E-value: 8.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 100 LSLLNPG-------KILEEEMTRYAYYYSG--LGAGVL--VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDIN 168
Cdd:cd18542 14 LNLLIPLlirriidSVIGGGLRELLWLLALliLGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 169 DTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKIL-SAFSDK--- 244
Cdd:cd18542 94 RTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVrPAFEEIreq 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 245 --ELaayakaGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTL 322
Cdd:cd18542 174 egEL------NTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYL 247
|
250
....*....|....*..
gi 9961250 323 VISKEYTIGNaMTVFFS 339
Cdd:cd18542 248 VINGEITLGE-LVAFIS 263
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1049-1259 |
8.61e-23 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 98.66 E-value: 8.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGTVFvdfgfqlLDGQEAKKLN----VQWLRAQLGI 1121
Cdd:COG4181 25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVR-------LAGQDLFALDedarARLRARHVGF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 VSQE----PILfdcSIAENIAY-----GDNSrvvsqdeivSAAKAAnihpfiETLphkyeTRVGDKG------TQLSGGQ 1186
Cdd:COG4181 95 VFQSfqllPTL---TALENVMLplelaGRRD---------ARARAR------ALL-----ERVGLGHrldhypAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1187 KQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1259
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1055-1261 |
8.65e-23 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 97.95 E-value: 8.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1055 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQwlRAQLGIVSQEPILF-DCSI 1133
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV-------LINGVDVTAAPPA--DRPVSMLFQENNLFaHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1134 AENIAYGDNSRV----VSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEAT 1209
Cdd:cd03298 88 EQNVGLGLSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1210 SALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1261
Cdd:cd03298 157 AALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1052-1270 |
8.99e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.90 E-value: 8.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGQEAKklNVQWLRAQLGIVSQ--EPILF 1129
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIA-GYHITPETGNK--NLKKLRKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRVVSQDEIVSAAKaanihpfietlphKYETRVG------DKGT-QLSGGQKQRIAIARALIRQPQI 1202
Cdd:PRK13641 100 ENTVLKDVEFGPKNFGFSEDEAKEKAL-------------KWLKKVGlsedliSKSPfELSGGQMRRVAIAGVMAYEPEI 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1203 LLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:PRK13641 167 LCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
412-657 |
1.11e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.03 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI----IGVVSQEPVLFS-TTI 486
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENICYGrgnVTMDEIKKAVKEANAYEFIMKLpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 566
Cdd:PRK10070 124 LDNTAFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 567 SEAEVQAALDK--AREGRTTIVIAHRL-STVRNADVIAGFEDGVIVEQGSHSELMKKEG-----VYFKLVNMqtsgSQIQ 638
Cdd:PRK10070 199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAndyvrTFFRGVDI----SQVF 274
|
250
....*....|....*....
gi 9961250 639 SeefelndEKAATRMAPNG 657
Cdd:PRK10070 275 S-------AKDIARRTPNG 286
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
394-613 |
1.16e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 99.29 E-value: 1.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSraNVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN-VNYLREII 472
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEP--VLFSTTIAENICYGRGNVTMD--EIKKAVKEANAYEFIMKLPQKfdtlvgeRGAQLSGGQKQRIAIARALV 548
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 549 RNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTVRNADVIAGFEDGVIVEQGS 613
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1037-1270 |
1.42e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 99.00 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1037 NEVVFNYPTraNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWL- 1115
Cdd:PRK13639 5 RDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEV-------LIKGEPIKYDKKSLLe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1116 -RAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEI----VSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQ 1188
Cdd:PRK13639 76 vRKTVGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVekrvKEALKAVGMEGFENKPPH-----------HLSGGQKK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1189 RIAIARALIRQPQILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVFQNGRVKEHGTHQQL 1266
Cdd:PRK13639 145 RVAIAGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
|
....
gi 9961250 1267 LAQK 1270
Cdd:PRK13639 225 FSDI 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1044-1261 |
1.45e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 96.85 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1044 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGTVFVDfgfqlldgqeAKKLNVQWLRAQLGI 1121
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLIN----------GRPLDKRSFRKIIGY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 VSQEPILFDC-SIAENIAYgdnsrvvsqdeivsaakAANIhpfietlphkyetrvgdKGtqLSGGQKQRIAIARALIRQP 1200
Cdd:cd03213 87 VPQDDILHPTlTVRETLMF-----------------AAKL-----------------RG--LSGGERKRVSIALELVSNP 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1201 QILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHG 1261
Cdd:cd03213 131 SLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1032-1278 |
1.96e-22 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 98.77 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1032 GNITFNEVVFNYpTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFydplagtVFVDFGFQLlDGQEAKKLN 1111
Cdd:cd03289 1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-------LNTEGDIQI-DGVSWNSVP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 VQWLRAQLGIVSQEPILFDCSIAENI-AYGDNSrvvsQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRI 1190
Cdd:cd03289 72 LQKWRKAFGVIPQKVFIFSGTFRKNLdPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1191 AIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
....*...
gi 9961250 1271 GIYFSMVS 1278
Cdd:cd03289 228 SHFKQAIS 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1051-1264 |
2.09e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFV---DFGFqlldGQEAKKLNVQWLRAQLGIVSQE-- 1125
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagnHFDF----SKTPSDKAIRELRRNVGMVFQQyn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 --PILfdcSIAENIAYGDnSRVVSQDEIVSAAKAANIhpfIETLphkyetRVGDKGT----QLSGGQKQRIAIARALIRQ 1199
Cdd:PRK11124 93 lwPHL---TVQQNLIEAP-CRVLGLSKDQALARAEKL---LERL------RLKPYADrfplHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1200 PQILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1264
Cdd:PRK11124 160 PQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1048-1261 |
2.26e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.06 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIV 1122
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEV-------YLDGQDIFKMDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 SQEP-ILFDCSIAENIAYGD--NSRVVSQDEIVSAAKAAnihpfIET--LPHKYETRVGDKGTQLSGGQKQRIAIARALI 1197
Cdd:PRK14247 88 FQIPnPIPNLSIFENVALGLklNRLVKSKKELQERVRWA-----LEKaqLWDEVKDRLDAPAGKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1198 RQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVFQNGRVKEHG 1261
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1034-1262 |
2.55e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.66 E-value: 2.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFgfQLLDGQEAKKlN 1111
Cdd:PRK13649 3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDD--TLITSTSKNK-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 VQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVSAAKaanihpfiETLphkyeTRVG------DKGT-QL 1182
Cdd:PRK13649 80 IKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAR--------EKL-----ALVGiseslfEKNPfEL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1183 SGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1260
Cdd:PRK13649 147 SGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLS 226
|
..
gi 9961250 1261 GT 1262
Cdd:PRK13649 227 GK 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1033-1257 |
2.56e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.85 E-value: 2.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NITfneVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVFVDFGFQLLDGQEAKKLNV 1112
Cdd:COG1101 6 NLS---KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAI-------AGSLPPDSGSILIDGKDVTKLPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 qWLRAQL-GIVSQEPILFDC---SIAEN--IAYGDNSRVvsqdEIVSAAKAANIHPFIET-------LPHKYETRVGdkg 1179
Cdd:COG1101 76 -YKRAKYiGRVFQDPMMGTApsmTIEENlaLAYRRGKRR----GLRRGLTKKRRELFRELlatlglgLENRLDTKVG--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1180 tQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGR 1256
Cdd:COG1101 148 -LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGR 226
|
.
gi 9961250 1257 V 1257
Cdd:COG1101 227 I 227
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
409-613 |
2.63e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 97.80 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVnylREII--GVVS--QEPVLFST 484
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP---HRIArlGIARtfQNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 485 -TIAENI---CYGRGNVTM-----------DEIKKAVKEANAY-EFiMKLPQKFDTLVGErgaqLSGGQKQRIAIARALV 548
Cdd:COG0411 94 lTVLENVlvaAHARLGRGLlaallrlprarREEREARERAEELlER-VGLADRADEPAGN----LSYGQQRRLEIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 549 RNPKILLLDEATSALdteSEAEVQAALD-----KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 613
Cdd:COG0411 169 TEPKLLLLDEPAAGL---NPEETEELAElirrlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1049-1257 |
2.68e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 97.80 E-value: 2.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVqWLRAQLGIVS--QEP 1126
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRI-------LFDGRDITGLPP-HRIARLGIARtfQNP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILF-DCSIAENIA----YGDNSRVVS---------QDEIVSAAKAANIhpfIET--LPHKYETRVGDkgtqLSGGQKQRI 1190
Cdd:COG0411 89 RLFpELTVLENVLvaahARLGRGLLAallrlprarREEREARERAEEL---LERvgLADRADEPAGN----LSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1191 AIARALIRQPQILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
415-589 |
2.71e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.68 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 415 LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNvNYLREIiGVVSQEPVLFS-TTIAENICYG 493
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPI-NMMFQSYALFPhMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 494 --RGNVTMDEIKKAVKE----ANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE- 566
Cdd:PRK11607 116 lkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKl 184
|
170 180
....*....|....*....|....*.
gi 9961250 567 ---SEAEVQAALDkaREGRTTIVIAH 589
Cdd:PRK11607 185 rdrMQLEVVDILE--RVGVTCVMVTH 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1047-1261 |
2.95e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 96.20 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1047 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDF-GFQLLDGQeakklnvqwlraQLGIVSQE 1125
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGkPLDIAARN------------RIGYLPEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILF-DCSIAENIAYGDNSRVVSQDEIvsaakAANIHPFIET--LPHKYETRVgdkgTQLSGGQKQRIAIARALIRQPQI 1202
Cdd:cd03269 79 RGLYpKMKVIDQLVYLAQLKGLKKEEA-----RRRIDEWLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPEL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1203 LLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1261
Cdd:cd03269 150 LILDEPFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
402-598 |
3.20e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 402 SYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqdirNFNVNYLREIIGVVSQEPVl 481
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 482 fstTIAENICYGR-------GNVTMDEiKKAVKEAnayefIMKLpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 554
Cdd:NF040873 73 ---TVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961250 555 LLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRNAD 598
Cdd:NF040873 142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
405-580 |
4.44e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.63 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIRNFNVnYLREIiGVVSQEPVL 481
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA-EQRRI-GILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 482 FS-TTIAENICYG-----RGNVTMDEIKKAVKEANayefimkLPQKFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 555
Cdd:COG4136 88 FPhLSVGENLAFAlpptiGRAQRRARVEQALEEAG-------LAGFADRDP----ATLSGGQRARVALLRALLAEPRALL 156
|
170 180
....*....|....*....|....*.
gi 9961250 556 LDEATSALDTESEAEVQA-ALDKARE 580
Cdd:COG4136 157 LDEPFSKLDAALRAQFREfVFEQIRQ 182
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1034-1262 |
5.00e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.88 E-value: 5.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVvfNYPTRANVP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfQLLDGQEAKK 1109
Cdd:PRK13643 2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG---DIVVSSTSKQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 LNVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEI--VSAAKAANI---HPFIETLPHkyetrvgdkgtQL 1182
Cdd:PRK13643 77 KEIKPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAekIAAEKLEMVglaDEFWEKSPF-----------EL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1183 SGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1260
Cdd:PRK13643 146 SGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISC 225
|
..
gi 9961250 1261 GT 1262
Cdd:PRK13643 226 GT 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1051-1266 |
5.20e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.39 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVFVDFGFQLLDGQEAKKLNVQwlRAQLGIVSQEPILF- 1129
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRII-------AGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYG---------DNSRVVSQD-----EIVSAAKAANIHPfietlphkyetrvgdkgTQLSGGQKQRIAIARA 1195
Cdd:PRK10851 88 HMTVFDNIAFGltvlprrerPNAAAIKAKvtqllEMVQLAHLADRYP-----------------AQLSGGQKQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1196 LIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHGTHQQL 1266
Cdd:PRK10851 151 LAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1051-1261 |
7.25e-22 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 95.34 E-value: 7.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKlNVQWLRAQLGIVSQEPILFD 1130
Cdd:cd03264 15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTI-------RIDGQDVLK-QPQKLRRRIGYLPQEFGVYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 -CSIAENIAY-----GDNSRVVSQdEIVSAAKAANIHPFietlphkYETRVGdkgtQLSGGQKQRIAIARALIRQPQILL 1204
Cdd:cd03264 86 nFTVREFLDYiawlkGIPSKEVKA-RVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1205 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1261
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
711-968 |
7.89e-22 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 97.50 E-value: 7.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIaifgpgDDAVKQQKCN---IFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRL 787
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRII------DSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 788 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPII 867
Cdd:cd18542 75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 868 AVSGIVEMKLLaGNAKRDKKELEAA-GKIATEAIENIRTVVSLTQER----KFESmyVEKLYgpYRNSVQKAHIYGITFS 942
Cdd:cd18542 153 ALFSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFAREDyeieKFDK--ENEEY--RDLNIKLAKLLAKYWP 227
|
250 260
....*....|....*....|....*.
gi 9961250 943 ISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18542 228 LMDFLSGLQIVLVLWVGGYLVINGEI 253
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
394-608 |
8.08e-22 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 96.29 E-value: 8.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTInIDGqdirNFNVNYLREIIG 473
Cdd:PRK11247 13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG----TAPLAEAREDTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLFS-TTIAENICYG-RGNVTMD--EIKKAVKEANAyefimklpqkfdtlVGERGAQLSGGQKQRIAIARALVR 549
Cdd:PRK11247 85 LMFQDARLLPwKKVIDNVGLGlKGQWRDAalQALAAVGLADR--------------ANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVI 608
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
394-621 |
9.18e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 96.38 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG 473
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVL-FSTTIAENICYGRGnvTMDEIKKAVKEanayefimkLPQKFDTLVGERG------AQLSGGQKQRIAIARA 546
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRA--PHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 547 LVR------NPKILLLDEATSALDTESEAEV-QAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK13548 149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVlRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEV 228
|
....
gi 9961250 618 MKKE 621
Cdd:PRK13548 229 LTPE 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
394-612 |
9.22e-22 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 95.04 E-value: 9.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNvnylREIIG 473
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLF-STTIAENICY-GRgnvtmdeiKKAVKEANAYEFIMKLPQKFD--TLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYlAQ--------LKGLKKEEARRRIDEWLERLElsEYANKRVEELSKGNQQKVQFIAAVIH 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 550 NPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 612
Cdd:cd03269 146 DPELLILDEPFSGLDPVN-VELlkDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
410-621 |
9.36e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.46 E-value: 9.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF------------------------NV 465
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqktrfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 NYLREIIGVVSQ--EPVLFSTTIAENICYGRGNVTMDEiKKAVKEANAYEFIMKLPQKFDtlvgERGA-QLSGGQKQRIA 542
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRRVA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIAHRLSTV--RNADVIAgFEDGVIVEQGSHSELMK 619
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIF-FKDGKIIKDGDTYDILS 254
|
..
gi 9961250 620 KE 621
Cdd:PRK13651 255 DN 256
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1046-1267 |
1.14e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 95.99 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1046 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQE 1125
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEV-------RLNGRPLADWSPAELARRRAVLPQH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PIL-FDCSIAENIAYG--DNSRVVSQD-EIVSAAKAanihpfiET-LPHkYETRvgdKGTQLSGGQKQRIAIARALIR-- 1198
Cdd:PRK13548 85 SSLsFPFTVEEVVAMGraPHGLSRAEDdALVAAALA-------QVdLAH-LAGR---DYPQLSGGEQQRVQLARVLAQlw 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1199 ----QPQILLLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1267
Cdd:PRK13548 154 epdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
394-622 |
1.20e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.10 E-value: 1.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN---YLRE 470
Cdd:COG4152 2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 iigvvsqEPVLF-STTIAENICY-GR--GnVTMDEIKKAVKEanayefimkLPQKFDtlVGERGA----QLSGGQKQRIA 542
Cdd:COG4152 79 -------ERGLYpKMKVGEQLVYlARlkG-LSKAEAKRRADE---------WLERLG--LGDRANkkveELSKGNQQKVQ 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 543 IARALVRNPKILLLDEATSALDTESeAEV--QAALDKAREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMK 619
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVN-VELlkDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRR 218
|
...
gi 9961250 620 KEG 622
Cdd:COG4152 219 QFG 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
394-590 |
1.32e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 92.99 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVhfSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDirnfNVNYLreiig 473
Cdd:cd03223 1 IELENL--SLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 vvSQEPVLFSTTIAENICYGRGNVtmdeikkavkeanayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03223 70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*...
gi 9961250 554 LLLDEATSALDTESEAEVqaaLDKAREGRTTIV-IAHR 590
Cdd:cd03223 113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1052-1255 |
1.49e-21 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 94.84 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQWLraqlgIVSQEPILFD- 1130
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI-------LEGKQITEPGPDRM-----VVFQNYSLLPw 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 CSIAENIAYGDNS-----RVVSQDEIVSAakaaniHPFIETLPHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQILLL 1205
Cdd:TIGR01184 69 LTVRENIALAVDRvlpdlSKSERRAIVEE------HIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1206 DEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNG 1255
Cdd:TIGR01184 139 DEPFGALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
394-589 |
1.57e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.54 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYlreiiG 473
Cdd:PRK11248 2 LQISHLYADYGGK---PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQ-EPVLFSTTIAENICYGrgnVTMDEIKKAVKEANAYEFIMKlpqkfdtlVGERGA------QLSGGQKQRIAIARA 546
Cdd:PRK11248 74 VVFQnEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAH 589
Cdd:PRK11248 143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
394-620 |
2.02e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.96 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANV--KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgqDI------RNFNV 465
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstsKQKEI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 NYLREIIGVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKE-----ANAYEFIMKLPqkfdtlvgergAQLSGG 536
Cdd:PRK13643 80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSH 614
Cdd:PRK13643 149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTP 228
|
....*.
gi 9961250 615 SELMKK 620
Cdd:PRK13643 229 SDVFQE 234
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
392-653 |
2.05e-21 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 95.69 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPdEGTINIDGQDIRNFNVNYLREI 471
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFSTTIAENI-CYGRGNvtMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLdPYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL--------------STVRNADVIAGF--EDGVIVEQGSH 614
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIeamlecqrflvieeNKVRQYDSIQKLlnEKSHFKQAISP 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 9961250 615 SELMKKEGVYFKLVNMQTSGSQIQSEEFELNDEKAATRM 653
Cdd:cd03289 237 SDRLKLFPRRNSSKSKRKPRPQIQALQEETEEEVQDTRL 275
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
394-613 |
2.14e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.78 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVK--------ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPDEGTINIDGQDIRNFNV 465
Cdd:PRK15134 276 LDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 NYL---REIIGVVSQEP---------VLfsTTIAENIcygrgNVTMDEIKKAVKEANAYEFIMKLpqKFDTLVGER-GAQ 532
Cdd:PRK15134 355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGL-----RVHQPTLSAAQREQQVIAVMEEV--GLDPETRHRyPAE 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAHRLSTVRNA--DVIAgFEDGVI 608
Cdd:PRK15134 426 FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQVIV-LRQGEV 504
|
....*
gi 9961250 609 VEQGS 613
Cdd:PRK15134 505 VEQGD 509
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
402-558 |
2.29e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 94.71 E-value: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 402 SYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTT----VQLIQrlydPDEGTINIDGQDIRNFNVnYLREI--IGVV 475
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTfymiVGLVK----PDSGRIFLDGEDITHLPM-HKRARlgIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 476 SQEPVLF-STTIAENIcygrgnvtmdeikKAVKEanayefIMKLP-----QKFDTLVGE---------RGAQLSGGQKQR 540
Cdd:COG1137 84 PQEASIFrKLTVEDNI-------------LAVLE------LRKLSkkereERLEELLEEfgithlrksKAYSLSGGERRR 144
|
170
....*....|....*...
gi 9961250 541 IAIARALVRNPKILLLDE 558
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
111-350 |
2.41e-21 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 95.84 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 111 EEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGD 190
Cdd:cd18784 33 DKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 191 KVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFG 270
Cdd:cd18784 113 NLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 271 GQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGNamtvFFSILIGAFSVGQA 350
Cdd:cd18784 193 NEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSC 268
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1051-1267 |
3.23e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILF- 1129
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVD-GKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFieTLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEAT 1209
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1210 SALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1267
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1266 |
3.65e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 95.54 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NITFnevVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV---FVDFGFQ--------- 1100
Cdd:PRK13651 7 NIVK---IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKkktkekekv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1101 ----LLDGQEAKKL-NVQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAanihpFIET--LPHKY 1171
Cdd:PRK13651 84 leklVIQKTRFKKIkKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIELvgLDESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1172 ETRvgdKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLI 1249
Cdd:PRK13651 159 LQR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRT 235
|
250
....*....|....*...
gi 9961250 1250 VVFQNGR-VKEHGTHQQL 1266
Cdd:PRK13651 236 IFFKDGKiIKDGDTYDIL 253
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1051-1257 |
3.81e-21 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 93.49 E-value: 3.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTvfvdFGFQLLDGQEAKKlnVQWLRaQLGIVSQEPILFD 1130
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTT----SGQILFNGQPRKP--DQFQK-CVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 C-SIAENIAYGDNSRV-VSQDEIVSAAKAAnihpfIETLPHKYETRVGDKG-TQLSGGQKQRIAIARALIRQPQILLLDE 1207
Cdd:cd03234 95 GlTVRETLTYTAILRLpRKSSDAIRKKRVE-----DVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1208 ATSALDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVFQNGRV 1257
Cdd:cd03234 170 PTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
394-591 |
4.35e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 98.54 E-value: 4.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDiRNFNVNYLREI-- 471
Cdd:PRK10762 5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKE-VTFNGPKSSQEag 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFST-TIAENICYGRGNVT-MDEI--KKAVKEANAYEFIMKLPQKFDTLVGErgaqLSGGQKQRIAIARAL 547
Cdd:PRK10762 81 IGIIHQELNLIPQlTIAENIFLGREFVNrFGRIdwKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 9961250 548 VRNPKILLLDEATSAL-DTESEA------EVQAaldkarEGRTTIVIAHRL 591
Cdd:PRK10762 157 SFESKVIIMDEPTDALtDTETESlfrvirELKS------QGRGIVYISHRL 201
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
144-364 |
5.64e-21 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 94.81 E-value: 5.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 144 RQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAI 223
Cdd:cd18551 66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 224 SPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGI 303
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 304 AFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANARGAA 364
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
394-620 |
5.65e-21 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.59 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSypsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI--QRLYDPDEGTINIDGQDIRNFNVN----- 466
Cdd:COG0396 1 LEIKNLHVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDerara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 467 -------YLREIIGV-VSQepvlFSTTIAENIcyGRGNVTMDEIKKAVKEANAyefIMKLPQKFdtlvGERG--AQLSGG 536
Cdd:COG0396 78 giflafqYPVEIPGVsVSN----FLRTALNAR--RGEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 537 QKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGS 613
Cdd:COG0396 145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
....*..
gi 9961250 614 hSELMKK 620
Cdd:COG0396 225 -KELALE 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1033-1213 |
7.56e-21 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 95.68 E-value: 7.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NITFNEVVFNYPtrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpLAGTVfvdfgfqLLDGQeakk 1109
Cdd:PRK11650 3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEI-------WIGGR---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 lnvqwlraqlgIVSQ-EPILFDC-------------SIAENIAYGDNSRVVSQDEI----VSAAKAANIHPFIETLPHky 1171
Cdd:PRK11650 67 -----------VVNElEPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIeervAEAARILELEPLLDRKPR-- 133
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9961250 1172 etrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALD 1213
Cdd:PRK11650 134 ---------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
711-968 |
7.63e-21 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 94.42 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQqkcnIFSLIFLFlgIISFFTFFLQGFTFGKAGEILTRRLRSM 790
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSSGGL----LALLVALF--LLQAVLSALSSYLLGRTGERVVLDLRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 791 AFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQgatgtrlALIAQNIANLGTGII-------ISFIYGWQLTLLLLAV 863
Cdd:cd18551 75 LWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTLAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 864 VPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSI 943
Cdd:cd18551 146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
|
250 260
....*....|....*....|....*
gi 9961250 944 SQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18551 226 MGLAVQLALLVVLGVGGARVASGAL 250
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
412-608 |
7.75e-21 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 92.88 E-value: 7.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQD---------------IRnfnvnylREIIGVVS 476
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlaqaspreilaLR-------RRTIGYVS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 477 QepvlFSTTI----AENIcygrgnVTMDEIKKAVKEANAYEFIMKLPQKFDtlVGERGAQL-----SGGQKQRIAIARAL 547
Cdd:COG4778 100 Q----FLRVIprvsALDV------VAEPLLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIV-IAHrlstvrNADVIAGFEDGVI 608
Cdd:COG4778 168 IADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH------DEEVREAVADRVV 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1050-1260 |
8.26e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 93.61 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEakklnVQWLRAQLGIVSQ-EPIL 1128
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI-------TLDGKP-----VEGPGAERGVVFQnEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1129 FDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1209 TSALDTESEKVVQEALDK--AREGRTCIVIAHrlsTIQNA-----DLIVVFQN-GRVKEH 1260
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKlwQETGKQVLLITH---DIEEAvfmatELVLLSPGpGRVVER 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1051-1259 |
8.27e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.60 E-value: 8.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV-FVDFGFQLLDGQEAKKL--NVQWL----------RA 1117
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVsWRGEPLAKLNRAQRKAFrrDIQMVfqdsisavnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1118 QLGIVSQEPI--LFDCSIAENIAygdnsRVvsqDEIVSAAKAANIHpfIETLPhkyetrvgdkgTQLSGGQKQRIAIARA 1195
Cdd:PRK10419 107 TVREIIREPLrhLLSLDKAERLA-----RA---SEMLRAVDLDDSV--LDKRP-----------PQLSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1196 LIRQPQILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKE 1259
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1034-1261 |
9.61e-21 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 91.89 E-value: 9.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQ 1113
Cdd:cd03268 1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD-------GKSYQKNIEA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WlrAQLGIVSQEPILFD-CSIAENIAYGDNSRVVSQdeivsaakaANIHPFIETLPHKYETRvgDKGTQLSGGQKQRIAI 1192
Cdd:cd03268 71 L--RRIGALIEAPGFYPnLTARENLRLLARLLGIRK---------KRIDEVLDVVGLKDSAK--KKVKGFSLGMKQRLGI 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1193 ARALIRQPQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1261
Cdd:cd03268 138 ALALLGNPDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1056-1270 |
9.91e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.72 E-value: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1056 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQwlRAQLGIVSQEPILFD-CSIA 1134
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLT-------LNGQDHTTTPPS--RRPVSMLFQENNLFShLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1135 ENIAYGDNS----RVVSQDEIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATS 1210
Cdd:PRK10771 90 QNIGLGLNPglklNAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1211 ALD----TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:PRK10771 159 ALDpalrQEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1056-1267 |
1.04e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.26 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1056 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGQEAKKLNVQwlRAQLGIVSQE-PILFDCSIA 1134
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISDAELREVR--RKKIAMVFQSfALMPHMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1135 ENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYETrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDT 1214
Cdd:PRK10070 125 DNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1215 ESEKVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLL 1267
Cdd:PRK10070 198 LIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1050-1253 |
1.24e-20 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.08 E-value: 1.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILF 1129
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTL-------LFEGEDISTLKPEIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRVVSQDEivsAAKAANIHPFieTLPhkyETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEAT 1209
Cdd:PRK10247 94 GDTVYDNLIFPWQIRNQQPDP---AIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961250 1210 SALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIVVFQ 1253
Cdd:PRK10247 166 SALDESNKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1043-1269 |
1.38e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1043 YPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIV 1122
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSV-------LIRGEPITKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 SQEP--ILFDCSIAENIAYGDNSRVVSQDEIV----SAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARAL 1196
Cdd:PRK13652 84 FQNPddQIFSPTVEQDIAFGPINLGLDEETVAhrvsSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1197 IRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1051-1238 |
1.39e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 92.60 E-value: 1.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGTVFVdFGFQLLdgqeAKKLNVQWLRAQLGIVSQE 1125
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRL-FGRNIY----SPDVDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILF-DCSIAENIAYGD--NSRVVSQ---DEIVSAA--KAAnihpfietLPHKYETRVGDKGTQLSGGQKQRIAIARALI 1197
Cdd:PRK14267 94 PNPFpHLTIYDNVAIGVklNGLVKSKkelDERVEWAlkKAA--------LWDEVKDRLNDYPSNLSGGQRQRLVIARALA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9961250 1198 RQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1238
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
703-1282 |
2.40e-20 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.12 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 703 LNKTEWPYFVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAvkqqkcnifsliflFLGIISFFTFFLqGFTFGKAGEI 782
Cdd:PLN03232 295 LNNSLGGRFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDPA--------------WVGYVYAFLIFF-GVTFGVLCES 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 783 --------LTRRLRSMAFKAMLRQDMSWFDD-HKN-STGALSTRLATDAAQVQgatgtrlaLIAQNIANLGTG---IIIS 849
Cdd:PLN03232 360 qyfqnvgrVGFRLRSTLVAAIFHKSLRLTHEaRKNfASGKVTNMITTDANALQ--------QIAEQLHGLWSApfrIIVS 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 850 FIYGWQL--------TLLLLAVVPIIAVsgivemkLLAGNAKRDKKELEAAGK---IATEAIENIRTVVSLTQERKFESM 918
Cdd:PLN03232 432 MVLLYQQlgvaslfgSLILFLLIPLQTL-------IVRKMRKLTKEGLQWTDKrvgIINEILASMDTVKCYAWEKSFESR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 919 yVEKLYGPYRNSVQKAHIygitFSISQAFMYFS---YAGCFRFGAYLIVNGHM---RFRDVILVFSAIVFGAVALGHASS 992
Cdd:PLN03232 505 -IQGIRNEELSWFRKAQL----LSAFNSFILNSipvVVTLVSFGVFVLLGGDLtpaRAFTSLSLFAVLRSPLNMLPNLLS 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 993 FAPDyAKAKLSAAHLFMLFERQPLIDSYSEEGLKPdkfegNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSG 1072
Cdd:PLN03232 580 QVVN-ANVSLQRIEELLLSEERILAQNPPLQPGAP-----AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTG 653
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1073 CGKSTVVQLLERFYDPLAGTVFVdfgfqlldgqeakklnvqwLRAQLGIVSQEPILFDCSIAENIAYGDNsrvVSQDEIV 1152
Cdd:PLN03232 654 EGKTSLISAMLGELSHAETSSVV-------------------IRGSVAYVPQVSWIFNATVRENILFGSD---FESERYW 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1153 SAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTE-SEKVVQEALDKAREGR 1231
Cdd:PLN03232 712 RAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGK 791
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1232 TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQlLAQKGIYFSMVSVQAG 1282
Cdd:PLN03232 792 TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1047-1270 |
3.12e-20 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 91.61 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1047 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEP 1126
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTV-------FLGDKPISMLSSRQLARRLALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 IL-FDCSIAENIAYGDN------SRVVSQDE-IVSAAKAANihpFIETLPHKyetRVgdkgTQLSGGQKQRIAIARALIR 1198
Cdd:PRK11231 86 LTpEGITVRELVAYGRSpwlslwGRLSAEDNaRVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1199 QPQILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:PRK11231 156 DTPVVLLDEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1045-1267 |
3.14e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 3.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQ 1124
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTV-------LVAGDDVEALSARAASRRVASVPQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 EPIL-FDCSIAENIAYGDN---SRVVSQDEIVSAAKAanihpfiETLPHKYETRVGDKG-TQLSGGQKQRIAIARALIRQ 1199
Cdd:PRK09536 85 DTSLsFEFDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1200 PQILLLDEATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1267
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
711-968 |
4.02e-20 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 92.10 E-value: 4.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIaifgpgdDAVKQQKcNIFSLIFLFLGIISFFTF-----FLQGFTFGKAGEILTR 785
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLL-------DDIFVEK-DLEALLLVPLAIIGLFLLrglasYLQTYLMAYVGQRVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 786 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVP 865
Cdd:cd18552 73 DLRNDLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 866 IIAVSGIVEMKLLagnAKRDKKELEAAGKIAT---EAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFS 942
Cdd:cd18552 151 LAALPIRRIGKRL---RKISRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSP 227
|
250 260
....*....|....*....|....*.
gi 9961250 943 ISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18552 228 LMELLGAIAIALVLWYGGYQVISGEL 253
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
394-621 |
4.22e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.56 E-value: 4.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:PRK13537 8 IDFRNVEKRYGDKL---VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQ----EPvlfSTTIAENI-CYGRG-NVTMDEIKKAVkeANAYEFiMKLPQKFDTLVGErgaqLSGGQKQRIAIARAL 547
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLlVFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
405-612 |
4.32e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.14 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVL-FS 483
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 484 TTIAENICYGRGN-----VTMDEI-KKAVKEA-NAYEFIMKLPQKFDTlvgergaqLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK09536 92 FDVRQVVEMGRTPhrsrfDTWTETdRAAVERAmERTGVAQFADRPVTS--------LSGGERQRVLLARALAQATPVLLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 557 DEATSALDTESEAE-VQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQG 612
Cdd:PRK09536 164 DEPTASLDINHQVRtLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1030-1268 |
4.55e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 91.70 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1030 FEGNITFNEVVFNYPTRAnvpvlqglslevkkgqTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfGFQLLDGQEA-K 1108
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYS--GDVLLGGRSIfN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1109 KLNVQWLRAQLGIVSQEPILFDCSIAENIAYGDNS-RVVSQDEIVSAAKAAnihpFIET-LPHKYETRVGDKGTQLSGGQ 1186
Cdd:PRK14271 93 YRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAhKLVPRKEFRGVAQAR----LTEVgLWDAVKDRLSDSPFRLSGGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1187 KQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQ 1265
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQ 248
|
...
gi 9961250 1266 LLA 1268
Cdd:PRK14271 249 LFS 251
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
382-621 |
4.55e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.39 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 382 ERGHKPDSIkgnLEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIR 461
Cdd:PRK10575 3 EYTNHSDTT---FALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 462 NFNVN-YLREIIGVVSQEPVLFSTTIAENICYGR-------GNVTMDEIKKaVKEANAYEFIMKLPQKfdtLVGergaQL 533
Cdd:PRK10575 77 SWSSKaFARKVAYLPQQLPAAEGMTVRELVAIGRypwhgalGRFGAADREK-VEEAISLVGLKPLAHR---LVD----SL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 534 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-ARE-GRTTIVIAHRLS-TVRNADVIAGFEDGVIVE 610
Cdd:PRK10575 149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIA 228
|
250
....*....|.
gi 9961250 611 QGSHSELMKKE 621
Cdd:PRK10575 229 QGTPAELMRGE 239
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
394-610 |
4.94e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.36 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNV-NYLREII 472
Cdd:PRK11288 5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQE----PVLfstTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFD--TLVGErgaqLSGGQKQRIAIARA 546
Cdd:PRK11288 82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 547 LVRNPKILLLDEATSALdTESEAEVQAALDKA--REGRTTIVIAHRLSTV-RNADVIAGFEDGVIVE 610
Cdd:PRK11288 155 LARNARVIAFDEPTSSL-SAREIEQLFRVIRElrAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1033-1257 |
5.13e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 95.09 E-value: 5.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NIT--FNEVVfnyptrANvpvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEakkl 1110
Cdd:COG3845 10 GITkrFGGVV------AN----DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID-------GKP---- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1111 nVQW------LRAQLGIVSQEPILFDC-SIAENIAYGDNSRvvsQDEIVSAAKAANIhpfIETLPHKY------ETRVGD 1177
Cdd:COG3845 69 -VRIrsprdaIALGIGMVHQHFMLVPNlTVAENIVLGLEPT---KGGRLDRKAARAR---IRELSERYgldvdpDAKVED 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1178 kgtqLSGGQKQRIAIARALIRQPQILLLDEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQN 1254
Cdd:COG3845 142 ----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRR 216
|
...
gi 9961250 1255 GRV 1257
Cdd:COG3845 217 GKV 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
394-623 |
5.16e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 91.61 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ--DIRNFNVNYLREI 471
Cdd:PRK13638 2 LATSDLWFRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEP--VLFSTTIAENICYGRGN--VTMDEIKKAVKEANayefimklpqkfdTLVGERGAQ------LSGGQKQRI 541
Cdd:PRK13638 79 VATVFQDPeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 542 AIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG------S 613
Cdd:PRK13638 146 AIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGapgevfA 225
|
250
....*....|
gi 9961250 614 HSELMKKEGV 623
Cdd:PRK13638 226 CTEAMEQAGL 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1043-1252 |
5.64e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1043 YPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGfqlldgqeakklnvqwlrAQLGIV 1122
Cdd:NF040873 2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG------------------ARVAYV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 SQ---EPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPF----IETLPHKyetRVGDkgtqLSGGQKQRIAIARA 1195
Cdd:NF040873 61 PQrseVPDSLPLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALervgLADLAGR---QLGE----LSGGQRQRALLAQG 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1196 LIRQPQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVF 1252
Cdd:NF040873 134 LAQEADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
409-606 |
5.85e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 95.00 E-value: 5.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD---EGTINIDGQDIRNFNVnylREI----IGVVSQEPVL 481
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNI---RDTeragIAIIHQELAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 482 FST-TIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK13549 94 VKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961250 561 SALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 606
Cdd:PRK13549 172 ASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1042-1270 |
7.46e-20 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 91.46 E-value: 7.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1042 NYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldgqeakklnvqwlrAQLGI 1121
Cdd:cd03291 44 NLCLVGA-PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS--------------------GRISF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 VSQEPILFDCSIAENIAYGdnsrvVSQDEI--VSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQ 1199
Cdd:cd03291 103 SSQFSWIMPGTIKENIIFG-----VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1200 PQILLLDEATSALDTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:cd03291 178 ADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1050-1269 |
8.52e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 94.77 E-value: 8.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLerfydPLAGTVFVDfGFQLLDGQEAKKLNVQWLRA----QLGI 1121
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSPPVVYPS-GDIRFHGESLLHASEQTLRGvrgnKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 VSQEPIL-------FDCSIAENIA-YGDNSRVVSQDEIVSAAKAANIHpfietlphKYETRVGDKGTQLSGGQKQRIAIA 1193
Cdd:PRK15134 97 IFQEPMVslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
394-610 |
8.87e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIdGQDIRnfnvnylreiIG 473
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVLF--STTIAENICYGRGNVTmdeikkaVKEANAYefimkL------PQKFDTLVGErgaqLSGGQKQRIAIAR 545
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGT-------EQEVRGY-----LgrflfsGDDAFKPVGV----LSGGEKARLALAK 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 546 ALVRNPKILLLDEATSALDTESEAEVQAALDkAREGrTTIVIAH-R--LSTVrnADVIAGFEDGVIVE 610
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1050-1268 |
1.20e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 89.52 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTvvqlleRFYdPLAGTVFVDFGFQLLDGQEAKKLNVqWLRAQLGI--VSQEPI 1127
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTT------TFY-MIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIAYGDNSRVVSQDEIVSAAKAAnIHPF-IETLPHKyetrvgdKGTQLSGGQKQRIAIARALIRQPQILLL 1205
Cdd:cd03218 86 IFrKLTVEENILAVLEIRGLSKKEREEKLEEL-LEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1206 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
406-618 |
1.68e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 93.71 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTIN-------IDGQDIRNFNVNYLREIIGVVSQE 478
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 479 PVLFS-TTIAENICYGRGNVTMDEI--KKAV--------KEANAYEFIMKLPQkfdtlvgergaQLSGGQKQRIAIARAL 547
Cdd:TIGR03269 374 YDLYPhRTVLDNLTEAIGLELPDELarMKAVitlkmvgfDEEKAEEILDKYPD-----------ELSEGERHRVALAQVL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:TIGR03269 443 IKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIV 516
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
1051-1278 |
1.74e-19 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 1.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqlldgqeakklnvqWLRAQLGIVSQEPILFD 1130
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV--------------------WAERSIAYVPQQAWIMN 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 CSIAENIAYGDNSRvvsQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATS 1210
Cdd:PTZ00243 735 ATVRGNILFFDEED---AARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1211 ALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQlLAQKGIYFSMVS 1278
Cdd:PTZ00243 812 ALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAA 879
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1051-1268 |
1.97e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.62 E-value: 1.97e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqllDGQEAKKLNVQWL---RAQLGIVSQEP- 1126
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWF--------DGQPLHNLNRRQLlpvRHRIQVVFQDPn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 --ILFDCSIAENIAYG------DNSRVVSQDEIVSAAKAANIHPfieTLPHKYETrvgdkgtQLSGGQKQRIAIARALIR 1198
Cdd:PRK15134 373 ssLNPRLNVLQIIEEGlrvhqpTLSAAQREQQVIAVMEEVGLDP---ETRHRYPA-------EFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1199 QPQILLLDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:PRK15134 443 KPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
394-621 |
2.22e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 91.05 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfNVNYLREIIG 473
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPVL-FSTTIAEN-ICYGR-GNVTMDEIKKAVkeANAYEFiMKLPQKFDTLVgergAQLSGGQKQRIAIARALVRN 550
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENlLVFGRyFGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1034-1270 |
2.90e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 89.84 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfQLLDGQEAKKLN 1111
Cdd:PRK13646 3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD---DITITHKTKDKY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 VQWLRAQLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQDEIVSAAkaanihpFIETLPHKYETRVGDKGT-QLSGGQKQ 1188
Cdd:PRK13646 80 IRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-------HRLLMDLGFSRDVMSQSPfQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1189 RIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQ 1265
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKE 232
|
....*
gi 9961250 1266 LLAQK 1270
Cdd:PRK13646 233 LFKDK 237
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
103-342 |
4.35e-19 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 89.39 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 103 LNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQvSFWTLAAGRQI-RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDI 181
Cdd:cd18541 29 LTAGTLTASQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 182 SKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKI-----------LSAFSDKelaaya 250
Cdd:cd18541 108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKihkrfrkvqeaFSDLSDR------ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 251 kagavAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTI 330
Cdd:cd18541 182 -----VQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITL 256
|
250
....*....|....
gi 9961250 331 GN--AMTVFFSILI 342
Cdd:cd18541 257 GDlvAFNSYLGMLI 270
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
394-620 |
5.20e-19 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 86.43 E-value: 5.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSypsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRL--YDPDEGTINIDGQDIRNFNVN-YLRE 470
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEeRARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFSttiaenicygrgNVTMDEIKKAVKEAnayefimklpqkfdtlvgergaqLSGGQKQRIAIARALVRN 550
Cdd:cd03217 78 GIFLAFQYPPEIP------------GVKNADFLRYVNEG-----------------------FSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGSHS---ELMKK 620
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElalEIEKK 198
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1034-1239 |
5.61e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 85.28 E-value: 5.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNypTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLLdgqeakklnvq 1113
Cdd:cd03223 1 IELENLSLA--TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLL----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wlraqlgIVSQEPILFDCSIAENIAYgdnsrvvsqdeivsaakaanihPFietlphkyetrvgdkGTQLSGGQKQRIAIA 1193
Cdd:cd03223 68 -------FLPQRPYLPLGTLREQLIY----------------------PW---------------DDVLSGGEQQRLAFA 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1239
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1048-1261 |
5.94e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.47 E-value: 5.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfGFQLLDGQEAKKLNVqwlraqlGIVSQEPI 1127
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI--GEKRMNDVPPAERGV-------GMVFQSYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIAYGDNSRVVSQDEIvsaAKAANIHPFIETLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:PRK11000 86 LYpHLSVAENMSFGLKLAGAKKEEI---NQRVNQVAEVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1207 EATSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHG 1261
Cdd:PRK11000 159 EPLSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
392-591 |
6.20e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 93.44 E-value: 6.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 392 GNLEFNDVHFSYPSRANvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDpDEGTINIDGQDIRNFNVNYLREI 471
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFSTTIAENI-CYGRgnVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRN 550
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLdPYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSK 1371
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 591
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
389-627 |
6.61e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.53 E-value: 6.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 389 SIKGNLEFNDVHFSYPSRA--NVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEG-TINIDGQDIRNFN- 464
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLKk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 465 ---VNYLREIIGVVSQEP--VLFSTTIAENICYGRGNVTMD--EIKKAVKEanayefIMKLPQKFDTLVGERGAQLSGGQ 537
Cdd:PRK13645 82 ikeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENkqEAYKKVPE------LLKLVQLPEDYVKRSPFELSGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSH 614
Cdd:PRK13645 156 KRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSP 235
|
250
....*....|...
gi 9961250 615 SELMKKEGVYFKL 627
Cdd:PRK13645 236 FEIFSNQELLTKI 248
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
394-618 |
6.76e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 87.97 E-value: 6.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAN------VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNY 467
Cdd:COG4167 5 LEVRNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 468 LREIIGVVSQEPvlfSTTIAENICYG-------RGNVTMDEIKKavkeanaYEFImklpqkFDTL--VGERGAQ------ 532
Cdd:COG4167 85 RCKHIRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEER-------EERI------FATLrlVGLLPEHanfyph 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 533 -LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------EVQaaldkAREGRTTIVIAHRLSTVRN-ADVIAGF 603
Cdd:COG4167 149 mLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqiinlmlELQ-----EKLGISYIYVSQHLGIVKHiSDKVLVM 223
|
250
....*....|....*
gi 9961250 604 EDGVIVEQGSHSELM 618
Cdd:COG4167 224 HQGEVVEYGKTAEVF 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
411-621 |
8.54e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.73 E-value: 8.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVL-FSTTIAEN 489
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 490 ICYGRG------NVTMDEIKKAVKEANAYEFIMKLP-QKFDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK10253 102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 563 LDTESEAEVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK10253 174 LDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAE 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1051-1262 |
1.23e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQW---LRAQ-LGIVSQ-E 1125
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-------IFNGQPMSKLSSAAkaeLRNQkLGFIYQfH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILFDCSIAENIAY----GDNSRVVSQDEIVSAAKAANIhpfietlphkyETRVGDKGTQLSGGQKQRIAIARALIRQPQ 1201
Cdd:PRK11629 97 HLLPDFTALENVAMplliGKKKPAEINSRALEMLAAVGL-----------EHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1202 ILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1262
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1050-1270 |
1.24e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 88.73 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfqlLDGQEAKKlnVQWLRAQLGIVSQepilF 1129
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV------LGVPVPAR--ARLARARIGVVPQ----F 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 D-----CSIAEN-IAYGDNSRVvSQDEIvsaakAANIHPFIE--TLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQ 1201
Cdd:PRK13536 123 DnldleFTVRENlLVFGRYFGM-STREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1202 ILLLDEATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1270
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
411-617 |
1.95e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD------EGTINIDGQDIRNFNVNYLREI----IGVVSQEPV 480
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 481 L-------FSTTIAENICYGRGnvtMDeikkavKEANAYEFIMKLPQkfdtlVGERGA---------QLSGGQKQRIAIA 544
Cdd:PRK15134 103 VslnplhtLEKQLYEVLSLHRG---MR------REAARGEILNCLDR-----VGIRQAakrltdyphQLSGGERQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
409-647 |
2.04e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 90.23 E-value: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-IGVVSQE-PVLFSTTI 486
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENICYGR------GNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK09700 98 LENLYIGRhltkkvCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 561 SALdTESEAE-VQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKEgvyfkLVNMQTsGSQI 637
Cdd:PRK09700 174 SSL-TNKEVDyLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDD-----IVRLMV-GREL 246
|
250
....*....|
gi 9961250 638 QSEEFELNDE 647
Cdd:PRK09700 247 QNRFNAMKEN 256
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1051-1257 |
2.16e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.27 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----LAGTVfvdfgfQLLDGQEAKKLNVQWLRaqlgivsqe 1125
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTA------PLAEAREDTRLMFQDAR--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 pILFDCSIAENIAYG--DNSRvvsqDEIVSAAKAANIhpfietlphkyETRVGDKGTQLSGGQKQRIAIARALIRQPQIL 1203
Cdd:PRK11247 92 -LLPWKKVIDNVGLGlkGQWR----DAALQALAAVGL-----------ADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1204 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRV 1257
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1051-1268 |
2.62e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 87.17 E-value: 2.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfQLLDgqEAKKLNVQWLRAQLGIVSQ----EP 1126
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSI------SLCG--EPVPSRARHARQRVGVVPQfdnlDP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ilfDCSIAENIaygdnsRVVSQDEIVSAAKA-ANIHPFIE--TLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQIL 1203
Cdd:PRK13537 94 ---DFTVRENL------LVFGRYFGLSAAAArALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1204 LLDEATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
410-623 |
3.33e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 85.33 E-value: 3.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN-YLREIIGVVSQEPVLFST-TIA 487
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 488 ENIcygrgnVTMDEIKKAVKEANAYEFIMKLPQKFDT--LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:PRK10895 97 DNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 566 ESEAEVQAALDKARE-GRTTIVIAHR----LSTVRNADVIAgfeDGVIVEQGSHSELMKKEGV 623
Cdd:PRK10895 171 ISVIDIKRIIEHLRDsGLGVLITDHNvretLAVCERAYIVS---QGHLIAHGTPTEILQDEHV 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
378-641 |
3.70e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 91.23 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 378 DSFSERGHkPDSIKGNLEFNDVHFSYPS-RANVKilkGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINID 456
Cdd:TIGR01257 915 DSFFEREL-PGLVPGVCVKNLVKIFEPSgRPAVD---RLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG 990
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 457 GQDIRNfNVNYLREIIGVVSQEPVLFS-TTIAENICYgrgnvtMDEIK-KAVKEANAYEFIMKLPQKFDTLVGERGAQLS 534
Cdd:TIGR01257 991 GKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF------YAQLKgRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLS 1063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 535 GGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLStvrNADVIAgfEDGVIVEQG-- 612
Cdd:TIGR01257 1064 GGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQGrl 1138
|
250 260 270
....*....|....*....|....*....|....*.
gi 9961250 613 --SHSELMKKE----GVYFKLV-NMQTSGSQIQSEE 641
Cdd:TIGR01257 1139 ycSGTPLFLKNcfgtGFYLTLVrKMKNIQSQRGGCE 1174
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1051-1262 |
4.08e-18 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 84.88 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWlRAQLGI--VSQEPIL 1128
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSI-------RLDGEDITKLPPHE-RARAGIayVPQGREI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1129 F-DCSIAENIAYGDNSRvvsqdeivsAAKAANIHPFIETL-PHKYETRvGDKGTQLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:TIGR03410 87 FpRLTVEENLLTGLAAL---------PRRSRKIPDEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1207 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGT 1262
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1046-1269 |
4.33e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.48 E-value: 4.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1046 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLLDGQEAKKLNVQWLRAQLGIVSQE 1125
Cdd:TIGR03269 294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPDGRGRAKRYIGILHQE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILF-DCSIAENIaygdnSRVVSQDEIVSAAKAANIHPFIET-LPHKYETRVGDKGT-QLSGGQKQRIAIARALIRQPQI 1202
Cdd:TIGR03269 374 YDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRI 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1203 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:TIGR03269 449 VILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1048-1262 |
4.69e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 85.12 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPLAGTVfvdfgfqLLDGQEAKKLNVQwLRAQLGI-VS 1123
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSI-------LLDGEDILELSPD-ERARAGIfLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 -QEPI----------LfdcSIAENIAYGDNSRVV-SQDEIVSAAKAANihpfietLPHKYETR---VGdkgtqLSGGQKQ 1188
Cdd:COG0396 83 fQYPVeipgvsvsnfL---RTALNARRGEELSAReFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1189 RIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGRVKEHGT 1262
Cdd:COG0396 148 RNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
400-612 |
4.80e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 84.51 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 400 HFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNylreiigvVSQEP 479
Cdd:cd03220 26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG--------GGFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 480 VLfstTIAENIcYGRG---NVTMDEIKKavKEANAYEFiMKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLL 556
Cdd:cd03220 98 EL---TGRENI-YLNGrllGLSRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 557 DEATSALDTESEAEVQAALDKAREGRTTIVIA-HRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:cd03220 167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1052-1266 |
5.07e-18 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 84.34 E-value: 5.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdFGFQLLdgQEAKKLnvqwlRAQLGIVSQEPILFDC 1131
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV-AGHDVV--REPREV-----RRRIGIVFQDLSVDDE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1132 SIA-ENIA-----YGDNSRVVSQdeivsaaKAANIHPFIEtLPHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQILLL 1205
Cdd:cd03265 88 LTGwENLYiharlYGVPGAERRE-------RIDELLDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1206 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQL 1266
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1049-1269 |
5.15e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.81 E-value: 5.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQ-WLRAQLGIVSQEPI 1127
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI-------LIDGQEMRFASTTaALAAGVAIIYQELH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIAYGD--NSR-VVSQDEIVSAAKAANIHPFIETLPhkyETRVGDkgtqLSGGQKQRIAIARALIRQPQIL 1203
Cdd:PRK11288 90 LVpEMTVAENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1204 LLDEATSALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNGR-VKEHG-----THQQLLAQ 1269
Cdd:PRK11288 163 AFDEPTSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRyVATFDdmaqvDRDQLVQA 236
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1054-1266 |
5.43e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 86.68 E-value: 5.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1054 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfVDFGFQLLDGQEakklnVQWL--RAQLGIVSQEPILF-- 1129
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEV-AWLGKDLLGMKD-----DEWRavRSDIQMIFQDPLASln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 -DCSIAENIA------YGDNSRVVSQDEIVSAAKAANIHP-FIETLPHKYetrvgdkgtqlSGGQKQRIAIARALIRQPQ 1201
Cdd:PRK15079 113 pRMTIGEIIAeplrtyHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEF-----------SGGQCQRIGIARALILEPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1202 ILLLDEATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1266
Cdd:PRK15079 182 LIICDEPVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1036-1238 |
5.68e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 5.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1036 FNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGfqlldgqeakklnvqwl 1115
Cdd:COG0488 1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1116 rAQLGIVSQEPILFD-CSIAENIAYGDNSRVVSQDEIVSA-----------AKAANIHPFIETL-PHKYETRVGD--KG- 1179
Cdd:COG0488 61 -LRIGYLPQEPPLDDdLTVLDTVLDGDAELRALEAELEELeaklaepdedlERLAELQEEFEALgGWEAEARAEEilSGl 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1180 -----------TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH 1238
Cdd:COG0488 140 gfpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1049-1256 |
6.17e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 88.83 E-value: 6.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPlAGTVFvdfGFQLLDGQEAKKLNVQWL-RAQLGIVSQEPI 1127
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-P-HGTYE---GEIIFEGEELQASNIRDTeRAGIAIIHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIAYGD---NSRVVSQDEIVSAAKA------ANIHPfietlphkyETRVGDkgtqLSGGQKQRIAIARALI 1197
Cdd:PRK13549 93 LVkELSVLENIFLGNeitPGGIMDYDAMYLRAQKllaqlkLDINP---------ATPVGN----LGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1198 RQPQILLLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1256
Cdd:PRK13549 160 KQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
394-606 |
8.48e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 81.34 E-value: 8.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgqdiRNFNVNYLreiig 473
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 vvsqepvlfsttiaenicygrgnvtmdeikkavkeanayefimklpqkfdtlvgergAQLSGGQKQRIAIARALVRNPKI 553
Cdd:cd03221 69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 554 LLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH-R--LSTVrnADVIAGFEDG 606
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHdRyfLDQV--ATKIIELEDG 143
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1050-1268 |
1.14e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQ--EAKKLNVQWLRAQLGIVSQEP- 1126
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAV-------LWQGKplDYSKRGLLALRQQVATVFQDPe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 -ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAAnihpfiETLPHKYETRvgDKGTQ-LSGGQKQRIAIARALIRQPQILL 1204
Cdd:PRK13638 88 qQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEA------LTLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1205 LDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1268
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
409-564 |
1.31e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.29 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVN---YLR-EIIGVVSQEPVLFST 484
Cdd:PRK10584 23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 485 TIAenicygRGNVTMDEIKKAVKEANAYEFIMKLPQKFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:PRK10584 103 LNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
....
gi 9961250 561 SALD 564
Cdd:PRK10584 175 GNLD 178
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1051-1257 |
1.49e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 81.71 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNV-QWLRAQLGIVSQEP--- 1126
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI-------TLDGKPVTRRSPrDAIRAGIAYVPEDRkre 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 -ILFDCSIAENIAygdnsrvvsqdeivsaakaanihpfietLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQPQILLL 1205
Cdd:cd03215 88 gLVLDLSVAENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1206 DEATSALDTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVFQNGRV 1257
Cdd:cd03215 129 DEPTRGVDVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1049-1257 |
1.56e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 88.24 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQWL----RAQLGIVSQ 1124
Cdd:PRK10535 21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA-------GQDVATLDADALaqlrREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 E-PILFDCSIAENI----AYGDNSRvvsqdeivsAAKAANIHPFIETLphKYETRVGDKGTQLSGGQKQRIAIARALIRQ 1199
Cdd:PRK10535 94 RyHLLSHLTAAQNVevpaVYAGLER---------KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1200 PQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1257
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1052-1284 |
1.67e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.91 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTvvqLLERFYDPLAGTVFVDFGFQLLDG--QEAKKL--NVQWLRAQLGIVSQEPI 1127
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKST---LLRHLSGLITGDKSAGSHIELLGRtvQREGRLarDIRKSRANTGYIFQQFN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LFD-CSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLphkyeTRVG------DKGTQLSGGQKQRIAIARALIRQP 1200
Cdd:PRK09984 97 LVNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1201 QILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK--GIYFS 1275
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfdHLYRS 251
|
....*....
gi 9961250 1276 MVSVQAGTQ 1284
Cdd:PRK09984 252 INRVEENAK 260
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
394-623 |
1.68e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.39 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNF-NVNYLREII 472
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEPVLFS-TTIAENICYGRGNVTMDEIKKAVKEAnaYEFIMKLPQKfdtlVGERGAQLSGGQKQRIAIARALVRNP 551
Cdd:PRK11614 83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 552 KILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS--TVRNADVIAGFEDGVIVEQGSHSELMKKEGV 623
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1034-1260 |
1.76e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 87.43 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfqlldGQeakklNVQ 1113
Cdd:COG0488 316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--------GE-----TVK 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wlraqLGIVSQEPILFDcsiaeniaygDNSRVVsqDEIVSAAKAANIHPFIETL------PHKYETRVGDkgtqLSGGQK 1187
Cdd:COG0488 380 -----IGYFDQHQEELD----------PDKTVL--DELRDGAPGGTEQEVRGYLgrflfsGDDAFKPVGV----LSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVFQNGRVKEH 1260
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
411-592 |
1.79e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ-----------DIRNfnvnylREiIGVVSQ-E 478
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQpmsklssaakaELRN------QK-LGFIYQfH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 479 PVLFSTTIAEnicygrgNVTMDEI--KKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK11629 97 HLLPDFTALE-------NVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 9961250 557 DEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLS 592
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
398-617 |
1.82e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.99 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 398 DVHFSYPSRANVKILKGLNLKVQSGQT---------VALVGSSGCGKSTTVQLIQRLYDP-----DEGTINIDGQDIRNF 463
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGFAGKTVLDQVsmgfparavTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 464 -NVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQRIA 542
Cdd:PRK14271 94 rDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLC 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 543 IARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1052-1263 |
2.06e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.62 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgFQLLDGQEAKKLNVQWLRAQLGIVSQEP-ILFD 1130
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIW----FSGHDITRLKNREVPFLRRQIGMIFQDHhLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 CSIAENIAYgdnsrvvsqDEIVSAAKAANIHPFIETLPHKyetrVG--DKG----TQLSGGQKQRIAIARALIRQPQILL 1204
Cdd:PRK10908 94 RTVYDNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1205 LDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVFQNGRVkeHGTH 1263
Cdd:PRK10908 161 ADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
422-612 |
2.63e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.22 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 422 GQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN---VNYLREIIGVVSQEPVLfSTTIAENICYGrgnvT 498
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYA-SLDPRQTVGDS----I 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 499 MDEIK-------KAVKEANAY---------EFIMKLPQKFdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK10261 425 MEPLRvhgllpgKAAAARVAWllervgllpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 9961250 563 LDTESEAE-VQAALDKARE-GRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQG 612
Cdd:PRK10261 494 LDVSIRGQiINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
386-609 |
2.71e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 82.77 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 386 KPDSIKGNLEfndvHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNV 465
Cdd:cd03267 15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 NYLREIIGVVSQE-------PVLFSTTIAENIcYgrgNVTMDEIKKAVKEANAyefIMKLPQKFDTLVgergAQLSGGQK 538
Cdd:cd03267 91 KFLRRIGVVFGQKtqlwwdlPVIDSFYLLAAI-Y---DLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 539 QRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA-REGRTTIVIahrlsTVRNADVIAGFEDGVIV 609
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL-----TSHYMKDIEALARRVLV 226
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
399-594 |
2.85e-17 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 82.23 E-value: 2.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 399 VHFSYPSRANV---KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI---RNFNVNYLREII 472
Cdd:PRK10908 2 IRFEHVSKAYLggrQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEP-VLFSTTIAENICYGR--GNVTMDEIKKAVKEANAYEFIMKLPQKFDTlvgergaQLSGGQKQRIAIARALVR 549
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 9961250 550 NPKILLLDEATSALDTE-SEAEVQAALDKAREGRTTIVIAHRLSTV 594
Cdd:PRK10908 155 KPAVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1055-1269 |
2.88e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 83.35 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1055 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWlRAQLgI--VSQEPilfdcs 1132
Cdd:COG4167 32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEI-------LINGHKLEYGDYKY-RCKH-IrmIFQDP------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1133 iaeNIAYGDNSRVVSQDEI--------VSAAKAANIhpfIETLphkyeTRVG-------DKGTQLSGGQKQRIAIARALI 1197
Cdd:COG4167 97 ---NTSLNPRLNIGQILEEplrlntdlTAEEREERI---FATL-----RLVGllpehanFYPHMLSSGQKQRVALARALI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1198 RQPQILLLDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:COG4167 166 LQPKIIIADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1030-1269 |
3.34e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.52 E-value: 3.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1030 FEGNITFNEVVFNYPTRA--NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfGFQLLDGQEA 1107
Cdd:PRK13645 3 FSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV--GDYAIPANLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1108 KKLNVQWLRAQLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQDEIVSaaKAANIHPFIEtLPHKYETRvgdKGTQLSGG 1185
Cdd:PRK13645 81 KIKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK--KVPELLKLVQ-LPEDYVKR---SPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1186 QKQRIAIARALIRQPQILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG 1261
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
|
250
....*....|....
gi 9961250 1262 ------THQQLLAQ 1269
Cdd:PRK13645 234 spfeifSNQELLTK 247
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
415-618 |
3.86e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.54 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 415 LNLKVQ-----SGQTvALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ---DIRNfNVN---YLREIiGVVSQEPVLFS 483
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK-GIClppEKRRI-GYVFQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 484 -TTIAENICYGrgnvtMDEikkavkeanayefimKLPQKFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKI 553
Cdd:PRK11144 90 hYKVRGNLRYG-----MAK---------------SMVAQFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 554 LLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFEDGVIVEQGS-----HSELM 618
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPleevwASSAM 222
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
412-606 |
1.41e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 79.01 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-IGVVSQEP----VLFSTTI 486
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENIcygrgnvtmdeikkavkeanayefimklpqkfdTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 566
Cdd:cd03215 96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9961250 567 SEAEVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFEDG 606
Cdd:cd03215 139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
753-912 |
1.79e-16 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 81.38 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 753 IFSLIFLFLGIISFFTFFLqgftFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 832
Cdd:cd18575 41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 833 ALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIV---EMKLLAGNAkRDKkeLEAAGKIATEAIENIRTVVSL 909
Cdd:cd18575 115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
|
...
gi 9961250 910 TQE 912
Cdd:cd18575 192 TRE 194
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
406-588 |
1.97e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.53 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVnylREIIGVVSQ----EPVL 481
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDV---AEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 482 fstTIAENI-----CYGRGNVTMDEIKKAVKEANayefIMKLPQKFdtlvgergaqLSGGQKQRIAIARALVRNPKILLL 556
Cdd:PRK13539 89 ---TVAENLefwaaFLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|..
gi 9961250 557 DEATSALDTESEAEVqAALDKAREGRTTIVIA 588
Cdd:PRK13539 152 DEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1049-1256 |
2.15e-16 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.72 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDplAGTVFVDFGFqllDGQEAKKLNVQWL-RAQLGIVSQEPI 1127
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYP--HGTWDGEIYW---SGSPLKASNIRDTeRAGIVIIHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIAYGD----NSRVVSQDEIVSAAKAANIHPFIETLPhkyETR-VGDKGtqlsGGQKQRIAIARALIRQPQ 1201
Cdd:TIGR02633 89 LVpELSVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1202 ILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1256
Cdd:TIGR02633 162 LLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1051-1259 |
2.84e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 79.44 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQW---LRAQ-LGIVSQEP 1126
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVS-------LVGQPLHQMDEEArakLRAKhVGFVFQSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILFDCSIA-ENIAY-----GDNSRVvSQDEIVSAAKAANIHPFIETLPhkyetrvgdkgTQLSGGQKQRIAIARALIRQP 1200
Cdd:PRK10584 98 MLIPTLNAlENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1201 QILLLDEATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1259
Cdd:PRK10584 166 DVLFADEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
743-968 |
3.02e-16 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 80.82 E-value: 3.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 743 DDAVKQQKCNIFSLIFLFLGIISFFTFFLQG-----FTFGKAGeiLTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRL 817
Cdd:cd18784 24 DGIVIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 818 ATDaaqvqgaTGTRLALIAQNI----ANL--GTG-IIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELE 890
Cdd:cd18784 100 TSD-------TTTMSDTVSLNLniflRSLvkAIGvIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 891 AAGKIATEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18784 173 KANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
137-332 |
4.18e-16 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 80.46 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 137 FWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKL 216
Cdd:cd18590 59 LFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 217 TLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAIS 296
Cdd:cd18590 139 TLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTV 218
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961250 297 ANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 332
Cdd:cd18590 219 RAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGS 254
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1045-1237 |
4.53e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQ 1124
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI-------KLDGGDIDDPDVAEACHYLGHRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 -EPILfdcSIAENIAYGDNSRVVSQDEIVSAAKAANIHPfIETLPHKYetrvgdkgtqLSGGQKQRIAIARALIRQPQIL 1203
Cdd:PRK13539 84 mKPAL---TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....
gi 9961250 1204 LLDEATSALDTESEKVVQEALdKAREGRTCIVIA 1237
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
129-346 |
5.06e-16 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 80.25 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 129 VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIV 208
Cdd:cd18564 69 LASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 209 GFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKE 288
Cdd:cd18564 149 MFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLR 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 289 IGIK-KAISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSILIGAFS 346
Cdd:cd18564 229 AGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPG-DLLVFLAYLKNLYK 285
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
394-609 |
6.27e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 80.54 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFND--VHFSYPSrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIRNFN---V 465
Cdd:PRK09473 13 LDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPekeL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 NYLR-EIIGVVSQEPVL-------FSTTIAENICYGRG---------NVTMDEikkAVKEANAYEFIMKLPQKFdtlvge 528
Cdd:PRK09473 92 NKLRaEQISMIFQDPMTslnpymrVGEQLMEVLMLHKGmskaeafeeSVRMLD---AVKMPEARKRMKMYPHEF------ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 529 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-IAHRLStvrnadVIAGFEDG 606
Cdd:PRK09473 163 -----SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGICDK 231
|
...
gi 9961250 607 VIV 609
Cdd:PRK09473 232 VLV 234
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
711-966 |
7.89e-16 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 79.74 E-value: 7.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIaifgpgDDAVKQQKCNI-----FSLIFLFLGIISFFTFFLQGFTFGKAGEILTR 785
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAI------DDYIVPGQGDLqglllLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 786 RLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVP 865
Cdd:cd18544 75 DLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 866 IIAVSgIVEMKLLAGNAKRDKKELEAA--GKIAtEAIENIRTVVSLTQERKFESMYvEKLYGPYRNSVQKA-HIYGITFS 942
Cdd:cd18544 153 LLLLA-TYLFRKKSRKAYREVREKLSRlnAFLQ-ESISGMSVIQLFNREKREFEEF-DEINQEYRKANLKSiKLFALFRP 229
|
250 260
....*....|....*....|....
gi 9961250 943 ISQAFMYFSYAGCFRFGAYLIVNG 966
Cdd:cd18544 230 LVELLSSLALALVLWYGGGQVLSG 253
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
711-968 |
8.28e-16 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 79.75 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDDAVKQQKCNIFSLIFLFLGI--ISFFTFFLQGFTFGKAGEILTRRL 787
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIdLIIEGLGGGGGVDFSGLLRILLLLLGLylLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 788 RSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPII 867
Cdd:cd18547 81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 868 AVSgiveMKLLAGNAKRD-KKELEAAGKI---ATEAIENIRTVVSLTQE----RKFESMyVEKLYgpyrNSVQKAHIY-G 938
Cdd:cd18547 159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREeeaiEEFDEI-NEELY----KASFKAQFYsG 229
|
250 260 270
....*....|....*....|....*....|
gi 9961250 939 ITFSISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18547 230 LLMPIMNFINNLGYVLVAVVGGLLVINGAL 259
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1047-1269 |
9.17e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 79.38 E-value: 9.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1047 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNvqwlRAQLGIVSQEP 1126
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEV-------LWDGEPLDPED----RRRIGYLPEER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILF-DCSIAENIAY-----GdnsrvVSQDEIVSAAKAanihpFIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALIR 1198
Cdd:COG4152 81 GLYpKMKVGEQLVYlarlkG-----LSKAEAKRRADE-----WLERlgLGDRANKKVEE----LSKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1199 QPQILLLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:COG4152 147 DPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1049-1261 |
9.50e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 77.96 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfqllDGQeakklnVQW-LRAQLGIVSQ--- 1124
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-------RGR------VSSlLGLGGGFNPEltg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 -EPILFDCSIaeniaYGdnsrvVSQDEIvsAAKAANIHPFIEtLPHKYETRVGdkgtQLSGGQKQRIAIARALIRQPQIL 1203
Cdd:cd03220 102 rENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1204 LLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG 1261
Cdd:cd03220 165 LIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1049-1262 |
1.24e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVD----------FGFQL-LDGQEakklNVqWLRA 1117
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNgrvsallelgAGFHPeLTGRE----NI-YLNG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1118 Q-LGIVSQEpilfdcsIAENIaygdnsrvvsqDEIVSaakAANIHPFIETlPHKYetrvgdkgtqLSGGQKQRIAIARAL 1196
Cdd:COG1134 114 RlLGLSRKE-------IDEKF-----------DEIVE---FAELGDFIDQ-PVKT----------YSSGMRARLAFAVAT 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1197 IRQPQILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1262
Cdd:COG1134 162 AVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
379-613 |
1.39e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 379 SFSERGHKPDSIKGNLefndVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ 458
Cdd:COG1134 13 SYRLYHEPSRSLKELL----LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 459 dirnfnvnylreiigvVSqePVL-FST------TIAENIcYGRG---NVTMDEIKKAVKEANAY----EFImklpqkfDT 524
Cdd:COG1134 89 ----------------VS--ALLeLGAgfhpelTGRENI-YLNGrllGLSRKEIDEKFDEIVEFaelgDFI-------DQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 525 LVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAEVQaalDKAREGRTTIVIAHRLSTVRN-ADV 599
Cdd:COG1134 143 PVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDR 215
|
250
....*....|....
gi 9961250 600 IAGFEDGVIVEQGS 613
Cdd:COG1134 216 AIWLEKGRLVMDGD 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1050-1207 |
1.43e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.76 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFYdPLAGTVFVDFGFQLLDGQEAKKLNVqWLRAQLGI--VSQEPI 1127
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FY-MIVGLVKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LF-DCSIAENIaygdnsRVVSQDEIVSAAKAANIhpfIETLPHKYE-TRVGD-KGTQLSGGQKQRIAIARALIRQPQILL 1204
Cdd:COG1137 89 IFrKLTVEDNI------LAVLELRKLSKKEREER---LEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFIL 159
|
...
gi 9961250 1205 LDE 1207
Cdd:COG1137 160 LDE 162
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1033-1266 |
1.64e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NITFNEvvfnypTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGF------QLLDGQE 1106
Cdd:PRK10261 19 NIAFMQ------EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLlrrrsrQVIELSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1107 AKKLNVQWLR-AQLGIVSQEPI-----LFDC--SIAENIAYGDNsrvVSQDEIVSAAKA-------ANIHPFIETLPHky 1171
Cdd:PRK10261 93 QSAAQMRHVRgADMAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKRmldqvriPEAQTILSRYPH-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1172 etrvgdkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQ 1244
Cdd:PRK10261 168 ---------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVA 233
|
250 260
....*....|....*....|...
gi 9961250 1245 N-ADLIVVFQNGRVKEHGTHQQL 1266
Cdd:PRK10261 234 EiADRVLVMYQGEAVETGSVEQI 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
393-619 |
1.71e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 79.02 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 393 NLEFNDVHF---SYPSRANVKIlkglNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYD-PDEGT---INIDGQDIRNFNV 465
Cdd:PRK11022 5 NVDKLSVHFgdeSAPFRAVDRI----SYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMaekLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 466 NYLREIIG----VVSQEPVlfsTTIaeNICYGRGNVTMDEIK------KAVKEANAYEFImklpqkfdTLVG-----ER- 529
Cdd:PRK11022 81 KERRNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSRl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 530 ---GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGF 603
Cdd:PRK11022 148 dvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVM 227
|
250
....*....|....*.
gi 9961250 604 EDGVIVEQGSHSELMK 619
Cdd:PRK11022 228 YAGQVVETGKAHDIFR 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
409-606 |
1.86e-15 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.02 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD---EGTINIDGQDIRNFNV-NYLREIIGVVSQEPVLF-S 483
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 484 TTIAENICYG-----RGNVTMDEikKAVKEANAYEFIMKLPQKFDTL-VGERGaqlsGGQKQRIAIARALVRNPKILLLD 557
Cdd:TIGR02633 93 LSVAENIFLGneitlPGGRMAYN--AMYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 558 EATSALdTESEAEVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDG 606
Cdd:TIGR02633 167 EPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
387-619 |
1.93e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 81.25 E-value: 1.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 387 PDSIKGNLEFNDVHFSYPSRANVK-ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIrn 462
Cdd:TIGR00955 15 AQDGSWKQLVSRLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 463 fNVNYLREIIGVVSQEPVLFSTTIAENICYGRGNVTMDE-IKKAVKEANAYEFI--MKLPQKFDTLVGERGAQ--LSGGQ 537
Cdd:TIGR00955 93 -DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRrVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRVkgLSGGE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLST--VRNADVIAGFEDGVIVEQGSH 614
Cdd:TIGR00955 172 RKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSP 251
|
....*
gi 9961250 615 SELMK 619
Cdd:TIGR00955 252 DQAVP 256
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
126-335 |
2.09e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 78.36 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 126 GVLVAAYIqvSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISK--------ISEGIgdkvgmffQ 197
Cdd:cd18574 56 SLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEfkssfkqcVSQGL--------R 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 198 AVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELE 277
Cdd:cd18574 126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 278 RYQKHLENAKE--------IGIKKAISaNISMGIAFLLIYasyalafWYGSTLVISKEYTIGNAMT 335
Cdd:cd18574 206 LYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGDLMS 263
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1050-1262 |
2.34e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.98 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfqlldGQEAKKLNVQWLRAQLGIVSQEPILF 1129
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLV--------GGKDIETNLDAVRQSLGMCPQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 D-CSIAENIAYGDNSRVVSQDEIVSAAKAanihpFIET--LPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:TIGR01257 1016 HhLTVAEHILFYAQLKGRSWEEAQLEMEA-----MLEDtgLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLD 1086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1207 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVFQNGRVKEHGT 1262
Cdd:TIGR01257 1087 EPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
407-617 |
2.81e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 407 ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD----EGTINIDGQDIrnfNVNYLREI-IGVVSQ---- 477
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPV---APCALRGRkIATIMQnprs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 478 --EPVLFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFdtlvgerGAQLSGGQKQRIAIARALVRNPKILL 555
Cdd:PRK10418 91 afNPLHTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLY-------PFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 556 LDEATSALDTESEAEVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFEDGVIVEQGSHSEL 617
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1049-1259 |
2.96e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.22 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPlAGTVFVDFgfqLLDGQEAKKLNvqwLRA--QLGIV--SQ 1124
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-P-HGSYEGEI---LFDGEVCRFKD---IRDseALGIViiHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 E----PILfdcSIAENIAYGdNSR----VVSQDEIVSAAKA------ANIHPfietlphkyETRVGDKGTqlsgGQKQRI 1190
Cdd:NF040905 86 ElaliPYL---SIAENIFLG-NERakrgVIDWNETNRRAREllakvgLDESP---------DTLVTDIGV----GKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1191 AIARALIRQPQILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKE 1259
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
410-625 |
3.06e-15 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 75.36 E-value: 3.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLYDPD-EGTINIDGQDIrnfNVNYLReIIGVVSQEPVLFsttia 487
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPL---DKNFQR-STGYVEQQDVHS----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 488 enicygrGNVTmdeikkaVKEanAYEFIMKLpqkfdtlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:cd03232 92 -------PNLT-------VRE--ALRFSALL----------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 568 EAEVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFeDGVIveqgshseLMKKEG--VYF 625
Cdd:cd03232 144 AYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKF-DRLL--------LLKRGGktVYF 191
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
766-968 |
4.00e-15 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 77.59 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 766 FFTFFLQG-FTF------GKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDaaqVQGATGTRLALIAQN 838
Cdd:cd18574 49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFDTHR--TGELVNRLTAD---VQEFKSSFKQCVSQG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 839 IANLG--TGIIISFIY-GWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKF 915
Cdd:cd18574 124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRE 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 916 ESMYVEKLygpyrNSVQKAHIY-GITFSISQAFMYFSYAG----CFRFGAYLIVNGHM 968
Cdd:cd18574 204 LELYEEEV-----EKAAKLNEKlGLGIGIFQGLSNLALNGivlgVLYYGGSLVSRGEL 256
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1041-1268 |
4.74e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.75 E-value: 4.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1041 FNYPT----RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGqeakklNVQWLR 1116
Cdd:PRK15112 14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLID-DHPLHFG------DYSYRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1117 AQLGIVSQEPI-----------LFDCSIAENIAYGDNSRvvsQDEIVSAAKAANIHP-FIETLPHkyetrvgdkgtQLSG 1184
Cdd:PRK15112 87 QRIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQR---EKQIIETLRQVGLLPdHASYYPH-----------MLAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1185 GQKQRIAIARALIRQPQILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1261
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERG 232
|
....*..
gi 9961250 1262 THQQLLA 1268
Cdd:PRK15112 233 STADVLA 239
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1045-1266 |
4.93e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.73 E-value: 4.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVFVDFGFQLLDGQEAKKLNVQWL---RAQLGI 1121
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI-------GGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 VSQEPILF-DCSIAENIAYG-----------DNSRVVSQDEIVSAAKAANIHPfietlphkyetrvgdkgTQLSGGQKQR 1189
Cdd:PRK11831 89 LFQSGALFtDMNVFDNVAYPlrehtqlpaplLHSTVMMKLEAVGLRGAAKLMP-----------------SELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1190 IAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1266
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
409-610 |
5.41e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.45 E-value: 5.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD---EGTINIDGQ-----DIRNfnvnylREIIGVV--SQE 478
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD------SEALGIViiHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 479 ----PVLfstTIAENICYG-----RGNVTMDEIKKAVKEanayefIMK---LPQKFDTLVGERGAqlsgGQKQRIAIARA 546
Cdd:NF040905 87 laliPYL---SIAENIFLGnerakRGVIDWNETNRRARE------LLAkvgLDESPDTLVTDIGV----GKQQLVEIAKA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 547 LVRNPKILLLDEATSAL-DTESEAEVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVE 610
Cdd:NF040905 154 LSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1034-1256 |
5.64e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 73.25 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGfqlldgqeakklnvq 1113
Cdd:cd03221 1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wlraqlgivsqepilfdcsiaENIAYgdnsrvvsqdeivsaakaanihpfietlphkYEtrvgdkgtQLSGGQKQRIAIA 1193
Cdd:cd03221 63 ---------------------VKIGY-------------------------------FE--------QLSGGEKMRLALA 82
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1194 RALIRQPQILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVFQNGR 1256
Cdd:cd03221 83 KLLLENPNLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
394-609 |
6.65e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 6.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVhfSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI-I 472
Cdd:COG3845 258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 473 GVVSQEP-----VLfSTTIAENI--------CYGRGNVtmdeIKKAVKEANAYEFImklpQKFD-------TLVGergaQ 532
Cdd:COG3845 336 AYIPEDRlgrglVP-DMSVAENLilgryrrpPFSRGGF----LDRKAIRAFAEELI----EEFDvrtpgpdTPAR----S 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRN-ADVIAGFEDGVIV 609
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1050-1257 |
7.04e-15 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerF--YDPLAGTVFvdfgfqlLDGQEAKKLNV-QWLRAQLGIVS--- 1123
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIR-------LDGKPVRIRSPrDAIRAGIAYVPedr 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 -QEPILFDCSIAENI---AYGDNSR--VVSQDEIVSAAKAanihpFIETL---PHKYETRVGdkgtQLSGGQKQRIAIAR 1194
Cdd:COG1129 337 kGEGLVLDLSIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRLrikTPSPEQPVG----NLSGGNQQKVVLAK 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1195 ALIRQPQILLLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVFQNGRV 1257
Cdd:COG1129 408 WLATDPKVLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1051-1261 |
1.05e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 74.10 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGTVfvdfgfqLLDGQEAKKLNVQwLRAQLGI--VSQEP 1126
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEI-------LFKGEDITDLPPE-ERARLGIflAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 IlfdcsiaeniaygdnsrvvsqdEIvSAAKAANihpFIetlphkyetRVGDKGtqLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:cd03217 87 P----------------------EI-PGVKNAD---FL---------RYVNEG--FSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1207 EATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGRVKEHG 1261
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1051-1268 |
1.18e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.31 E-value: 1.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGTVFVDFGF---------QLLDGQEAKKLNVQwlraql 1119
Cdd:TIGR03269 15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALcekcgyverPSKVGEPCPVCGGT------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1120 gIVSQEPILFDCS------IAENIA---------YGDNSRVV----SQDEIVSAAKAAnIHPFIETLPH-KYETRVGDKG 1179
Cdd:TIGR03269 89 -LEPEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITHIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1180 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1256
Cdd:TIGR03269 167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
|
250
....*....|..
gi 9961250 1257 VKEHGTHQQLLA 1268
Cdd:TIGR03269 247 IKEEGTPDEVVA 258
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
405-575 |
1.37e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 73.68 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFST 484
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 485 TIAENICYGRGNVTMDEIKKAVKEAN--AYEfimklpqkfDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGlnGFE---------DRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170
....*....|...
gi 9961250 563 LDTESEAEVQAAL 575
Cdd:cd03231 156 LDKAGVARFAEAM 168
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
55-332 |
1.43e-14 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 75.90 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 55 LFMSLGTIMAIAhgsgLPLMMivfGEMTDKFVDTAGNfSFPVNFSlsllnpgkileeEMTRYAYYYSGLGAGVLVAAYIQ 134
Cdd:cd18547 6 ILAIISTLLSVL----GPYLL---GKAIDLIIEGLGG-GGGVDFS------------GLLRILLLLLGLYLLSALFSYLQ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 135 VSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGW 214
Cdd:cd18547 66 NRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 215 KLTLVIMAISPILGLSAAVWAKI--------------LSAFsdkelaayakagavAEEALGAIRTVIAFGGQNKELERYQ 280
Cdd:cd18547 146 LLTLIVLVTVPLSLLVTKFIAKRsqkyfrkqqkalgeLNGY--------------IEEMISGQKVVKAFNREEEAIEEFD 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 281 KHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN 332
Cdd:cd18547 212 EINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVGV 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1034-1262 |
1.44e-14 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 75.12 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldGQEAKKLNVQ 1113
Cdd:COG4604 2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD-------GLDVATTPSR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEP-ILFDCSIAENIAYG----DNSRVVSQD-EIVSAAkaanIHPF-IETLPHKYETrvgdkgtQLSGGQ 1186
Cdd:COG4604 72 ELAKRLAILRQENhINSRLTVRELVAFGrfpySKGRLTAEDrEIIDEA----IAYLdLEDLADRYLD-------ELSGGQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1187 KQRIAIARALIRQPQILLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVFQNGR 1256
Cdd:COG4604 141 RQRAFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGR 213
|
....*.
gi 9961250 1257 VKEHGT 1262
Cdd:COG4604 214 VVAQGT 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1040-1261 |
1.45e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.36 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1040 VFNYPTRaNVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdFGFQLLDGQEAKKLnvQWLRAQL 1119
Cdd:PRK10261 329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEII--FNGQRIDTLSPGKL--QALRRDI 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1120 GIVSQEPILfDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIEtlphkyetRVGDKGT-------QLSGGQKQRIAI 1192
Cdd:PRK10261 404 QFIFQDPYA-SLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLE--------RVGLLPEhawryphEFSGGQRQRICI 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1193 ARALIRQPQILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1261
Cdd:PRK10261 475 ARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1034-1272 |
1.48e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptrANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfGFQLLDGQEAKklnvq 1113
Cdd:PRK11614 6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFD-GKDITDWQTAK----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFD-CSIAENIAYGD--NSRVVSQDEIVSAakaanihpfIETLPHKYETRVGDKGTqLSGGQKQRI 1190
Cdd:PRK11614 77 IMREAVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1191 AIARALIRQPQILLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQ 1265
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDA 223
|
....*..
gi 9961250 1266 LLAQKGI 1272
Cdd:PRK11614 224 LLANEAV 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1051-1267 |
1.52e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQWLRAQLGIVSQEPIL-F 1129
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW-------LDGEHIQHYASKEVARRIGLLAQNATTpG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYG--------DNSRVVSQDEIVSAAKAANIhpfietlphkyeTRVGDKGTQ-LSGGQKQRIAIARALIRQP 1200
Cdd:PRK10253 95 DITVQELVARGryphqplfTRWRKEDEEAVTKAMQATGI------------THLADQSVDtLSGGQRQRAWIAMVLAQET 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1201 QILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1267
Cdd:PRK10253 163 AIMLLDEPTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1049-1255 |
1.66e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVF-----VDF-GFQllDGQEAKklnvqwlraqLGIV 1122
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILylgkeVTFnGPK--SSQEAG----------IGII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 SQEPILFD-CSIAENIAYGDnsrvvsqdEIVSA----------AKAANIHPFIeTLPHKYETRVGDkgtqLSGGQKQRIA 1191
Cdd:PRK10762 85 HQELNLIPqLTIAENIFLGR--------EFVNRfgridwkkmyAEADKLLARL-NLRFSSDKLVGE----LSIGEQQMVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1192 IARALIRQPQILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNG 1255
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDG 217
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
103-331 |
1.67e-14 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 75.50 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 103 LNPGKILEEEMTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDIS 182
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 183 KISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGA 262
Cdd:cd18544 110 ALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 263 IRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 331
Cdd:cd18544 190 MSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG 258
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1049-1257 |
2.69e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLlerfydpLAGTVFVDFGFQLLDGQEAKKLNVQwLRAQLGI--VSQEP 1126
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKI-------IAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILF-DCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKYEtrVGDkgtqlsggqKQRIAIARALIRQPQILLL 1205
Cdd:PRK15439 96 LLFpNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAGSLE--VAD---------RQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1206 DEATSALD-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1257
Cdd:PRK15439 165 DEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
111-558 |
3.23e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 77.15 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 111 EEMTRYAYYYSGLGAGVLVAAYI-QVSFWTLAAgRQIRKIRQKFFHAILR------QEIGwfdindTTELNTRLTDDISK 183
Cdd:COG4615 45 AALARLLLLFAGLLVLLLLSRLAsQLLLTRLGQ-HAVARLRLRLSRRILAaplerlERIG------AARLLAALTEDVRT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 184 ISEGigdkvgmFFQAVATFFAGFIVGFirgwklTLVIMA-ISPILGLSAAVWAKILSAF---SDKELAAYAKAGAVAEEA 259
Cdd:COG4615 118 ISQA-------FVRLPELLQSVALVLG------CLAYLAwLSPPLFLLTLVLLGLGVAGyrlLVRRARRHLRRAREAEDR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 260 L-GAIRTVIafGGqNKEL------------ERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLV-IS 325
Cdd:COG4615 185 LfKHFRALL--EG-FKELklnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGwAD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 326 KEYTIGNAMTVFFsiLIGAfsVGQAAPCIDAFANARGAAyvifdiidnnPKIDSFSERGHKPDSIKGN------------ 393
Cdd:COG4615 262 PAVLSGFVLVLLF--LRGP--LSQLVGALPTLSRANVAL----------RKIEELELALAAAEPAAADaaappapadfqt 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRANVK--ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREI 471
Cdd:COG4615 328 LELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPVLFSTTiaenicYGRGNVTMDEikkavkEANAYEFIMKLPQK-------FDTLvgergaQLSGGQKQRIAIA 544
Cdd:COG4615 408 FSAVFSDFHLFDRL------LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALL 469
|
490
....*....|....
gi 9961250 545 RALVRNPKILLLDE 558
Cdd:COG4615 470 VALLEDRPILVFDE 483
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1044-1257 |
3.45e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 73.52 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1044 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfQLLDGQEAKKLnvqwlRAQLGIV- 1122
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA---GLVPWKRRKKF-----LRRIGVVf 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 -SQEPILFDCSIAENIAYgdNSRVVSQDEivsAAKAANIHPFIETLPHkyeTRVGDKGT-QLSGGQKQRIAIARALIRQP 1200
Cdd:cd03267 101 gQKTQLWWDLPVIDSFYL--LAAIYDLPP---ARFKKRLDELSELLDL---EELLDTPVrQLSLGQRMRAEIAAALLHEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1201 QILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:cd03267 173 EILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
394-617 |
3.57e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 74.42 E-value: 3.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSypsRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYL---RE 470
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFS-TTIAENICYG-RGNVTMDE--IKKAVkeanayefIMKLPQkfdtlVGERGA------QLSGGQKQR 540
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKLEA-----VGLRGAaklmpsELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 541 IAIARALVRNPKILLLDEATSALDTESEA-------EVQAALdkareGRTTIVIAHR----LSTVRNADVIAgfeDGVIV 609
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGvlvklisELNSAL-----GVTCVVVSHDvpevLSIADHAYIVA---DKKIV 223
|
....*...
gi 9961250 610 EQGSHSEL 617
Cdd:PRK11831 224 AHGSAQAL 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1046-1237 |
3.97e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.39 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1046 RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQE 1125
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEV-------RWNGTPLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILFDCSIAENIAY-----GDNSRVVSQdeivsAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIARALIRQP 1200
Cdd:TIGR01189 83 GLKPELSALENLHFwaaihGGAQRTIED-----ALAAVGLTGFEDLPAA-----------QLSAGQQRRLALARLWLSRR 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961250 1201 QILLLDEATSALDTESEKVVQEALDkAREGRTCIVIA 1237
Cdd:TIGR01189 147 PLWILDEPTTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
410-594 |
3.98e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirnfnvnyLReiIGVVSQEPVLFSTT--IA 487
Cdd:PRK09544 18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQKLYLDTTLplTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 488 ENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKfdtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:PRK09544 87 NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180
....*....|....*....|....*....
gi 9961250 568 EAEVQAALDKARE--GRTTIVIAHRLSTV 594
Cdd:PRK09544 156 QVALYDLIDQLRRelDCAVLMVSHDLHLV 184
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
409-647 |
4.52e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.76 E-value: 4.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRL--YDPDEGTI----------------NIDGQ------------ 458
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 459 --DIRNFNVNYLREIIGVVSqepVLFSTTIAeniCYGRGNVtMDEIKKAVKEAnAYEFIMKLPQKFDTL----VGER--- 529
Cdd:TIGR03269 93 evDFWNLSDKLRRRIRKRIA---IMLQRTFA---LYGDDTV-LDNVLEALEEI-GYEGKEAVGRAVDLIemvqLSHRith 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 530 -GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA--REGRTTIVIAHRLSTVRN-ADVIAGFED 605
Cdd:TIGR03269 165 iARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLEN 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 9961250 606 GVIVEQGSHSELMKKegvyFklvnMQTSGSQIQSEEFELNDE 647
Cdd:TIGR03269 245 GEIKEEGTPDEVVAV----F----MEGVSEVEKECEVEVGEP 278
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1052-1267 |
5.24e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 73.42 E-value: 5.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV-FVDFGFQLLDGQEAKKLNVQWL-RAQLGIVSQEP--- 1126
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALSEAERRRLlRTEWGFVHQHPrdg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILFDCSIAENIA----------YGdNSRVVSQD-----EIVSAakaanihpfietlphkyetRVGDKGTQLSGGQKQRIA 1191
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYG-DIRATAGDwlervEIDAA-------------------RIDDLPTTFSGGMQQRLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1192 IARALIRQPQILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1264
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTD 237
|
...
gi 9961250 1265 QLL 1267
Cdd:PRK11701 238 QVL 240
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1054-1266 |
7.41e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 73.10 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1054 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLrAQLGIVS--QEPILF-D 1130
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI-------LLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 CSIAENIaygdnsrVVSQDEIVsaaKAANIHPFIET------------LPHKYETRVG-------DKGTqLSGGQKQRIA 1191
Cdd:PRK11300 95 MTVIENL-------LVAQHQQL---KTGLFSGLLKTpafrraesealdRAATWLERVGllehanrQAGN-LAYGQQRRLE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1192 IARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1266
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
400-621 |
9.18e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 400 HFSYPSRANVkILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLYDPDE-------GTINIDGQDIRNFNVNYLREI 471
Cdd:PRK13547 6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQ--EPVlFSTTIAENICYGR----------GNVTMDEIKKAVKEANAyefimklpqkfDTLVGERGAQLSGGQKQ 539
Cdd:PRK13547 85 RAVLPQaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 540 RIAIARAL---------VRNPKILLLDEATSALDTESEAEVQAAL-DKARE---GRTTIVIAHRLSTvRNADVIAGFEDG 606
Cdd:PRK13547 153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVrRLARDwnlGVLAIVHDPNLAA-RHADRIAMLADG 231
|
250
....*....|....*
gi 9961250 607 VIVEQGSHSELMKKE 621
Cdd:PRK13547 232 AIVAHGAPADVLTPA 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1051-1224 |
1.01e-13 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 71.37 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFD 1130
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRV-------LLNGGPLDFQRDSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 CSIAENIAY--GDNSRvvsqDEIVSAAKAANIHPFiETLPhkyetrvgdkGTQLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:cd03231 88 LSVLENLRFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170
....*....|....*.
gi 9961250 1209 TSALDTESEKVVQEAL 1224
Cdd:cd03231 153 TTALDKAGVARFAEAM 168
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
975-1269 |
1.01e-13 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 75.39 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 975 LVFsaivFGAVALGHAS-SFAPDYAkaklsaahLFMLFERQPLI------------------------DSYSEEGLKPDK 1029
Cdd:PRK10522 249 LVF----YMANSLGWADtNVAATYS--------LTLLFLRTPLLsavgalptllsaqvafnklnklalAPYKAEFPRPQA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1030 FEG--NITFNEVVFNYPTR--ANVPVlqglSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQ 1105
Cdd:PRK10522 317 FPDwqTLELRNVTFAYQDNgfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI-------LLDGK 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1106 EAKKLNVQWLRAQLGIVSQEPILFDcsiaeniaygdnsRVVSQDEivSAAKAANIHPFIETLPHKYETRVGD---KGTQL 1182
Cdd:PRK10522 386 PVTAEQPEDYRKLFSAVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgriSNLKL 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1183 SGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE- 1259
Cdd:PRK10522 451 SKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSEl 530
|
330
....*....|
gi 9961250 1260 HGTHQQLLAQ 1269
Cdd:PRK10522 531 TGEERDAASR 540
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
421-609 |
1.21e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 69.71 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 421 SGQTVALVGSSGCGKSTTVQLIQRLYDPDEGT-INIDGQDIRNFNVNYLREIIgvvsqepvlfsttiaenicygrgnvtm 499
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 500 deikkavkeanayefimklpqkfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD--- 576
Cdd:smart00382 54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961250 577 ---KAREGRTTIVIAHRLSTVRNADVIAGFEDGVIV 609
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
405-588 |
1.23e-13 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 70.85 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFST 484
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 485 TIAENICYGRGnvTMDEIKKAVKEANAyefIMKLPQKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:TIGR01189 89 SALENLHFWAA--IHGGAQRTIEDALA---AVGLTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....
gi 9961250 565 TESEAEVQAALDkAREGRTTIVIA 588
Cdd:TIGR01189 160 KAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
406-613 |
1.25e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.66 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--RNFNVNYLREI------------ 471
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrRSRQVIELSEQsaaqmrhvrgad 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 472 IGVVSQEPV-----LFST--TIAENICYGRGnVTMDEikkAVKEANAYEFIMKLPQKfDTLVGERGAQLSGGQKQRIAIA 544
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG-ASREE---AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGGMRQRVMIA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 545 RALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRT--TIVIAHRLSTVRN-ADVIAGFEDGVIVEQGS 613
Cdd:PRK10261 181 MALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGS 252
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
410-590 |
1.32e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLY--DPDEGTINIDGQDIrnfnvnylreiigvvSQEpvlfsTTIA 487
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 488 ENIcYGRGNVTMD-EIKKAVKEANAYEFImklpQKFDtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 566
Cdd:COG2401 104 DAI-GRKGDFKDAvELLNAVGLSDAVLWL----RRFK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180
....*....|....*....|....*.
gi 9961250 567 SEAEVQAALDK-AREGRTTIVIA-HR 590
Cdd:COG2401 171 TAKRVARNLQKlARRAGITLVVAtHH 196
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
711-968 |
1.49e-13 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 72.83 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDDavkQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRS 789
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIdALTAGTLT---ASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 790 MAFKAMLRQDMSWFddHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAV 869
Cdd:cd18541 78 DLFAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLAL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 870 SGIVEMKLLagnAKRDKKELEAAGKIATEAIEN---IRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQA 946
Cdd:cd18541 156 LVYRLGKKI---HKRFRKVQEAFSDLSDRVQESfsgIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGL 232
|
250 260
....*....|....*....|..
gi 9961250 947 FMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18541 233 LIGLSFLIVLWYGGRLVIRGTI 254
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1050-1239 |
1.83e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.14 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERfydplagtvfvdfgfQLLDGQEAKKLNVQWLraqlgivsqePILF 1129
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG---------------ALKGTPVAGCVDVPDN----------QFGR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIA-YGDNSRVVsqdEIVSAAKAANIHPFIETLPHkyetrvgdkgtqLSGGQKQRIAIARALIRQPQILLLDEA 1208
Cdd:COG2401 99 EASLIDAIGrKGDFKDAV---ELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190
....*....|....*....|....*....|...
gi 9961250 1209 TSALDTESEKVVQEALDKA--REGRTCIVIAHR 1239
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLarRAGITLVVATHH 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
412-617 |
2.14e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.28 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNY-LREIIGVVS----QEPVLFSTTI 486
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENIC------YGRGNVtMDEiKKAVKEANAYefIMKL---PQKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:COG1129 348 RENITlasldrLSRGGL-LDR-RRERALAEEY--IKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 558 EATSALDTESEAEVQAALDK-AREGRTTIVIahrlST-----VRNADVIAGFEDGVIVEQGSHSEL 617
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVGELDREEA 481
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
756-1259 |
2.41e-13 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 74.45 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 756 LIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGtRLALI 835
Cdd:COG4615 52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERI--GAARLLAALTEDVRTISQAFV-RLPEL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 836 AQNIANlgtgIIISFIY-GWQLTLLLLAVVPIIAVSGIVEMKLLagnaKRDKKELEAAGKIATEAIENIRTVVS------ 908
Cdd:COG4615 129 LQSVAL----VLGCLAYlAWLSPPLFLLTLVLLGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFRALLEgfkelk 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 909 LTQERKFEsmYVEKLYGP----YRNSVQKAH-IYGITFSISQAFMYFSYAGCFrfgaYLIVNGHMRFRDVILVFS-AIVF 982
Cdd:COG4615 201 LNRRRRRA--FFDEDLQPtaerYRDLRIRADtIFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVlVLLF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 983 GAVALGHASSFAPDYAKAKLSAAHL--FMLFERQPLIDSYSEEGLKPDKFEGNITFNEVVFNYPTRANVP--VLQGLSLE 1058
Cdd:COG4615 275 LRGPLSQLVGALPTLSRANVALRKIeeLELALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEgfTLGPIDLT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1059 VKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQWLRAQLGIVSQEPILFDcsiaenia 1138
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI-------LLDGQPVTADNREAYRQLFSAVFSDFHLFD-------- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1139 ygdnsRVVSQDEIVSAAKAaniHPFIETL--PHKyeTRVGDKG---TQLSGGQKQRIAIARALIRQPQILLLDEATSALD 1213
Cdd:COG4615 420 -----RLLGLDGEADPARA---RELLERLelDHK--VSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 9961250 1214 TESEKVVQEAL--DKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1259
Cdd:COG4615 490 PEFRRVFYTELlpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
758-982 |
3.30e-13 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 72.21 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 758 FLFLGIISFFTF-------FLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQGATGT 830
Cdd:cd18565 53 LWLLGGLTVAAFlleslfqYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 831 RLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLagnAKRDKKELEAAGKIAT---EAIENIRTVV 907
Cdd:cd18565 131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRI---EPRYRAVREAVGDLNArleNNLSGIAVIK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 908 SLTQERkFESMYVEKLYGPYRNSVQKAHIYGITFsisQAFMYF----SYAGCFRFGAYLIVNGHMRFRDVILV--FSAIV 981
Cdd:cd18565 208 AFTAED-FERERVADASEEYRDANWRAIRLRAAF---FPVIRLvagaGFVATFVVGGYWVLDGPPLFTGTLTVgtLVTFL 283
|
.
gi 9961250 982 F 982
Cdd:cd18565 284 F 284
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
410-613 |
3.97e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.20 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEG----------TINIDGQ---DIRNFnvnylREIIGVVS 476
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrTVQREGRlarDIRKS-----RANTGYIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 477 QEPVLFST-TIAENICYGRGNVT------MDEIKKAVKEaNAYEFIMKLPQKFdtLVGERGAQLSGGQKQRIAIARALVR 549
Cdd:PRK09984 93 QQFNLVNRlSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRVGMVH--FAHQRVSTLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 550 NPKILLLDEATSALDTESEAEVQAALD--KAREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGS 613
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1049-1255 |
5.48e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.89 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQwLRAQLG--IVSQEP 1126
Cdd:PRK09700 18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-------TINNINYNKLDHK-LAAQLGigIIYQEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILFD-CSIAENIAYGDN-SRVVSQDEIVSAAK---AANIHPFIETLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQ 1201
Cdd:PRK09700 90 SVIDeLTVLENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1202 ILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNG 1255
Cdd:PRK09700 166 VIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1055-1261 |
5.60e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 5.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1055 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDP------LAGTVFVDfgfqlldgqEAKKLNVQWLRAQLGIVS 1123
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPqkgrivLNGRVLFD---------AEKGICLPPEKRRIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 QEPILF-DCSIAENIAYGDNSRVVSQ-DEIVSAAkaaNIHPFIETLPHKyetrvgdkgtqLSGGQKQRIAIARALIRQPQ 1201
Cdd:PRK11144 83 QDARLFpHYKVRGNLRYGMAKSMVAQfDKIVALL---GIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1202 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVFQNGRVKEHG 1261
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
406-618 |
7.37e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.20 E-value: 7.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 406 RANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPvlfSTT 485
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 486 IAENICYG-------RGNVTMDEIKKAVKEANAYEFIMKLPQKfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK15112 100 LNPRQRISqildfplRLNTDLEPEQREKQIIETLRQVGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 559 ATSALDTESEAE-VQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:PRK15112 176 ALASLDMSMRSQlINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
415-629 |
8.32e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 8.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 415 LNLKVQSGQTVALVGSSGCGKSTtvqLIQRLYD--PDEGTINIDGQDIRNFNVNYLREIIGVVSQE-------PVLFSTT 485
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtppfamPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 486 IaenicYGRGNVTMDEIKKAVKE-ANAYEFIMKLPqkfdTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLD 557
Cdd:PRK03695 92 L-----HQPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 558 EATSALDTESeaevQAALDK-----AREGRTTIVIAHRLS-TVRNADVIAGFEDGVIVEQGSHSELMKKE------GVYF 625
Cdd:PRK03695 159 EPMNSLDVAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEnlaqvfGVNF 234
|
....
gi 9961250 626 KLVN 629
Cdd:PRK03695 235 RRLD 238
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
122-345 |
9.87e-13 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 70.12 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 122 GLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVAT 201
Cdd:cd18548 47 LLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIM 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 202 FFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQK 281
Cdd:cd18548 127 LIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDK 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 282 HLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN-------AMTVFFSILIGAF 345
Cdd:cd18548 207 ANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDlvafinyLMQILMSLMMLSM 277
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
143-335 |
1.11e-12 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 70.19 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 143 GRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLV-IM 221
Cdd:cd18589 65 SRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLtAL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 222 AISPILGLSAAV--WAKILSAFSDKELAAYAKAGAvaeEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANI 299
Cdd:cd18589 145 GLPLLLLVPKFVgkFQQSLAVQVQKSLARANQVAV---ETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAV 221
|
170 180 190
....*....|....*....|....*....|....*....
gi 9961250 300 SM---GIAFLLIYASyalAFWYGSTLVISKEYTIGNAMT 335
Cdd:cd18589 222 SMwtsSFSGLALKVG---ILYYGGQLVTAGTVSSGDLVT 257
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
409-586 |
2.10e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 2.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIiGVV----SQ----EPV 480
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlwwdLPA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 481 LFSTTIAENIcYGrgnVTMDEIKKAVKEANAyefIMKLPQKFDTLVgeRgaQLSGGQKQRIAIARALVRNPKILLLDEAT 560
Cdd:COG4586 114 IDSFRLLKAI-YR---IPDAEYKKRLDELVE---LLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180
....*....|....*....|....*..
gi 9961250 561 SALDTESEAEVQAALDKA-REGRTTIV 586
Cdd:COG4586 183 IGLDVVSKEAIREFLKEYnRERGTTIL 209
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
414-589 |
3.18e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 414 GLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREII------GVvsqEPVLfstTIA 487
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGI---KTEL---TAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 488 ENI---CYGRGNVTMDEIKKAvkeanayefimkLPQkfdtlVGERG------AQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK13538 93 ENLrfyQRLHGPGDDEALWEA------------LAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|..
gi 9961250 559 ATSALDTESEAEVQAALDK-AREGRTTIVIAH 589
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1052-1267 |
3.18e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.85 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----LAGTVfvdfgfqLLDGqeaKKLNVQWLRAQLGIVSQEPI 1127
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSV-------LLNG---MPIDAKEMRAISAYVQQDDL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1128 LFDCSIAEN----IAYGDNSRVVSQDE----------IVSAAKAANihpfietlphkyeTRVGDKGTQ--LSGGQKQRIA 1191
Cdd:TIGR00955 110 FIPTLTVREhlmfQAHLRMPRRVTKKEkrervdevlqALGLRKCAN-------------TRIGVPGRVkgLSGGERKRLA 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1192 IARALIRQPQILLLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHGTHQQLL 1267
Cdd:TIGR00955 177 FASELLTDPPLLFCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
398-591 |
3.51e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 398 DVHFSYPSranVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrNFNVN--YLREIIGVV 475
Cdd:PRK10982 3 NISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSkeALENGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 476 SQE-PVLFSTTIAENICYGRgnvtmdEIKKA--VKEANAYEFIMKLPQKFDTLVG--ERGAQLSGGQKQRIAIARALVRN 550
Cdd:PRK10982 79 HQElNLVLQRSVMDNMWLGR------YPTKGmfVDQDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961250 551 PKILLLDEATSALdteSEAEVQ---AALDKARE-GRTTIVIAHRL 591
Cdd:PRK10982 153 AKIVIMDEPTSSL---TEKEVNhlfTIIRKLKErGCGIVYISHKM 194
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
412-594 |
3.76e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.37 E-value: 3.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNfnvnYLRE-IIGVVSQEPVL---FSTTIA 487
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKnLVAYVPQSEEVdwsFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 488 ENICYGR-GNVTMDEIKKA-----VKEANAYEFIMKLPQKfdtLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATS 561
Cdd:PRK15056 99 DVVMMGRyGHMGWLRRAKKrdrqiVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|....
gi 9961250 562 ALDTESEAEVQAALDKAR-EGRTTIVIAHRLSTV 594
Cdd:PRK15056 172 GVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
752-968 |
6.39e-12 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 67.86 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLaTDAAQVQGA-TGT 830
Cdd:cd18570 42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK--TGEIISRF-NDANKIREAiSST 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 831 RLALIAQNIANLGTGIIIsFIYGWQLTLLLLAVVPIIAVSGIVEMKLLagnAKRDKKELEAAGKIAT---EAIENIRTVV 907
Cdd:cd18570 119 TISLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYILIILLFNKPF---KKKNREVMESNAELNSyliESLKGIETIK 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 908 SLTQERKFESMyVEKLYGPYRNSVQKAHIYGITFS-ISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18570 195 SLNAEEQFLKK-IEKKFSKLLKKSFKLGKLSNLQSsIKGLISLIGSLLILWIGSYLVIKGQL 255
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
711-968 |
6.47e-12 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 67.89 E-value: 6.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEII--AIFGPGDDAVKqqkcnIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLR 788
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdgPIAHGDRSALW-----PLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 789 SMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGtRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIA 868
Cdd:cd18543 76 TDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 869 VSGIVEMKLLAGNAKRDKkelEAAGKIATEAIEN---IRTVVSLTQER----KFESMyVEKLygpYRNSVQKAHIYGITF 941
Cdd:cd18543 153 LVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRERreldRFEAA-ARRL---RATRLRAARLRARFW 225
|
250 260
....*....|....*....|....*..
gi 9961250 942 SISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18543 226 PLLEALPELGLAAVLALGGWLVANGSL 252
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
404-588 |
6.66e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.13 E-value: 6.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 404 PSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD---EGTINIDGQDIRNFNVNYLREIIgVVSQEPV 480
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 481 LFST-TIAEnicygrgnvTMDeikkAVKEANAYEFImklpqkfdtlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDEA 559
Cdd:cd03233 94 HFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190
....*....|....*....|....*....|
gi 9961250 560 TSALDTESEAE-VQAALDKAREGRTTIVIA 588
Cdd:cd03233 146 TRGLDSSTALEiLKCIRTMADVLKTTTFVS 175
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
756-974 |
7.82e-12 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 67.42 E-value: 7.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 756 LIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA--TGTRLA 833
Cdd:cd18548 43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 834 LIAqnIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQE- 912
Cdd:cd18548 121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 913 ---RKFESMYVEklygpYRNSVQKA-HIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVI 974
Cdd:cd18548 199 yeeERFDKANDD-----LTDTSLKAgRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLV 259
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
414-612 |
8.21e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 8.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 414 GLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDI--------------RNF-NVNYLREIIGV---- 474
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 475 VSQEPVLFSTTIAenicygrGNVTMDEIKKAvkEANAYEFIMKLPQKFDTL-VGERGA-QLSGGQKQRIAIARALVRNPK 552
Cdd:PRK11300 103 VAQHQQLKTGLFS-------GLLKTPAFRRA--ESEALDRAATWLERVGLLeHANRQAgNLAYGQQRRLEIARCMVTQPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 553 ILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIagfedgVIVEQG 612
Cdd:PRK11300 174 ILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRI------YVVNQG 230
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1026-1267 |
8.41e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.12 E-value: 8.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1026 KPDKFEGNITFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgFQLLDGQ 1105
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD--AQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1106 EAKKL--NVQWLRAQL----GIVSQEPIlfdcSIAENIAYGDNSRVVSQD-EIVSAAKA-ANIHPFIEtlphkyetRVGD 1177
Cdd:PRK10575 79 SSKAFarKVAYLPQQLpaaeGMTVRELV----AIGRYPWHGALGRFGAADrEKVEEAISlVGLKPLAH--------RLVD 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1178 kgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVFQ 1253
Cdd:PRK10575 147 ---SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALR 222
|
250
....*....|....
gi 9961250 1254 NGRVKEHGTHQQLL 1267
Cdd:PRK10575 223 GGEMIAQGTPAELM 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
411-598 |
9.13e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTTIAENi 490
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 491 CY-----GRGNVTMDEIKKavkeanayefIMKLPQKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:PRK13540 95 CLydihfSPGAVGITELCR----------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180 190
....*....|....*....|....*....|....
gi 9961250 566 ESEAEVQAALDKAR-EGRTTIVIAHRLSTVRNAD 598
Cdd:PRK13540 161 LSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
125-331 |
1.03e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 67.15 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 125 AGVLVAAYIQVSFWTLAAGRQIRK--------IRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFF 196
Cdd:cd18563 46 VLGLAGAYVLSALLGILRGRLLARlgeritadLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 197 QAVATFFAGFIVGFIRGWKLTLVIMAISPILG-LSAAVWAKILSAFSdKELAAYAKAGAVAEEALGAIRTVIAFGGQNKE 275
Cdd:cd18563 126 TNILMIIGIGVVLFSLNWKLALLVLIPVPLVVwGSYFFWKKIRRLFH-RQWRRWSRLNSVLNDTLPGIRVVKAFGQEKRE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 276 LERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIG 331
Cdd:cd18563 205 IKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG 260
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1047-1261 |
1.37e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 66.26 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1047 ANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLerfyDPLAGTVFVDFGFQLLDGQ--EAKKLN------------ 1111
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL----GILPAGVRQTAGRVLLDGKpvAPCALRgrkiatimqnpr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1112 -----VQWLRA-------QLGIVSQEPILFDCsiAENIAYGDNSRVVSqdeivsaakaanIHPFietlphkyetrvgdkg 1179
Cdd:PRK10418 90 safnpLHTMHTharetclALGKPADDATLTAA--LEAVGLENAARVLK------------LYPF---------------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1180 tQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1256
Cdd:PRK10418 140 -EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGR 218
|
....*
gi 9961250 1257 VKEHG 1261
Cdd:PRK10418 219 IVEQG 223
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
123-346 |
1.41e-11 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 66.74 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 123 LGAGVLVAA--YIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFFQAVA 200
Cdd:cd18550 46 VAVAVASALlgVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 201 TFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGA--IRTVIAFGGQNKELER 278
Cdd:cd18550 126 TLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAAR 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 279 YQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAFS 346
Cdd:cd18550 206 FARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIGGGLTIGTlvAFTALLGRLYGPLT 275
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
422-612 |
1.41e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 422 GQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREII---------GVVSQEP-------VLFSTT 485
Cdd:PRK11701 32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAErrrllrtewGFVHQHPrdglrmqVSAGGN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 486 IAENIC------YGR---------GNVTMDEIKkavkeanayefIMKLPQKFdtlvgergaqlSGGQKQRIAIARALVRN 550
Cdd:PRK11701 112 IGERLMavgarhYGDiratagdwlERVEIDAAR-----------IDDLPTTF-----------SGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 551 PKILLLDEATSALDTeseaEVQAA-LDKARE-----GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQG 612
Cdd:PRK11701 170 PRLVFMDEPTGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1042-1257 |
1.84e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.13 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1042 NYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPLAGTVfvdfgfqLLDGQEAKKLNV-QWLRAQ 1118
Cdd:COG3845 264 SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSI-------RLDGEDITGLSPrERRRLG 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1119 LGIVSQEP-----ILfDCSIAENIAYGDNSR-------VVSQDEIVSAAKAAnihpfIEtlphKYETRVGDKGT---QLS 1183
Cdd:COG3845 335 VAYIPEDRlgrglVP-DMSVAENLILGRYRRppfsrggFLDRKAIRAFAEEL-----IE----EFDVRTPGPDTparSLS 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1184 GGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
363-623 |
2.02e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 68.07 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 363 AAYVIFDIIdNNPKIDSFSERGHKPDSIKG--NLEFNDVHFSYPSRANVkiLKGLNLKVQSGQTVALVGSSGCGKSTTVQ 440
Cdd:PRK10522 291 SAQVAFNKL-NKLALAPYKAEFPRPQAFPDwqTLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAM 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 441 LIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPVLFSTtiaenicygrgnvTMDEIKKAVKEANAYEFI--MKL 518
Cdd:PRK10522 368 LLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQ-------------LLGPEGKPANPALVEKWLerLKM 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 519 PQKFdTLVGERGA--QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKARE-GRTTIVIAHRLSTV 594
Cdd:PRK10522 435 AHKL-ELEDGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYF 513
|
250 260 270
....*....|....*....|....*....|
gi 9961250 595 RNADVIAGFEDGVIVE-QGSHSELMKKEGV 623
Cdd:PRK10522 514 IHADRLLEMRNGQLSElTGEERDAASRDAV 543
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1037-1241 |
2.30e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 65.47 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1037 NEVVFNYPtrANVPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDP---------LAGTVFVDFGF 1099
Cdd:cd03236 4 DEPVHRYG--PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPpdwdeildeFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1100 QLLDGQEAKKLNVQWlraqlgiVSQEPILFDCSIAENIAYGDNSRVvsQDEIVsaaKAANIHPFIETlphkyetrvgdKG 1179
Cdd:cd03236 81 KLLEGDVKVIVKPQY-------VDLIPKAVKGKVGELLKKKDERGK--LDELV---DQLELRHVLDR-----------NI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1180 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE----KVVQEAldkAREGRTCIVIAHRLS 1241
Cdd:cd03236 138 DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1045-1257 |
2.52e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.83 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKLN-----------VQ 1113
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTI-------TLHGKKINNHNaneainhgfalVT 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKyeTRVGdkgtQLSGGQKQRIAIA 1193
Cdd:PRK10982 330 EERRSTGIYAYLDIGFNSLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHR--TQIG----SLSGGNQQKVIIG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1194 RALIRQPQILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
394-620 |
2.85e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 65.43 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYpsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI--QRLYDPDEGTINIDGQDIRNFN------- 464
Cdd:CHL00131 8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEpeerahl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 465 -----VNYLREIIGVvsqepvlfsttiaENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDtLVGERGAQL------ 533
Cdd:CHL00131 85 giflaFQYPIEIPGV-------------SNADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvne 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 534 --SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAH--RLSTVRNADVIAGFEDGVI 608
Cdd:CHL00131 151 gfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKI 230
|
250
....*....|..
gi 9961250 609 VEQGShSELMKK 620
Cdd:CHL00131 231 IKTGD-AELAKE 241
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
752-968 |
2.92e-11 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 65.82 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIFLFLGIISFFTFFLQG-----FTFgkAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG 826
Cdd:cd18590 33 NAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTSRLSTDTTLMSR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 827 AtgtrlalIAQNI----ANLG-TGIIISFIYG--WQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEA 899
Cdd:cd18590 109 S-------VALNAnvllRSLVkTLGMLGFMLSlsWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 900 IENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18590 182 VSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1039-1269 |
3.31e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 66.29 E-value: 3.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1039 VVFNYPTrANVPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLerfyDPLAGTVFVDfGFQLLDGQE-----AKKLNV 1112
Cdd:PRK09473 20 VTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALM----GLLAANGRIG-GSATFNGREilnlpEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 qwLRA-QLGIVSQEP-----------------ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPfietlpHKYetr 1174
Cdd:PRK09473 94 --LRAeQISMIFQDPmtslnpymrvgeqlmevLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYP------HEF--- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1175 vgdkgtqlSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVV 1251
Cdd:PRK09473 163 --------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLV 234
|
250
....*....|....*...
gi 9961250 1252 FQNGRVKEHGTHQQLLAQ 1269
Cdd:PRK09473 235 MYAGRTMEYGNARDVFYQ 252
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1013-1241 |
4.18e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.47 E-value: 4.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1013 RQPLIDSYSEEGLKPDKFEGN----ITFNEVVF-NYP--TRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF 1085
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRgiveYQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGEL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1086 YDPLAGTVFVDfgfqlldgqeakklnvqwLRAQLGIVSQEPILFDCSIAENIAYGDNS-----RVVSQDEIVsaAKAANI 1160
Cdd:TIGR00954 502 WPVYGGRLTKP------------------AKGKLFYVPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLE--QILDNV 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1161 HpfietLPHKYETRVG-----DKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAreGRTCIV 1235
Cdd:TIGR00954 562 Q-----LTHILEREGGwsavqDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFS 634
|
....*.
gi 9961250 1236 IAHRLS 1241
Cdd:TIGR00954 635 VSHRKS 640
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1051-1272 |
4.33e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.53 E-value: 4.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFYdPLAGTVFVDFGFQLLDGQEAKKLNVQwLRAQLGI--VSQEPil 1128
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTT------FY-MVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEA-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1129 fdcSIAENIAYGDNSRVVSQ--DEIVSAAKAANIHPFIETLpHKYETRvGDKGTQLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:PRK10895 88 ---SIFRRLSVYDNLMAVLQirDDLSAEQREDRANELMEEF-HIEHLR-DSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1207 EATSALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLLAQKGI 1272
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
394-620 |
4.92e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 64.43 E-value: 4.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKST-TVQLIQRL-YDPDEGTINIDGQDIRNFN------- 464
Cdd:PRK09580 2 LSIKDLHVSVEDKA---ILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 465 -----VNYLREIIGVVSQepvLFSTTIAENICYGRGNVTMD--EIKKAVKEANAyefIMKLPQkfDTLVGERGAQLSGGQ 537
Cdd:PRK09580 79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDrfDFQDLMEEKIA---LLKMPE--DLLTRSVNVGFSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 538 KQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREG-RTTIVIAH--RLSTVRNADVIAGFEDGVIVEQGSH 614
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
....*.
gi 9961250 615 SeLMKK 620
Cdd:PRK09580 231 T-LVKQ 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1034-1240 |
5.02e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.36 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqlldgQEAKKLNVq 1113
Cdd:PRK09544 5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRI- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wlraqlGIVSQEpILFDCSIAENIaygdnSRV------VSQDEIVSAAKAANIHPFIETLPHKyetrvgdkgtqLSGGQK 1187
Cdd:PRK09544 70 ------GYVPQK-LYLDTTLPLTV-----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGET 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1188 QRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIV--IAHRL 1240
Cdd:PRK09544 127 QRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
403-616 |
5.53e-11 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.35 E-value: 5.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 403 YPSRANVKILKGLNLKVQSG-----QTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIrNFNVNYLReiigvvsq 477
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIK-------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 478 epVLFSTTIAEnicygrgnvTMDEIKKAVKEANAYEF-IMKlPQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 556
Cdd:cd03237 72 --ADYEGTVRD---------LLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 557 DEATSALDTESEAEVQAALDKAREG--RTTIVIAHrlsTVRNADVIAgfeDGVIVEQGSHSE 616
Cdd:cd03237 140 DEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH---DIIMIDYLA---DRLIVFEGEPSV 195
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
756-966 |
5.71e-11 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 64.80 E-value: 5.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 756 LIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALI 835
Cdd:cd18589 40 TVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 836 AQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKF 915
Cdd:cd18589 118 MWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGE 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 916 ESMYVEKLYGPYRNSVQKAHIYGI---TFSISQAFMyfsYAGCFRFGAYLIVNG 966
Cdd:cd18589 198 AQRYRQRLQKTYRLNKKEAAAYAVsmwTSSFSGLAL---KVGILYYGGQLVTAG 248
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1034-1255 |
6.27e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 63.03 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPT-RANVPVLQGLSLEVKKGQTLALVGSSGCGKSTvvqLLerfyDPLAG--TVFVDFGFQLLDGQEAKKL 1110
Cdd:cd03232 4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LL----DVLAGrkTAGVITGEILINGRPLDKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1111 nvqwLRAQLGIVSQEPILFDCS-IAENIAYGDNSRvvsqdeivsaakaanihpfietlphkyetrvgdkgtQLSGGQKQR 1189
Cdd:cd03232 77 ----FQRSTGYVEQQDVHSPNLtVREALRFSALLR------------------------------------GLSVEQRKR 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1190 IAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVFQNG 1255
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
113-331 |
7.95e-11 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 64.41 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 113 MTRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKV 192
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 193 GMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKI--------------LSAFsdkelaayakagavAEE 258
Cdd:cd18545 119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRarkawqrvrkkisnLNAY--------------LHE 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 259 ALGAIRTVIAFGGQNKELERYQKHLENAKEIGIkKAISANISMGIAFLLIYA-SYALAFWYGSTLVISKEYTIG 331
Cdd:cd18545 185 SISGIRVIQSFAREDENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG 257
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
410-589 |
8.46e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.11 E-value: 8.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLyDPDegtinIDGQDIR--NFNVNYLreiigvvSQEPVLFST-TI 486
Cdd:TIGR03719 19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKD-----FNGEARPqpGIKVGYL-------PQEPQLDPTkTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENICYGrgnvtMDEIKKAVKEANayEFIMKL---PQKFDTLVGERG--------------------------------- 530
Cdd:TIGR03719 86 RENVEEG-----VAEIKDALDRFN--EISAKYaepDADFDKLAAEQAelqeiidaadawdldsqleiamdalrcppwdad 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 531 -AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALdKAREGrTTIVIAH 589
Cdd:TIGR03719 159 vTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1048-1262 |
9.80e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.51 E-value: 9.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1048 NVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGTVFVdFGFQLLDgQEAKKlnvqwlRAQLGI---- 1121
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILF-KGESILD-LEPEE------RAHLGIflaf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 --------VSQEPILfdcsiaeNIAYgdNSRVVSQdeivsaaKAANIHP--FIETLPHKYETrVGDKGTQL--------S 1183
Cdd:CHL00131 91 qypieipgVSNADFL-------RLAY--NSKRKFQ-------GLPELDPleFLEIINEKLKL-VGMDPSFLsrnvnegfS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1184 GGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVFQNGRVKEH 1260
Cdd:CHL00131 154 GGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKT 233
|
..
gi 9961250 1261 GT 1262
Cdd:CHL00131 234 GD 235
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
711-974 |
9.87e-11 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 64.39 E-value: 9.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIaifgpgDDAVKQQKCN---IFSLIFLFLGIISFF-TFFLQGFtfgkaGEIL--- 783
Cdd:cd18549 4 FFLDLFCAVLIAALDLVFPLIVRYII------DDLLPSKNLRlilIIGAILLALYILRTLlNYFVTYW-----GHVMgar 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 784 -TRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVqgatgTRLA-------LIAqnIANLGTGIIISFIYGWQ 855
Cdd:cd18549 73 iETDMRRDLFEHLQKLSFSFFDNNK--TGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 856 LTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELeaaGKI---ATEAIENIRTVVSLTQE----RKFESMYVEklygpYR 928
Cdd:cd18549 144 LTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEInaqLEDSLSGIRVVKAFANEeyeiEKFDEGNDR-----FL 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 9961250 929 NSVQKAHIY-GITFSISQAFMYFSYAGCFRFGAYLIVNGHMRFRDVI 974
Cdd:cd18549 216 ESKKKAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLV 262
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
407-592 |
1.55e-10 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 65.54 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 407 ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgqdiRNFNVNYlreiigvVSQEPVLFSTTI 486
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----AKGKLFY-------VPQRPYMTLGTL 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENICYGRGnvTMDEIKKAVKEANAYEFIMKLpqKFDTLVGERGA---------QLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:TIGR00954 532 RDQIIYPDS--SEDMKRRGLSDKDLEQILDNV--QLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961250 558 EATSALDTESEaevQAALDKARE-GRTTIVIAHRLS 592
Cdd:TIGR00954 608 ECTSAVSVDVE---GYMYRLCREfGITLFSVSHRKS 640
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1034-1243 |
1.73e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.36 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYptRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgFQLLDGQEAKKLNVQ 1113
Cdd:PRK15056 7 IVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI---LGQPTRQALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 WLRAQLGIVSQEPILFDcSIAENIAYGDNS---RVVSQD-EIVSAAKAAnihpfIETLPHKYEtRVGdkgtQLSGGQKQR 1189
Cdd:PRK15056 82 YVPQSEEVDWSFPVLVE-DVVMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1190 IAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1243
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1061-1252 |
1.81e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 60.46 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1061 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfqlldgqeakkLNVQWLRAQLGIVSQEpilfdcsiaeniayg 1140
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------IDGEDILEEVLDQLLL--------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1141 dnsrvvsqdeivsaakaanihpfietlphkyeTRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVV 1220
Cdd:smart00382 52 --------------------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALL 99
|
170 180 190
....*....|....*....|....*....|....*....
gi 9961250 1221 QEALD-------KAREGRTCIVIAHRLSTIQNADLIVVF 1252
Cdd:smart00382 100 LLLEElrlllllKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
411-625 |
2.23e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQ-LIQRLydpDEGTINiDGQDIRNF---NVNYLReIIGVVSQEPV-LFSTT 485
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERV---TTGVIT-GGDRLVNGrplDSSFQR-SIGYVQQQDLhLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 486 IAENICYGRGNVTMDEIKKavKEANAY-EFIMKL---PQKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL-LDEAT 560
Cdd:TIGR00956 853 VRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPT 930
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 561 SALDTESEAEVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFEDGVIVEQGSHSelmkkegVYF 625
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFDRLLLLQKGGQT-------VYF 985
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
711-934 |
2.96e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 62.94 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFSVIFSEIIAIFGPGddavKQQKCNIFSLIFLFLG--IISFFTFFLQGFTFGKAGEILTRRLR 788
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIG----SKSLGLLLGLALLLLGayLLRALLNFLRIYLNHVAEQKVVADLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 789 SMAFKAMLRQDMSWFDDHknSTGALSTRLATDAAQVQgatgtRLAL--IAQNIANLGTGIIIS---FIYGWQLTLLLLAV 863
Cdd:cd18778 77 SDLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVE-----RLIAdgIPQGITNVLTLVGVAiilFSINPKLALLTLIP 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 864 VPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQERKfESMYVEKLYGPYRNSVQKA 934
Cdd:cd18778 150 IPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEE-EAKRFEALSRRYRKAQLRA 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1053-1238 |
3.36e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1053 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAKKL------NVQWLRAQLGIVS--- 1123
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEV-------LWQGEPIRRQrdeyhqDLLYLGHQPGIKTelt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1124 -QEPILFDCSIAeniaygdnsRVVSQDEIVSAAKAANIHPFiETLPHKyetrvgdkgtQLSGGQKQRIAIARALIRQPQI 1202
Cdd:PRK13538 91 aLENLRFYQRLH---------GPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961250 1203 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAH 1238
Cdd:PRK13538 151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
756-917 |
4.44e-10 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 62.53 E-value: 4.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 756 LIFLFLGIISFftffLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALI 835
Cdd:cd18564 62 GIALLRGLASY----AGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDLLVSGVLPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 836 AQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIV---EMKLLAgnakRDKKELEAA-GKIATEAIENIRTVVSLTQ 911
Cdd:cd18564 136 LTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRfsrRIKEAS----REQRRREGAlASVAQESLSAIRVVQAFGR 211
|
....*.
gi 9961250 912 ERKFES 917
Cdd:cd18564 212 EEHEER 217
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
147-338 |
4.75e-10 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 62.08 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 147 RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDdISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPI 226
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 227 LGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFL 306
Cdd:cd18570 154 YILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961250 307 LIYASYALAFWYGSTLVISKEYTIG-----NAMTVFF 338
Cdd:cd18570 234 ISLIGSLLILWIGSYLVIKGQLSLGqliafNALLGYF 270
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
755-968 |
6.69e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 61.74 E-value: 6.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 755 SLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLAL 834
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERET--SGRIMTRMTSDIDALSELLQTGLVQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 835 IAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKlLAGNAKRDKKElEAAGKIAT--EAIENIRTVVSLTQE 912
Cdd:cd18546 120 LVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-RIAAVNADlqETLAGIRVVQAFRRE 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 913 RKFESMYVEkLYGPYRNSVQKAHIYgitFSISQAFMYF----SYAGCFRFGAYLIVNGHM 968
Cdd:cd18546 198 RRNAERFAE-LSDDYRDARLRAQRL---VAIYFPGVELlgnlATAAVLLVGAWRVAAGTL 253
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1051-1280 |
1.48e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTvvqLLERFYDPLAGTVFVdfGFQLLDGqeaKKLNVQWLRaQLGIVSQEPILF- 1129
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKST---LLNALAGRIQGNNFT--GTILANN---RKPTKQILK-RTGFVTQDDILYp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIAYGDNSRV---VSQDEIVSAAKAAnihpFIETLPHKYE-TRVGDKGTQ-LSGGQKQRIAIARALIRQPQILL 1204
Cdd:PLN03211 154 HLTVRETLVFCSLLRLpksLTKQEKILVAESV----ISELGLTKCEnTIIGNSFIRgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1205 LDEATSALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHGTHQQLLAqkgiYFSMVSVQ 1280
Cdd:PLN03211 230 LDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1046-1262 |
2.05e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1046 RANVpVLQGLSLEVKKGQTLALVGSSGCGKSTvvqLLERFYDPLAGTVFVD----FGFQLLDGQEAKKLNVQWL---RAQ 1118
Cdd:PRK13547 12 RHRA-ILRDLSLRIEPGRVTALLGRNGAGKST---LLKALAGDLTGGGAPRgarvTGDVTLNGEPLAAIDAPRLarlRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1119 LGIVSQEPILFdcsiaeniaygdnsrvvSQDEIVS-------AAKAANIHPFIETLPHKYE-----TRVGDKGTQLSGGQ 1186
Cdd:PRK13547 88 LPQAAQPAFAF-----------------SAREIVLlgryphaRRAGALTHRDGEIAWQALAlagatALVGRDVTTLSGGE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1187 KQRIAIARAL---------IRQPQILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVFQN 1254
Cdd:PRK13547 151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLAD 230
|
....*...
gi 9961250 1255 GRVKEHGT 1262
Cdd:PRK13547 231 GAIVAHGA 238
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1055-1267 |
2.16e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1055 LSLEVKKGQTLALVGSSGCGKSTvvqLLERFYDPLAGTVFVDFGFQLLDGQEAKKLNVQwlRAQLgiVSQEPILF----- 1129
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLLPGSGSIQFAGQPLEAWSAAELARH--RAYL--SQQQTPPFampvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 ---DCSIAENIAYGDNSRVVsqDEIVSAAKaanihpfietLPHKYETRVGdkgtQLSGGQKQRIAIArALIRQ------P 1200
Cdd:PRK03695 88 qylTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwpdinP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 1201 --QILLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1267
Cdd:PRK03695 151 agQLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
753-968 |
2.40e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 60.22 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 753 IFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQG-ATGTR 831
Cdd:cd18563 44 LLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDfLSDGL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 832 LALIAQNIANLGTGIIIsFIYGWQLTLLLLAVVPIIAV-SGIVEMKLLAGNAKRDKKELEAAGKIAtEAIENIRTVVSLT 910
Cdd:cd18563 122 PDFLTNILMIIGIGVVL-FSLNWKLALLVLIPVPLVVWgSYFFWKKIRRLFHRQWRRWSRLNSVLN-DTLPGIRVVKAFG 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 911 QErKFESMYVEKLYGPYRNSVQKAH--------IYGITFSISQAFMYFsyagcfrFGAYLIVNGHM 968
Cdd:cd18563 200 QE-KREIKRFDEANQELLDANIRAEklwatffpLLTFLTSLGTLIVWY-------FGGRQVLSGTM 257
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
405-613 |
2.62e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 59.55 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQ------LIQRLYDPDEGTINIDGQDirnfNVNYLREIIgVVSQE 478
Cdd:cd03271 4 KGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHLKKEQPGNHDRIE----GLEHIDKVI-VIDQS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 479 PV-------------LFsTTIAE---NICYG-RGNVTMDEIK---KAVKE------ANAYEFIMKLPQ---KFDTLV--- 526
Cdd:cd03271 79 PIgrtprsnpatytgVF-DEIRElfcEVCKGkRYNRETLEVRykgKSIADvldmtvEEALEFFENIPKiarKLQTLCdvg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 527 ------GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRN 596
Cdd:cd03271 158 lgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKC 237
|
250 260
....*....|....*....|...
gi 9961250 597 ADVI------AGFEDGVIVEQGS 613
Cdd:cd03271 238 ADWIidlgpeGGDGGGQVVASGT 260
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
419-592 |
2.77e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.30 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 419 VQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTI--NIDGQDIrnfnvnyLREIIGVVSQEpvLFSTTIAENICYGRGN 496
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddPPDWDEI-------LDEFRGSELQN--YFTKLLEGDVKVIVKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 497 VTMDEIKKAVKeANAYEFIMKLPQ--KFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 565
Cdd:cd03236 94 QYVDLIPKAVK-GKVGELLKKKDErgKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....*...
gi 9961250 566 ESEAEVQAALDK-AREGRTTIVIAHRLS 592
Cdd:cd03236 173 KQRLNAARLIRElAEDDNYVLVVEHDLA 200
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1055-1268 |
3.49e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1055 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PLAGTVFVDfGFQL-----LDGQEAKKLNVQWLRAQLGIVSqepil 1128
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFIN-GKPVdirnpAQAIRAGIAMVPEDRKRHGIVP----- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1129 fDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLphKYETRVGDKG-TQLSGGQKQRIAIARALIRQPQILLLDE 1207
Cdd:TIGR02633 353 -ILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 1208 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK----EHG-THQQLLA 1268
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1050-1250 |
4.12e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.73 E-value: 4.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVFVDfgfqllDG--QEAKKLNVQWL-----RAQLGIV 1122
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLD------DGriIYEQDLIVARLqqdppRNVEGTV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 sqepilFDcSIAENIA--------YGDNSRVVSQDEivSAAKAANIHPFIETLPH----KYETRVGD-----------KG 1179
Cdd:PRK11147 84 ------YD-FVAEGIEeqaeylkrYHDISHLVETDP--SEKNLNELAKLQEQLDHhnlwQLENRINEvlaqlgldpdaAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1180 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIV 1250
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIV 224
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
125-345 |
5.08e-09 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 59.00 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 125 AGVLVAAYI-------QVSFWTLAAGRQI-RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISE----GIGDkv 192
Cdd:cd18549 45 GAILLALYIlrtllnyFVTYWGHVMGARIeTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 193 gmFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQ 272
Cdd:cd18549 123 --LFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANE 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 273 NKELERYQK---HLENAKEIGIKkaISANISMGIAFL--LIYASyALAFwyGSTLVISKEYTIGNAMTvfFSILIGAF 345
Cdd:cd18549 201 EYEIEKFDEgndRFLESKKKAYK--AMAYFFSGMNFFtnLLNLV-VLVA--GGYFIIKGEITLGDLVA--FLLYVNVF 271
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1052-1252 |
5.17e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1052 LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlldgqeaKKLNV----QWLRA-QLGI 1121
Cdd:PRK13409 350 LGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD-------------PELKIsykpQYIKPdYDGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 VSQepilFDCSIAENIaygDNSRVvsQDEIvsaakaanIHPFieTLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQ 1201
Cdd:PRK13409 417 VED----LLRSITDDL---GSSYY--KSEI--------IKPL--QLERLLDKNVKD----LSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1202 ILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVF 1252
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMVF 527
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1055-1262 |
7.30e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 7.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1055 LSLEVKKGQTLALVGSSGCGKSTvvqllerfyDPLAGTVFVDFGFQLL------DGQEAKKLNVQWLR----AQLGIVSQ 1124
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSV---------SSLAIMGLIDYPGRVMaeklefNGQDLQRISEKERRnlvgAEVAMIFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1125 EPI--LFDC-----SIAENIAY--GDNSRVVSQD--EIVSAAKAANIHPFIETLPHkyetrvgdkgtQLSGGQKQRIAIA 1193
Cdd:PRK11022 97 DPMtsLNPCytvgfQIMEAIKVhqGGNKKTRRQRaiDLLNQVGIPDPASRLDVYPH-----------QLSGGMSQRVMIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1194 RALIRQPQILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGT 1262
Cdd:PRK11022 166 MAIACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1038-1247 |
7.40e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.27 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1038 EVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFvdfgfqlLDGQEAKKLNVQWlRA 1117
Cdd:PRK13540 6 ELDFDYHDQ---PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL-------FERQSIKKDLCTY-QK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1118 QLGIVSQEP-ILFDCSIAENIAYG--DNSRVVSQDEIVSaakaanihpfIETLPHKYETRVGdkgtQLSGGQKQRIAIAR 1194
Cdd:PRK13540 75 QLCFVGHRSgINPYLTLRENCLYDihFSPGAVGITELCR----------LFSLEHLIDYPCG----LLSSGQKRQVALLR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1195 ALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1247
Cdd:PRK13540 141 LWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
711-869 |
8.95e-09 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 58.26 E-value: 8.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 711 FVVGTVCAIANGGLQPAFsvIFSEIIaifgpgDDAVKQQKCNIFSLIFLFL---GIISFFTFFLQGFTFGKAGEILTRRL 787
Cdd:cd18550 3 LVLLLILLSALLGLLPPL--LLREII------DDALPQGDLGLLVLLALGMvavAVASALLGVVQTYLSARIGQGVMYDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 788 RSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPII 867
Cdd:cd18550 75 RVQLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLF 152
|
..
gi 9961250 868 AV 869
Cdd:cd18550 153 VL 154
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
411-593 |
1.06e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 411 ILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQ-RLYDPD-EGTINIDGqdiRNFNVNYLREIiGVVSQEPVLFS-TTIA 487
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILKRT-GFVTQDDILYPhLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 488 ENICYGRGNVTMDEIKKAVKEANAYEFI--MKLPQKFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190
....*....|....*....|....*....|..
gi 9961250 563 LD-TESEAEVQAALDKAREGRTTIVIAHRLST 593
Cdd:PLN03211 237 LDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
394-616 |
1.17e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.18 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRAnvkILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIdGQDIRNFNVNYLREIIg 473
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 vvsqEPvlfSTTIAENICYGrgnvtMDEIKKAVKEAN--AY--EFIMKLP--QKfdtLVGergaQLSGGQKQRIAIARAL 547
Cdd:TIGR03719 398 ----DP---NKTVWEEISGG-----LDIIKLGKREIPsrAYvgRFNFKGSdqQK---KVG----QLSGGERNRVHLAKTL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 548 VRNPKILLLDEATSALDTESEAEVQAALDKAreGRTTIVIAH-RLSTVRNADVIAGFEDGVIVE--QGSHSE 616
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
395-566 |
1.52e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 395 EFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQ-DIRNFNvNYlREIIg 473
Cdd:PRK11147 321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFD-QH-RAEL- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 vvsqEPvlfSTTIAENICYGRGNVTMDEIKKAVKeanAY--EFIMKlPQKFDTLVgergAQLSGGQKQRIAIARALVRNP 551
Cdd:PRK11147 395 ----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLKPS 459
|
170
....*....|....*
gi 9961250 552 KILLLDEATSALDTE 566
Cdd:PRK11147 460 NLLILDEPTNDLDVE 474
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
394-623 |
2.28e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 58.36 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgqdiRNFNVNY------ 467
Cdd:PRK15064 320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS----ENANIGYyaqdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 468 --------LREIIGVVSQ----EPVLFSTtiaenicYGRGNVTMDEIKKAVKeanayefimklpqkfdtlvgergaQLSG 535
Cdd:PRK15064 393 ydfendltLFDWMSQWRQegddEQAVRGT-------LGRLLFSQDDIKKSVK------------------------VLSG 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 536 GQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKArEGrTTIVIAH------RLSTvrnaDVIAGFEDGVIV 609
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
|
250
....*....|....
gi 9961250 610 EQGSHSELMKKEGV 623
Cdd:PRK15064 516 FSGTYEEYLRSQGI 529
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
99-347 |
2.84e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 56.81 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 99 SLSLLNPGKILEEEMTRYAYYYSGL--GAGVL--VAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELN 174
Cdd:cd18565 35 SFLPLVPASLGPADPRGQLWLLGGLtvAAFLLesLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLM 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 175 TRLTDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGA 254
Cdd:cd18565 115 SVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 255 VAEEALGAIRTVIAFGGQNKELERYQKHLENAKEigikKAISAnISMGIAF-----LLIYASYALAFWYGSTLVISKEYT 329
Cdd:cd18565 195 RLENNLSGIAVIKAFTAEDFERERVADASEEYRD----ANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPL 269
|
250
....*....|....*...
gi 9961250 330 IGNAMTVffsiliGAFSV 347
Cdd:cd18565 270 FTGTLTV------GTLVT 281
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
379-589 |
3.26e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 379 SFSERGHKPDSikgnleFNDVHFSYPSRanVKILKGLNLKVQSGQ-----TVALVGSSGCGKSTTVQLIQRLYDPDEGTI 453
Cdd:PRK13409 325 EFEERPPRDES------ERETLVEYPDL--TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 454 NIDgqdIRnfnVNYLREIIGVVSQEPV-LFSTTIAENIcygRGNVTMDEIKKAvkeanayefiMKLPQKFDTLVGErgaq 532
Cdd:PRK13409 397 DPE---LK---ISYKPQYIKPDYDGTVeDLLRSITDDL---GSSYYKSEIIKP----------LQLERLLDKNVKD---- 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAH 589
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1174-1250 |
3.75e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.08 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1174 RVGDKGTQLSGGQKQRIAIARALIRQ---PQILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLI 1249
Cdd:cd03271 162 KLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
.
gi 9961250 1250 V 1250
Cdd:cd03271 242 I 242
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
394-572 |
3.83e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 394 LEFNDVHFSYPsrANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTInidgqdIRNFNVNylreiIG 473
Cdd:PLN03073 509 ISFSDASFGYP--GGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 474 VVSQEPV----LFSTTIaenicygrgnVTMDEIKKAVKEanayefimklpQKFDTLVGERGAQ----------LSGGQKQ 539
Cdd:PLN03073 576 VFSQHHVdgldLSSNPL----------LYMMRCFPGVPE-----------QKLRAHLGSFGVTgnlalqpmytLSGGQKS 634
|
170 180 190
....*....|....*....|....*....|....
gi 9961250 540 RIAIARALVRNPKILLLDEATSALDTES-EAEVQ 572
Cdd:PLN03073 635 RVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
410-567 |
4.23e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 410 KILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLyDPDegtinIDGQDIR--NFNVNYLreiigvvSQEPVLFST-TI 486
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-DKE-----FEGEARPapGIKVGYL-------PQEPQLDPEkTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENICYGrgnvtMDEIKKAVKEANAYEFIMKLPQ-KFDTLVGERG----------------------------------A 531
Cdd:PRK11819 88 RENVEEG-----VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcppwdakvT 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 9961250 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 567
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1056-1269 |
5.00e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.95 E-value: 5.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1056 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDF------GFQlldgQEAKKLNVQWLRAQLGIVSQEPILF 1129
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFshitrlSFE----QLQKLVSDEWQRNNTDMLSPGEDDT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1130 DCSIAENIaygdnsrvvsQDEIVSAAK----AANIHpfIETL---PHKYetrvgdkgtqLSGGQKQRIAIARALIRQPQI 1202
Cdd:PRK10938 99 GRTTAEII----------QDEVKDPARceqlAQQFG--ITALldrRFKY----------LSTGETRKTLLCQALMSEPDL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1203 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1269
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
123-341 |
5.73e-08 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 55.95 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 123 LGAGVLVAAYIQVSFWT---LAAGRQIRkIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGdKVGMFFQAV 199
Cdd:cd18543 46 LALGVAEAVLSFLRRYLagrLSLGVEHD-LRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 200 ATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERY 279
Cdd:cd18543 124 LTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRF 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 280 QKHLENAKEIGIKKA-ISANISMGIAfLLIYASYALAFWYGSTLVISKEYTIGnAMTVFFSIL 341
Cdd:cd18543 204 EAAARRLRATRLRAArLRARFWPLLE-ALPELGLAAVLALGGWLVANGSLTLG-TLVAFSAYL 264
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
385-609 |
6.90e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 385 HKPDSIKGN-LEFNDVHFSYPSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPD-EGTINIDGQ--DI 460
Cdd:TIGR02633 248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 461 RN---------FNVNYLREIIGVVSQEPVLFSTTIAENICY-GRGNVT----MDEIKKAVKEANAYEFIMKLPQkfdtlv 526
Cdd:TIGR02633 328 RNpaqairagiAMVPEDRKRHGIVPILGVGKNITLSVLKSFcFKMRIDaaaeLQIIGSAIQRLKVKTASPFLPI------ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 527 gergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVrnadviAGFED 605
Cdd:TIGR02633 402 ----GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV------LGLSD 471
|
....
gi 9961250 606 GVIV 609
Cdd:TIGR02633 472 RVLV 475
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1038-1268 |
7.44e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.48 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1038 EVVF---NY----PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLA--GTVFvdfgfqlLDGQEAK 1108
Cdd:PRK13549 257 EVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIF-------IDGKPVK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1109 KLN-VQWLRAQLGIVSQEP----ILFDCSIAENIAYGDNSRVVSQDEIVSAAKAANIHPFIETLPHKY---ETRVGdkgt 1180
Cdd:PRK13549 329 IRNpQQAIAQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTaspELAIA---- 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1181 QLSGGQKQRIAIARALIRQPQILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVFQNG 1255
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEG 481
|
250
....*....|....*...
gi 9961250 1256 RVK-----EHGTHQQLLA 1268
Cdd:PRK13549 482 KLKgdlinHNLTQEQVME 499
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
761-968 |
8.29e-08 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 55.28 E-value: 8.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 761 LGIISFFTFFLQGF---TFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQGATGTRLALIAQ 837
Cdd:cd18566 48 VVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLTGQALLALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 838 NIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAIENIRTVVSLTQE----R 913
Cdd:cd18566 125 DLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEpqmlR 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 914 KFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMyfsyAGCFRFGAYLIVNGHM 968
Cdd:cd18566 205 RYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM----VAVVAFGALLVINGDL 255
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
708-968 |
8.73e-08 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 55.18 E-value: 8.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 708 WPYFVVGTVCAIANGGLQPAFSVIFSEII-AIFGPGDDAvkqqkcNIFSLIFLFLGIISFFTFFLQGFTF--GKAGEILT 784
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIdHFITPGTLD------GLTGFILLYLGLILIQALSVFLFIRlaGKIEMGVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 785 RRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIAQNIANLGTGIIISFIYGWQLTLLLLAVV 864
Cdd:cd18540 75 YDLRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 865 PIIA-VSGIVEMKLLAGNAKRDKKELEAAGKIaTEAIENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSI 943
Cdd:cd18540 153 PVLAvVSIYFQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPI 231
|
250 260
....*....|....*....|....*
gi 9961250 944 SQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18540 232 VLFLGSIATALVLWYGGILVLAGAI 256
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1043-1262 |
9.38e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 54.72 E-value: 9.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1043 YPTRANVPVLQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDfgfqlldgqeakklnvqwlra 1117
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1118 qLGIVSQEPilfdcsiaENIAYGDNSRVvsQDEIVSAAKAANIHPFIET---LPHKYETRVGDKGTQLSGGQKQRIAIAR 1194
Cdd:cd03237 60 -LDTVSYKP--------QYIKADYEGTV--RDLLSSITKDFYTHPYFKTeiaKPLQIEQILDREVPELSGGELQRVAIAA 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 1195 ALIRQPQILLLDEATSALDTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVFQnGRVKEHGT 1262
Cdd:cd03237 129 CLSKDADIYLLDEPSAYLDVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
752-968 |
9.57e-08 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 55.17 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGA-TGT 830
Cdd:cd18545 40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLlSNG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 831 RLALIAQNIANLGTgIIISFIYGWQLTLLLLAVVPIIAVSgiveMKLLAGNAKRDKKELEAagKIAT------EAIENIR 904
Cdd:cd18545 118 LINLIPDLLTLVGI-VIIMFSLNVRLALVTLAVLPLLVLV----VFLLRRRARKAWQRVRK--KISNlnaylhESISGIR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 905 TVVSLTQE----RKFESMyVEKLYGPYRNSVQKAHIYG----ITFSISQAFMYFsyagcfrFGAYLIVNGHM 968
Cdd:cd18545 191 VIQSFAREdeneEIFDEL-NRENRKANMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
716-974 |
1.32e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 54.91 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 716 VCAIANGGLQPAFSVIFSEIIaifgpgdDAVKQQKcNIFSLIFLFLGIISFFTF-----FLQGFTFGKAGEILTRRLRSM 790
Cdd:cd18782 9 ALSFVVQLLGLANPLLFQVII-------DKVLVQQ-DLATLYVIGVVMLVAALLeavltALRTYLFTDTANRIDLELGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 791 AFKAMLRQDMSWFDdhKNSTGALSTRLAtDAAQVQG-ATGTRLALIAQNIANLGTgIIISFIYGWQLTLLLLAVVPIIAV 869
Cdd:cd18782 81 IIDHLLRLPLGFFD--KRPVGELSTRIS-ELDTIRGfLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 870 SGIVEMKLLagnAKRDKKELEAAGKIAT---EAIENIRTVVSLTQERKFESMYvEKLYGPYRNSVQKAHIYGITFS-ISQ 945
Cdd:cd18782 157 LTFLFGPIL---RRQIRRRAEASAKTQSylvESLTGIQTVKAQNAELKARWRW-QNRYARSLGEGFKLTVLGTTSGsLSQ 232
|
250 260
....*....|....*....|....*....
gi 9961250 946 AFMYFSYAGCFRFGAYLIVNGHMRFRDVI 974
Cdd:cd18782 233 FLNKLSSLLVLWVGAYLVLRGELTLGQLI 261
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1044-1257 |
1.44e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1044 PTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdFGFqllDGQEAKKLNVQwlraQLGIV- 1122
Cdd:COG4586 30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV-LGY---VPFKRRKEFAR----RIGVVf 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1123 ---SQepILFDCSIAENIA-----YGdnsrvVSQDEIvsaakAANIHPFIETLphkyetRVGDKGT----QLSGGQKQRI 1190
Cdd:COG4586 102 gqrSQ--LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVELL------DLGELLDtpvrQLSLGQRMRC 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1191 AIARALIRQPQILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1257
Cdd:COG4586 164 ELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
409-588 |
1.74e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.89 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKST-----TVQLIQRLYDpDEGTINIDGQDIRNFNVNYLREIIgVVSQEPVLF- 482
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGITPEEIKKHYRGDVV-YNAETDVHFp 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 483 STTIAENI-----CYGRGNVTM--DEIKKAVKEANAYEFIMKLPQKFDTLVGE---RGaqLSGGQKQRIAIARALVRNPK 552
Cdd:TIGR00956 152 HLTVGETLdfaarCKTPQNRPDgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAK 229
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961250 553 ILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIA 588
Cdd:TIGR00956 230 IQCWDNATRGLDSATALEFIRALkTSANILDTTPLVA 266
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1180-1216 |
1.85e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.51 E-value: 1.85e-07
10 20 30
....*....|....*....|....*....|....*..
gi 9961250 1180 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTES 1216
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
404-594 |
2.02e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.32 E-value: 2.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 404 PSRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYdPD--EGTINIDGQ--DIRN------FNVNYL---RE 470
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDGKpvKIRNpqqaiaQGIAMVpedRK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFSTTIAENICYGRGNVtmdeIKKAVKEANAYEFIMKLPQKFDTLVgERGAQLSGGQKQRIAIARALVRN 550
Cdd:PRK13549 349 RDGIVPVMGVGKNITLAALDRFTGGSR----IDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQQKAVLAKCLLLN 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 9961250 551 PKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTV 594
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEV 468
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
417-567 |
2.06e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 417 LKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDgQDI----------RNF--NV-NYLREiiGVVSQEPVL-- 481
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLivarlqqdppRNVegTVyDFVAE--GIEEQAEYLkr 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 482 ---FSTTIAENicYGRGNVT-MDEIKKAVKEANAYEF-------IMKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRN 550
Cdd:PRK11147 101 yhdISHLVETD--PSEKNLNeLAKLQEQLDHHNLWQLenrinevLAQLGLDPDAALSS----LSGGWLRKAALGRALVSN 174
|
170
....*....|....*..
gi 9961250 551 PKILLLDEATSALDTES 567
Cdd:PRK11147 175 PDVLLLDEPTNHLDIET 191
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1058-1262 |
2.60e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 55.18 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1058 EVKKGQTLALVGSSGCGKSTVVQLLerfydplAGTVFVDfgfqllDGQEAKKLNV----QWLRAQLGIVSQEpILFDcSI 1133
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPD------EGEVDEDLKIsykpQYISPDYDGTVEE-FLRS-AN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1134 AENIaygDNSRVvsQDEIvsaakaanIHPFieTLPHKYETRVGDkgtqLSGGQKQRIAIARALIRQPQILLLDEATSALD 1213
Cdd:COG1245 427 TDDF---GSSYY--KTEI--------IKPL--GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1214 TESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFqNGRVKEHGT 1262
Cdd:COG1245 488 VEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIDYiSDRLMVF-EGEPGVHGH 538
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1050-1269 |
2.69e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 53.26 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGTVfvdfgfqLLDGQEAKKLNVQwLRAQLGI--VSQE 1125
Cdd:PRK09580 15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTV-------EFKGKDLLELSPE-DRAGEGIfmAFQY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILFDcsiaeniayGDNSRVVSQDEIVSAAKAANIHP--------FIE------TLPHKYETRVGDKGtqLSGGQKQRIA 1191
Cdd:PRK09580 87 PVEIP---------GVSNQFFLQTALNAVRSYRGQEPldrfdfqdLMEekiallKMPEDLLTRSVNVG--FSGGEKKRND 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1192 IARALIRQPQILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVFQNGRVKEHGTH---QQ 1265
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQ 235
|
....
gi 9961250 1266 LLAQ 1269
Cdd:PRK09580 236 LEEQ 239
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1180-1216 |
2.94e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.94 E-value: 2.94e-07
10 20 30
....*....|....*....|....*....|....*..
gi 9961250 1180 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTES 1216
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
419-591 |
2.97e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 2.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 419 VQSGQTVALVGSSGCGKSTTVQLIQrlydpdegtinidGQDIRNFNvNYLREiigvVSQEPVL--FSTTIAENicYGR-- 494
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILS-------------GELIPNLG-DYEEE----PSWDEVLkrFRGTELQN--YFKkl 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 495 --GNVT-------MDEIKKAVKeANAYEFIMKLPQ--KFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKIL 554
Cdd:PRK13409 156 ynGEIKvvhkpqyVDLIPKVFK-GKVRELLKKVDErgKLDEVVERLGlenildrdiSELSGGELQRVAIAAALLRDADFY 234
|
170 180 190
....*....|....*....|....*....|....*..
gi 9961250 555 LLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRL 591
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1049-1256 |
3.03e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 3.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1049 VPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGQEAK-KLNVQWLRAQLGIVSQE-P 1126
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI-------LFQGKEIDfKSSKEALENGISMVHQElN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ILFDCSIAENIAYGDNSR---VVSQDEIVSAAKAANIHPFIETLPHkyetrvgDKGTQLSGGQKQRIAIARALIRQPQIL 1203
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYPTkgmFVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1204 LLDEATSALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVFQNGR 1256
Cdd:PRK10982 157 IMDEPTSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
405-612 |
3.45e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 51.55 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIqrLYDPDEGTINIDGQdirnfnvNYLREIIGVVSQepvlFST 484
Cdd:cd03238 4 SGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG--LYASGKARLISFLP-------KFSRNKLIFIDQ----LQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 485 TIAENICYgrgnvtmdeikkavkeanayefiMKLPQKFDTLvgergaqlSGGQKQRIAIARALVRNPK--ILLLDEATSA 562
Cdd:cd03238 71 LIDVGLGY-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTG 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 563 LDTESEAEVQAALDKAR-EGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQG 612
Cdd:cd03238 120 LHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
420-593 |
3.69e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.41 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 420 QSGQTVALVGSSGCGKSTTVQLIQrlydpdegtinidGQDIRNFNvNYLREiigvVSQEPVL--FSTTIAENicYGRgNV 497
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILS-------------GELKPNLG-DYDEE----PSWDEVLkrFRGTELQD--YFK-KL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 498 TMDEIKKAVKEanayEFIMKLPQKFDTLVG-------ERGA-------------------QLSGGQKQRIAIARALVRNP 551
Cdd:COG1245 156 ANGEIKVAHKP----QYVDLIPKVFKGTVRellekvdERGKldelaeklglenildrdisELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 9961250 552 KILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLST 593
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIrELAEEGKYVLVVEHDLAI 274
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1032-1225 |
3.69e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.57 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1032 GNITF--NEVVFNYPTRAnvpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVdfgfqlldgqeAKK 1109
Cdd:PRK11147 316 GKIVFemENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-----------GTK 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1110 LNVQWL---RAQLgivsqEPilfDCSIAENIAYGD-----NSR---VVS--QDEIVSAAKAANihpfietlPHKyetrvg 1176
Cdd:PRK11147 382 LEVAYFdqhRAEL-----DP---EKTVMDNLAEGKqevmvNGRprhVLGylQDFLFHPKRAMT--------PVK------ 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 9961250 1177 dkgtQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD 1225
Cdd:PRK11147 440 ----ALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
511-617 |
3.75e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 54.63 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 511 AYEFIMKLP---QKFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAE----V 571
Cdd:TIGR00630 796 AYEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLHFDDIKKllevL 875
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 572 QAALDKareGRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQGSHSEL 617
Cdd:TIGR00630 876 QRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
125-345 |
4.10e-07 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 53.31 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 125 AGVLVAAYIQVSFWT--------LAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFF 196
Cdd:cd18778 43 ALLLLGAYLLRALLNflriylnhVAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 197 QAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKEL 276
Cdd:cd18778 123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 277 ERYQKHLENAKeigiKKAISANISMGIAFLLIY----ASYALAFWYGSTLVISKEYTIGNamTVFFSILIGAF 345
Cdd:cd18778 203 KRFEALSRRYR----KAQLRAMKLWAIFHPLMEfltsLGTVLVLGFGGRLVLAGELTIGD--LVAFLLYLGLF 269
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
123-343 |
4.31e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 52.98 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 123 LGAGVLVAAYIQVSF-------WTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLtDDISKISEGIGDKVGMF 195
Cdd:cd18782 44 IGVVMLVAALLEAVLtalrtylFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 196 FQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAfggQNKE 275
Cdd:cd18782 123 LLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA---QNAE 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 276 L-------ERYQKHLENAKEIGIKKAISANISMGIAFLliyaSYALAFWYGSTLVISKEYTIGNAMTvfFSILIG 343
Cdd:cd18782 200 LkarwrwqNRYARSLGEGFKLTVLGTTSGSLSQFLNKL----SSLLVLWVGAYLVLRGELTLGQLIA--FRILSG 268
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1174-1250 |
4.37e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 54.63 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1174 RVGDKGTQLSGGQKQRIAIARALIRQ---PQILLLDEATSALDTESEK----VVQEALDKareGRTCIVIAHRLSTIQNA 1246
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTA 898
|
....
gi 9961250 1247 DLIV 1250
Cdd:TIGR00630 899 DYII 902
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
401-589 |
5.28e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 5.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 401 FSYPSRanVKILKGLNLKVQSGQ-----TVALVGSSGCGKSTTVQLIQRLYDPDEGTINidgQDIRnfnVNYLREIIGVV 475
Cdd:COG1245 342 VEYPDL--TKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLK---ISYKPQYISPD 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 476 SQEPV--LFSTTIAENIcygRGNVTMDEIKKAvkeanayefiMKLPQKFDTLVGErgaqLSGGQKQRIAIARALVRNPKI 553
Cdd:COG1245 414 YDGTVeeFLRSANTDDF---GSSYYKTEIIKP----------LGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADL 476
|
170 180 190
....*....|....*....|....*....|....*...
gi 9961250 554 LLLDEATSALDTESEAEVQAALDKAREGR--TTIVIAH 589
Cdd:COG1245 477 YLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
154-343 |
5.58e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 52.97 E-value: 5.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 154 FHAILRQEIGWFDINDTTELNTRLTDdISKISEgigdkvgmFF--QAVATF----FAG--FIVGFIRGWKLTLVIMAISP 225
Cdd:cd18566 82 FEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLALldlpFVLifLGLIWYLGGKLVLVPLVLLG 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 226 ILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAF 305
Cdd:cd18566 153 LFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQ 232
|
170 180 190
....*....|....*....|....*....|....*...
gi 9961250 306 LLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIG 343
Cdd:cd18566 233 LFSQVSMVAVVAFGALLVINGDLTVG--ALIACTMLSG 268
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
416-618 |
6.24e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 6.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 416 NLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIG---------VVSQEPVLFSTTI 486
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSdewqrnntdMLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 487 AENIcygrgnvtMDEIKKAvkeanayEFIMKLPQKF--DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:PRK10938 103 AEII--------QDEVKDP-------ARCEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 9961250 565 TESEAEVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELM 618
Cdd:PRK10938 168 VASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEIL 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
412-648 |
6.40e-07 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQdirnfnVNYLREIIGVVSQepvlfsTTIAENI- 490
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE------VSVIAISAGLSGQ------LTGIENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 491 ----CYGrgnVTMDEIKKAVKEANAY----EFIMKLPQKFdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK13546 108 fkmlCMG---FKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 563 LDtesEAEVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSELMKKegvYFKLVNMQTSGSQI 637
Cdd:PRK13546 174 GD---QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAFLNDFKKKSKA 247
|
250
....*....|...
gi 9961250 638 QSEEF--ELNDEK 648
Cdd:PRK13546 248 EQKEFrnKLDESR 260
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1050-1272 |
6.55e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.74 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1050 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqlldgqeakklnvQWL-RAQLGIVSQEP-- 1126
Cdd:PRK15064 333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------------KWSeNANIGYYAQDHay 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1127 ------ILFDCsIAENIAYGDNSRVV---------SQDEIVSAAKAanihpfietlphkyetrvgdkgtqLSGGQKQRIA 1191
Cdd:PRK15064 394 dfendlTLFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVKV------------------------LSGGEKGRML 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1192 IARALIRQPQILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVFQNGRVKEHGTHQQ 1265
Cdd:PRK15064 449 FGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEE 522
|
....*..
gi 9961250 1266 LLAQKGI 1272
Cdd:PRK15064 523 YLRSQGI 529
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1034-1264 |
7.48e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.71 E-value: 7.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPtraNVPVL-QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVD-------FGFQLLDGQ 1105
Cdd:PLN03073 509 ISFSDASFGYP---GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSakvrmavFSQHHVDGL 585
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1106 EakklnvqwlraqlgiVSQEPILFdcsiaeniaygdnsrvvsqdeivsaakaaNIHPFIETLPHKYETRVGDKGTQ---- 1181
Cdd:PLN03073 586 D---------------LSSNPLLY-----------------------------MMRCFPGVPEQKLRAHLGSFGVTgnla 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1182 ------LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVFQN 1254
Cdd:PLN03073 622 lqpmytLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSE 699
|
250
....*....|.
gi 9961250 1255 GRVKE-HGTHQ 1264
Cdd:PLN03073 700 GKVTPfHGTFH 710
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
404-616 |
8.46e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.38 E-value: 8.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 404 PSRANVKILKG------LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRnfnVNYLREII--GVV 475
Cdd:PRK11288 255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---IRSPRDAIraGIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 476 ------SQEPVLFSTTIAENICYG--RGNVTMDEIKKAVKEA-NAYEFIMKLPQKF---DTLVGergaQLSGGQKQRIAI 543
Cdd:PRK11288 332 lcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAIL 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 544 ARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVIVEQGSHSE 616
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
752-968 |
8.95e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 52.13 E-value: 8.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRlATDAAQVQGATGTR 831
Cdd:cd18555 42 NVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE--NRSSGDLLFR-ANSNVYIRQILSNQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 832 LALIAQNIANLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLagnAKRDKKELEAAGK---IATEAIENIRTVVS 908
Cdd:cd18555 119 VISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKI---KKLNQEEIVAQTKvqsYLTETLYGIETIKS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 909 LTQERKF----ESMYVEKLygpyRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18555 196 LGSEKNIykkwENLFKKQL----KAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
405-600 |
1.35e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 53.29 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSTTV---------QLIQRLYDP----DEGTI--------NIDGQDIRNF 463
Cdd:PRK00635 604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLIndtlvpaveEFIEQGFCSnlsiQWGAIsrlvhitrDLPGRSQRSI 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 464 NVNYLR---EIIGVVSQEP-----------VLFSTTIAENI-CYGRGNVT-MD--------------------EIKKAVK 507
Cdd:PRK00635 684 PLTYIKafdDLRELFAEQPrskrlgltkshFSFNTPLGACAeCQGLGSITtTDnrtsipcpsclgkrflpqvlEVRYKGK 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 508 ------EANAYE---FIMKLP---QKFDTL---------VGERGAQLSGGQKQRIAIARAL---VRNPKILLLDEATSAL 563
Cdd:PRK00635 764 niadilEMTAYEaekFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGL 843
|
250 260 270
....*....|....*....|....*....|....*...
gi 9961250 564 DTES-EAEVQAALDKAREGRTTIVIAHRLSTVRNADVI 600
Cdd:PRK00635 844 HTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
151-345 |
1.62e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 51.36 E-value: 1.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 151 QKFFHAILRQEIGWFDINDTTELNTRLtDDISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLS 230
Cdd:cd18555 79 SDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLL 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 231 AAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYA 310
Cdd:cd18555 158 LLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFI 237
|
170 180 190
....*....|....*....|....*....|....*
gi 9961250 311 SYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAF 345
Cdd:cd18555 238 APLLILWIGAYLVINGELTLG--ELIAFSSLAGSF 270
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
409-614 |
1.84e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLI--QRLYDPDEGTINIDG-----------------QDIRNFNVN--- 466
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqetfarisgyceqNDIHSPQVTvre 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 467 ------YLREIIGVVSQEPVLFSTTIAENicygrgnVTMDEIKKAvkeanayefIMKLPqkfdtlvGERGaqLSGGQKQR 540
Cdd:PLN03140 973 sliysaFLRLPKEVSKEEKMMFVDEVMEL-------VELDNLKDA---------IVGLP-------GVTG--LSTEQRKR 1027
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 541 IAIARALVRNPKILLLDEATSALDTESEAEVQAAL-DKAREGRTTIVIAHRLSTvrnaDVIAGFEDGVIVEQGSH 614
Cdd:PLN03140 1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1181-1252 |
1.94e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 1.94e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9961250 1181 QLSGGQKQRIAIARALIRQPQILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVF 1252
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
429-564 |
2.30e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 429 GSSGCGKSTTVQLIQRLYDPDEGTINIDGQ--DIRNFNVnylREIIGVVSQEpvlFSTtiaenicYG----RGN------ 496
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT---RRRVGYMSQA---FSL-------YGeltvRQNlelhar 365
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9961250 497 ---VTMDEIKKAVKEanayefimkLPQKFD--TLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 564
Cdd:NF033858 366 lfhLPAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1012-1271 |
2.92e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.94 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1012 ERQPLIDSyseeGLKPDKFEgnitFNEVVFNYPTRANvPVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerfydplag 1091
Cdd:TIGR01257 1924 ERQRIISG----GNKTDILR----LNELTKVYSGTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTT------------- 1981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1092 tvfvdfgFQLLDGQEAkklnvqwLRAQLGIVSQEPILFDCS-IAENIAYGDNSRVVsqDEIVSAAKAANIHPFIETLPHK 1170
Cdd:TIGR01257 1982 -------FKMLTGDTT-------VTSGDATVAGKSILTNISdVHQNMGYCPQFDAI--DDLLTGREHLYLYARLRGVPAE 2045
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1171 YETRVGDKGTQ--------------LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIV 1235
Cdd:TIGR01257 2046 EIEKVANWSIQslglslyadrlagtYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVL 2125
|
250 260 270
....*....|....*....|....*....|....*..
gi 9961250 1236 IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQKG 1271
Cdd:TIGR01257 2126 TSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1059-1251 |
3.26e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.35 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1059 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydplAGTVFVDFGFQLLDGQeakklnvqwLRA 1117
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQNYFKKLYNGE---------IKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1118 QLGI--VSQEPILFDCSIAENIAYGDNSRVVsqDEIVsaaKAANIHPFIetlphkyetrvgDKG-TQLSGGQKQRIAIAR 1194
Cdd:PRK13409 163 VHKPqyVDLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGLENIL------------DRDiSELSGGELQRVAIAA 225
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1195 ALIRQPQILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVV 1251
Cdd:PRK13409 226 ALLRDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHI 283
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
752-968 |
3.65e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 50.25 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIFLFLGI----ISFFTFFLQGFTFGKageiLTRRLRSMAFKAMLRQDMSWFDDHKnsTGALSTRLATDaaQVQGA 827
Cdd:cd18568 42 NLILIGLLIVGIfqilLSAVRQYLLDYFANR----IDLSLLSDFYKHLLSLPLSFFASRK--VGDIITRFQEN--QKIRR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 828 TGTRLALIAqnIANLGTGII---ISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAkrdKKELEAAGKIAT---EAIE 901
Cdd:cd18568 114 FLTRSALTT--ILDLLMVFIylgLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNS---REIFQANAEQQSflvEALT 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 902 NIRTVVSLTQERKFESmYVEKLYGPYRNSVQKAHIYGITFS-ISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18568 189 GIATIKALAAERPIRW-RWENKFAKALNTRFRGQKLSIVLQlISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1182-1268 |
5.35e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.77 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1182 LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGRV-- 1257
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsg 475
|
90
....*....|....
gi 9961250 1258 ---KEHGTHQQLLA 1268
Cdd:PRK10762 476 eftREQATQEKLMA 489
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
384-591 |
5.93e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.17 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 384 GHKPDSIKGNlEFNDVHFSYPSRANVKILKGlnlkVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNf 463
Cdd:TIGR01257 1932 GNKTDILRLN-ELTKVYSGTSSPAVDRLCVG----VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT- 2005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 464 NVNYLREIIGVVSQ-EPVLFSTTIAENI-CYGR-GNVTMDEIKKAvkeANAYEFIMKLPQKFDTLVGergaQLSGGQKQR 540
Cdd:TIGR01257 2006 NISDVHQNMGYCPQfDAIDDLLTGREHLyLYARlRGVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRK 2078
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 9961250 541 IAIARALVRNPKILLLDEATSALDTESEAEV-QAALDKAREGRTTIVIAHRL 591
Cdd:TIGR01257 2079 LSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
419-604 |
6.26e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.95 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 419 VQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGqdirnfnvnylreiigvvsqepvlfsttiaenicygrgnvt 498
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG----------------------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 499 mdeIKKAVKeanayefimklPQKFDtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKA 578
Cdd:cd03222 61 ---ITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 9961250 579 RE--GRTTIVIAHRLSTVRN-ADVIAGFE 604
Cdd:cd03222 118 SEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
429-600 |
6.61e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 6.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 429 GSSGCGKSTTVQLIQRLYDPDEGTINIdgqdiRNFNVNYLreiigvvsQEPvlFSTTIAENICYGRGNVTMDEIKKAVKE 508
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNI--------AKP--YCTYIGHNLGLKLEMTVFENLKFWSEI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 509 ANAYEFIMKLPQ--KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALD-KAREGRTTI 585
Cdd:PRK13541 98 YNSAETLYAAIHyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVL 177
|
170
....*....|....*
gi 9961250 586 VIAHRLSTVRNADVI 600
Cdd:PRK13541 178 LSSHLESSIKSAQIL 192
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
754-923 |
7.96e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 49.45 E-value: 7.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 754 FSLIFLFLGII-SFFTFFlQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRL 832
Cdd:cd18605 44 FLTVYGFLAGLnSLFTLL-RAFLFAYGGLRAARRLHNKLLSSILFAKMSFFD--KTPVGRILNRFSSDVYTIDDSLPFIL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 833 -ALIAQNIANLGTGIIISFIYGWqltlLLLAVVPIIAVSGIVEMKLLAGNakRDKKELEAA--GKIAT---EAIENIRTV 906
Cdd:cd18605 121 nILLAQLFGLLGYLVVICYQLPW----LLLLLLPLAFIYYRIQRYYRATS--RELKRLNSVnlSPLYThfsETLKGLVTI 194
|
170
....*....|....*..
gi 9961250 907 VSLTQERKFESMYVEKL 923
Cdd:cd18605 195 RAFRKQERFLKEYLEKL 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
375-598 |
8.76e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 8.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 375 PKIDSFSERGHKPDSIKgNLEFNDVHFSYPSRanvKILKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRlyDPDEGTIN 454
Cdd:PRK10938 243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGYSN 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 455 ---IDGQ---------DIRNFnvnylreiIGVVSQEPVL---FSTTIAENICYGrgnvTMDEIK--KAVKEANayefiMK 517
Cdd:PRK10938 317 dltLFGRrrgsgetiwDIKKH--------IGYVSSSLHLdyrVSTSVRNVILSG----FFDSIGiyQAVSDRQ-----QK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 518 LPQKFDTLVGERGAQ-------LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIV-- 586
Cdd:PRK10938 380 LAQQWLDILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfv 458
|
250 260
....*....|....*....|..
gi 9961250 587 ----------IAHRLSTVRNAD 598
Cdd:PRK10938 459 shhaedapacITHRLEFVPDGD 480
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
121-338 |
1.00e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 49.02 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 121 SGLGAGVLVAAYIQVSFWTLAAGRQ----IRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVGMFF 196
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 197 QAVATFFAGFIVGFIRGWKLTLVIMAISPILGLsAAVW----------------AKILSAFSdkelaayakagavaeEAL 260
Cdd:cd18546 122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-ATRWfrrrssrayrrareriAAVNADLQ---------------ETL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 261 GAIRTVIAFGGQNKELERYQKHLENAKEIGIKkaisANISMGIAF----LLIYASYALAFWYGSTLVISKEYTIGnAMTV 336
Cdd:cd18546 186 AGIRVVQAFRRERRNAERFAELSDDYRDARLR----AQRLVAIYFpgveLLGNLATAAVLLVGAWRVAAGTLTVG-VLVA 260
|
..
gi 9961250 337 FF 338
Cdd:cd18546 261 FL 262
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1182-1253 |
1.01e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.57 E-value: 1.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1182 LSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQ 1253
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1069-1249 |
1.08e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1069 GSSGCGKSTVVQLLERFYDPLAGTVFvdfgFQLLDGQEAKKLNVQWLRAQLGIVSqepilfDCSIAENIAYGdnSRVVSQ 1148
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIY----YKNCNINNIAKPYCTYIGHNLGLKL------EMTVFENLKFW--SEIYNS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1149 DEIVSAAkaanIHPFietlphKYETRVGDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALD-KA 1227
Cdd:PRK13541 101 AETLYAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKA 170
|
170 180
....*....|....*....|..
gi 9961250 1228 REGRTCIVIAHRLSTIQNADLI 1249
Cdd:PRK13541 171 NSGGIVLLSSHLESSIKSAQIL 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1142-1256 |
1.24e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1142 NSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGD---KGtqLSGGQKQRIAIARALIRQPQILLLDEATSALDTESek 1218
Cdd:TIGR00956 169 QNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT-- 244
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 9961250 1219 vvqeALDKAREGRTCIVIAHRLSTI------QNA----DLIVVFQNGR 1256
Cdd:TIGR00956 245 ----ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1034-1247 |
1.37e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1034 ITFNEVVFNYPTRanvPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-----ERFYDPLagtvfVDFGFQLLDGQ--- 1105
Cdd:PRK10938 261 IVLNNGVVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGYSNDL-----TLFGRRRGSGEtiw 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1106 EAKKlNVQWLRAQLGI---VS---QEPIL---FDcSIAENIAYGDNSRVVSQD--EIVSAAKAANIHPFietlpHkyetr 1174
Cdd:PRK10938 333 DIKK-HIGYVSSSLHLdyrVStsvRNVILsgfFD-SIGIYQAVSDRQQKLAQQwlDILGIDKRTADAPF-----H----- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1175 vgdkgtQLSGGQkQRIA-IARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAH 1238
Cdd:PRK10938 401 ------SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITH 471
|
....*....
gi 9961250 1239 RLSTIQNAD 1247
Cdd:PRK10938 472 RLEFVPDGD 480
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
114-233 |
1.44e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 48.27 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 114 TRYAYYYSGLGAGVLVAAYIQVSFWTLAAGRQI-RKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKV 192
Cdd:cd18580 38 GYYLGVYAALLVLASVLLVLLRWLLFVLAGLRAsRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLAL 117
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 9961250 193 GMFFQAVATFFAGFIvgfirgwkltlVIMAISPILGLSAAV 233
Cdd:cd18580 118 LDFLQSLFSVLGSLI-----------VIAIVSPYFLIVLPP 147
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
752-968 |
1.44e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 48.61 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 752 NIFSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFddHKNSTGALSTRL-ATDAAQvQGATGT 830
Cdd:cd18567 42 TVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF--EKRHLGDIVSRFgSLDEIQ-QTLTTG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 831 RLALIAQNIANLGTGIIIsFIYGWQLTLLLLAVVPIIAVsgiveMKLLAGNAKRDKKE--LEAAGKIATEAIENIRTVVS 908
Cdd:cd18567 119 FVEALLDGLMAILTLVMM-FLYSPKLALIVLAAVALYAL-----LRLALYPPLRRATEeqIVASAKEQSHFLETIRGIQT 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 909 L-------TQERKFESMYVEKLygpyrNSVQKAHIYGITFS-ISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18567 193 IklfgreaEREARWLNLLVDAI-----NADIRLQRLQILFSaANGLLFGLENILVIYLGALLVLDGEF 255
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
846-968 |
1.68e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 48.26 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 846 IIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRdKKELEAA-GKIATEAIENIRTVVSLTQERKFESMYVEKLY 924
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEE-KFQRGAEnQSFLVETVTGIETVKSLAVEPQFQRRWEELLA 211
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 9961250 925 GPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGAYLIVNGHM 968
Cdd:cd18588 212 RYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGEL 255
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
206-346 |
1.87e-05 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 48.26 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 206 FIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLEN 285
Cdd:cd18588 133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 286 AKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGnaMTVFFSILIGAFS 346
Cdd:cd18588 213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIG--QLIAFNMLAGQVS 271
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1047-1252 |
1.95e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.55 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1047 ANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ-------------LLERFYDPLagTVFVDfgfqlldgqeakklnvq 1113
Cdd:cd03238 6 ANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeglyasgkarlisFLPKFSRNK--LIFID----------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1114 wlraQLGIVsqepilfdcsIAENIAYgdnsrvvsqdeivsaakaanihpfietlphkyeTRVGDKGTQLSGGQKQRIAIA 1193
Cdd:cd03238 67 ----QLQFL----------IDVGLGY---------------------------------LTLGQKLSTLSGGELQRVKLA 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1194 RALIRQPQ--ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVF 1252
Cdd:cd03238 100 SELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
113-345 |
2.06e-05 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 47.86 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 113 MTRYA-------------YYYSGLGAGVLVAAYIQVSFWTLAAGRQ----IRKIRQKFFHAILRQEIGWFDINDTTELNT 175
Cdd:cd18540 24 LTKYAidhfitpgtldglTGFILLYLGLILIQALSVFLFIRLAGKIemgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 176 RLTDDISKISE----GIGDkvgmFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLsAAVW----------------A 235
Cdd:cd18540 104 RVTSDTQRLGEiiswGLVD----LVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV-VSIYfqkkilkayrkvrkinS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 236 KILSAFSdkelaayakagavaeEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANISMGIAFLLIYASYALA 315
Cdd:cd18540 179 RITGAFN---------------EGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALV 243
|
250 260 270
....*....|....*....|....*....|
gi 9961250 316 FWYGSTLVISKEYTIGnAMTVFFSILIGAF 345
Cdd:cd18540 244 LWYGGILVLAGAITIG-TLVAFISYATQFF 272
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1051-1242 |
2.98e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 48.39 E-value: 2.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTV---------FVDfgfQLLDGQEAKKlnvqwlraqlgi 1121
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIeigetvklaYVD---QSRDALDPNK------------ 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1122 vsqepilfdcSIAENIAYGDNSRVVSQDEIVSAAkaanihpfietlphkYETRVGDKGT-------QLSGGQKQRIAIAR 1194
Cdd:TIGR03719 402 ----------TVWEEISGGLDIIKLGKREIPSRA---------------YVGRFNFKGSdqqkkvgQLSGGERNRVHLAK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 9961250 1195 ALIRQPQILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAH------RLST 1242
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1056-1267 |
2.99e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.37 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1056 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVfvdfgfqLLDGqeaKKLNV----QWLRAqlGIV------SQE 1125
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQV-------YLDG---KPIDIrsprDAIRA--GIMlcpedrKAE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1126 PILFDCSIAENIAYGDNSRVVSQDEIVSAAK-AANIHPFIETLphKYETRVGD-KGTQLSGGQKQRIAIARALIRQPQIL 1203
Cdd:PRK11288 341 GIIPVHSVADNINISARRHHLRAGCLINNRWeAENADRFIRSL--NIKTPSREqLIMNLSGGNQQKAILGRWLSEDMKVI 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9961250 1204 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV-----KEHGTHQQLL 1267
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
405-621 |
3.27e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.24 E-value: 3.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 405 SRANVKILKGLNLKVQSGQTVALVGSSGCGKSttvQLIQRLYDPD---EGTINIDGQDIR-NFNVNYLREIIGVVSQ--- 477
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDkraGGEIRLNGKDISpRSPLDAVKKGMAYITEsrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 478 EPVLFST-TIAENICYGR--------GNVTMDEIKKAVKEANAYEFIMKLpqKFDTlVGERGAQLSGGQKQRIAIARALV 548
Cdd:PRK09700 349 DNGFFPNfSIAQNMAISRslkdggykGAMGLFHEVDEQRTAENQRELLAL--KCHS-VNQNITELSGGNQQKVLISKWLC 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 549 RNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFEDGVIVEQGSHSELMKKE 621
Cdd:PRK09700 426 CCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEE 500
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
412-588 |
4.12e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.80 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 412 LKGLNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFN-----------VNYLREIIGVVSQEPV 480
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 481 LFSTTIAeNICYGRGNVTMDEIKKAVKEANAYEFIM--KLPQKfDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDE 558
Cdd:PRK10982 344 GFNSLIS-NIRNYKNKVGLLDNSRMKSDTQWVIDSMrvKTPGH-RTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDE 417
|
170 180 190
....*....|....*....|....*....|.
gi 9961250 559 ATSALDTESEAEV-QAALDKAREGRTTIVIA 588
Cdd:PRK10982 418 PTRGIDVGAKFEIyQLIAELAKKDKGIIIIS 448
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
409-610 |
5.09e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 409 VKILKGLNLKVQSGQTVALVGSSGCGKSTTVqLIQRLYDPDEGTinidgqdiRNF-------NVNYLREIIGVvsQEPVL 481
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWrf*twcaNRRALRRTIG*--HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 482 FSTTIAENicyGRGNVTMD----EIKKAVKEANAYEFIMKLpqKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 557
Cdd:NF000106 95 *GRRESFS---GRENLYMIgr*lDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 558 EATSALDTESEAEV-QAALDKAREGRTTIV----------IAHRLSTVRNADVIAgfeDGVIVE 610
Cdd:NF000106 170 EPTTGLDPRTRNEVwDEVRSMVRDGATVLLttqymeeaeqLAHELTVIDRGRVIA---DGKVDE 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
533-571 |
5.72e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 5.72e-05
10 20 30
....*....|....*....|....*....|....*....
gi 9961250 533 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEV 571
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI 434
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1181-1273 |
6.04e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 6.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1181 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARegRTCIVIAHRLStiqnadlivvFQNGRVKE- 1259
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHARE----------FLNTVVTDi 411
|
90
....*....|....*
gi 9961250 1260 -HGTHQQLLAQKGIY 1273
Cdd:PLN03073 412 lHLHGQKLVTYKGDY 426
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1180-1259 |
6.06e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 47.09 E-value: 6.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1180 TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGRV 1257
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRL 487
|
..
gi 9961250 1258 KE 1259
Cdd:PRK09700 488 TQ 489
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
199-345 |
6.44e-05 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 46.40 E-value: 6.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 199 VATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSAFSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELER 278
Cdd:cd18568 126 LLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWR 205
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 279 YQKHLENAKEIGIKKAISANISMGIAFLLIYASYALAFWYGSTLVISKEYTIGN--AMTVFFSILIGAF 345
Cdd:cd18568 206 WENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQlvAFNMLFGSVINPL 274
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
1174-1250 |
7.52e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.37 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1174 RVGDKGTQLSGGQKQRIAIARALIRQPQ---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1246
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
....
gi 9961250 1247 DLIV 1250
Cdd:PRK00349 900 DWII 903
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
757-869 |
8.43e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 45.93 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 757 IFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLALIA 836
Cdd:cd18606 40 IYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD--TTPLGRILNRFSKDTDVLDNELPDSLRMFL 117
|
90 100 110
....*....|....*....|....*....|...
gi 9961250 837 QNIANLGTGIIISFIYgwqLTLLLLAVVPIIAV 869
Cdd:cd18606 118 YTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1051-1224 |
1.22e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1051 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGTVFVDFGFQLldGQEAKKlNVQWLRAqlgivSQEPILFD 1130
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKL--GYFAQH-QLEFLRA-----DESPLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1131 CSIAEniaygdnsRVVSQdeivsaakaaNIHPFIETLPHKyetrvGDKGT----QLSGGQKQRIAIARALIRQPQILLLD 1206
Cdd:PRK10636 399 ARLAP--------QELEQ----------KLRDYLGGFGFQ-----GDKVTeetrRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170
....*....|....*...
gi 9961250 1207 EATSALDTESEKVVQEAL 1224
Cdd:PRK10636 456 EPTNHLDLDMRQALTEAL 473
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
532-589 |
1.32e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.39 E-value: 1.32e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 9961250 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARegRTTIVIAH 589
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1176-1271 |
1.46e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 45.50 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1176 GDKGTQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQ 1253
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 9961250 1254 NGRVKEHGTHQQLLAQKG 1271
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
532-603 |
1.85e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.50 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 532 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTEseaEVQAALDKARE----GRTTIVIAHRLSTVRNADVIAGF 603
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR---DGQALAEAILEhlvkGAQVIVITHLPELAELADKLIHI 153
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
117-233 |
1.88e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 45.15 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 117 AYY---YSGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDDISKISEGIGDKVG 193
Cdd:cd18604 43 LYYlgiYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLS 122
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 9961250 194 MFFQAVATFFAGFIvgfirgwkltlVIMAISPILGLSAAV 233
Cdd:cd18604 123 SLLESTLSLLVILI-----------AIVVVSPAFLLPAVV 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
404-587 |
4.01e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 4.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 404 PSRANVKILKGLNLKVQSGQTVALVGSSGCGKS-TTVQLIQRLYDPD-EGTINIDGQDIRNFNVN--------YL---RE 470
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVDVSTVSdaidaglaYVtedRK 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 471 IIGVVSQEPVLFSTTIA--ENICygRGNVtMDEIKKaVKEANAYEFIM--KLPQkfdtlVGERGAQLSGGQKQRIAIARA 546
Cdd:NF040905 348 GYGLNLIDDIKRNITLAnlGKVS--RRGV-IDENEE-IKVAEEYRKKMniKTPS-----VFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 9961250 547 LVRNPKILLLDEATSALDTESEAEVQAALDK-AREGRTTIVI 587
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVI 460
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1181-1250 |
4.02e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.35 E-value: 4.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1181 QLSGGQKQRIAIARAL----IRQPQILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1250
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1181-1268 |
4.14e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 4.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1181 QLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRV 1257
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 9961250 1258 KEHGTHQQLLA 1268
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
407-612 |
4.67e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.02 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 407 ANVKILKGLNLKVQSGQTVALVGSSGCGKSTTVqliqrlYDpdegTINIDGQdiRNFN---VNYLREIIGVVSQEPVLF- 482
Cdd:cd03270 6 AREHNLKNVDVDIPRNKLVVITGVSGSGKSSLA------FD----TIYAEGQ--RRYVeslSAYARQFLGQMDKPDVDSi 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 483 ---STTIAENICYGRGNV-----TMDEI--KKAVKEANA-----YEFIMKLpqKFDTLVGERGAQ-LSGGQKQRIAIARA 546
Cdd:cd03270 74 eglSPAIAIDQKTTSRNPrstvgTVTEIydYLRLLFARVgirerLGFLVDV--GLGYLTLSRSAPtLSGGEAQRIRLATQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 547 LVRNPK--ILLLDEATSALDTESEAEVQAALDKARE-GRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQG 612
Cdd:cd03270 152 IGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAGVHGGEIVAQG 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
511-624 |
8.42e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 43.91 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 511 AYEF---IMKLPQKFDTLV---------GERGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA---EV- 571
Cdd:PRK00349 797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRkllEVl 876
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 572 QAALDKareGRTTIVIAHRLSTVRNADVIA--GFEDGV----IVEQGSHSELMKKEGVY 624
Cdd:PRK00349 877 HRLVDK---GNTVVVIEHNLDVIKTADWIIdlGPEGGDgggeIVATGTPEEVAKVEASY 932
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1045-1271 |
9.70e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1045 TRAnvpvLQGLSLEVKKGQTLALVGSSGCGKST---------VVQllerfydplAGTVFVdfgfqlLDGQEAKKLNvqwl 1115
Cdd:NF033858 14 TVA----LDDVSLDIPAGCMVGLIGPDGVGKSSllsliagarKIQ---------QGRVEV------LGGDMADARH---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1116 RAQLGivsqeP-ILF-----------DCSIAENIAY-GdnsRVVSQDE------IVSAAKAANIHPFIEtlphkyetRVG 1176
Cdd:NF033858 71 RRAVC-----PrIAYmpqglgknlypTLSVFENLDFfG---RLFGQDAaerrrrIDELLRATGLAPFAD--------RPA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1177 DKgtqLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA--- 1246
Cdd:NF033858 135 GK---LSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerf 204
|
250 260
....*....|....*....|....*
gi 9961250 1247 DLIVVFQNGRVKEHGTHQQLLAQKG 1271
Cdd:NF033858 205 DWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
532-618 |
1.17e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 42.48 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 532 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAEVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFEDGVI 608
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
|
90
....*....|
gi 9961250 609 VEQGSHSELM 618
Cdd:PRK15093 238 VETAPSKELV 247
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1175-1241 |
1.25e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.30 E-value: 1.25e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 1175 VGDKG-TQLSGGQKQRIAIARALIRQPQILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLS 1241
Cdd:PLN03140 1012 VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
754-883 |
1.63e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 42.11 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 754 FSLIFLFLGIISFFTFFLQGFTFGKAGEILTRRLRSMAFKAMLRQDMSWFDdhKNSTGALSTRLATDAAQVQGATGTRLA 833
Cdd:cd18580 41 LGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAPMSFFD--TTPSGRILNRFSKDIGLIDEELPLALL 118
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 834 LIAQNIANLGTGIIISFIYGWqltLLLLAVVPIIAVSGIV---------EMKLLAGNAK 883
Cdd:cd18580 119 DFLQSLFSVLGSLIVIAIVSP---YFLIVLPPLLVVYYLLqryylrtsrQLRRLESESR 174
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
504-600 |
1.72e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 504 KAVKEANAYEFIMKLPQ-KFDTLVGERGAQLSGGQKQ------RIAIARALVRNPKILLLDEATSALDTESEAEVQAALD 576
Cdd:cd03240 86 TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEII 165
|
90 100
....*....|....*....|....*..
gi 9961250 577 KAREG---RTTIVIAHRLSTVRNADVI 600
Cdd:cd03240 166 EERKSqknFQLIVITHDEELVDAADHI 192
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
1180-1250 |
1.83e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.83e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9961250 1180 TQLSGGQKQRIAIARALIRQPQ---ILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1250
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
713-987 |
2.23e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 41.70 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 713 VGTVCAIANGGLQPAFSVIFSEIIAIFGPGDDAVKQQkcnIFSLIFLFLGIISFFTFFLQGFTFGkaGEILTRRLRS--- 789
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSE---GYLLALALFLVSLLQSLLLHQYFFL--SFRLGMRVRSals 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 790 -MAFKAMLRQDMSWFDDHknSTGALSTRLATDAaqvqgatgTRLALIAQNIANLGTG---IIISFIYGWQLT-------- 857
Cdd:cd18579 76 sLIYRKALRLSSSARQET--STGEIVNLMSVDV--------QRIEDFFLFLHYLWSAplqIIVALYLLYRLLgwaalagl 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 858 LLLLAVVPIIAVSGIVEMKLLAGNAK-RDKKeleaaGKIATEAIENIRTVvsltqerkfesmyveKLYG---PYRNSVQK 933
Cdd:cd18579 146 GVLLLLIPLQAFLAKLISKLRKKLMKaTDER-----VKLTNEILSGIKVI---------------KLYAwekPFLKRIEE 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9961250 934 A--------HIYGITFSISQAFMYFS--YAGCFRFGAYLIVNGHMRfrdvilvfSAIVFGAVAL 987
Cdd:cd18579 206 LrkkelkalRKFGYLRALNSFLFFSTpvLVSLATFATYVLLGNPLT--------AAKVFTALSL 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
415-608 |
2.39e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 41.96 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 415 LNLKVQSGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNV-NYLREiiGVV-----SQEPVLF-STTIA 487
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaQRLAR--GLVylpedRQSSGLYlDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 488 ENIC---YGRGNVTMDEIK-KAVKEAnaYEFIMKLpqKFDTLvgERGAQ-LSGGQKQRIAIARALVRNPKILLLDEATSA 562
Cdd:PRK15439 360 WNVCaltHNRRGFWIKPAReNAVLER--YRRALNI--KFNHA--EQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 9961250 563 LDTESEAEV-QAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFEDGVI 608
Cdd:PRK15439 434 VDVSARNDIyQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
419-439 |
3.69e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 3.69e-03
10 20
....*....|....*....|.
gi 9961250 419 VQSGQTVALVGSSGCGKSTTV 439
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLV 212
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1052-1082 |
3.72e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 3.72e-03
10 20 30
....*....|....*....|....*....|..
gi 9961250 1052 LQGLSLEVKKGQTLALVGSSGCGKSTVV-QLL 1082
Cdd:PRK01889 185 LDVLAAWLSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
496-621 |
5.38e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 496 NVTMDEIKKAVKEANAYEFIMKLpqKFDTLVG------ERGAQ-LSGGQKQRIAIARAL------VrnpkILLLDEATSA 562
Cdd:TIGR00630 447 QLTLTPEEKKIAEEVLKEIRERL--GFLIDVGldylslSRAAGtLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIG 520
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9961250 563 L---DTESEAEVqaaLDKARE-GRTTIVIAHRLSTVRNADVI------AGFEDGVIVEQGSHSELMKKE 621
Cdd:TIGR00630 521 LhqrDNRRLINT---LKRLRDlGNTLIVVEHDEDTIRAADYVidigpgAGEHGGEVVASGTPEEILANP 586
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1182-1250 |
7.17e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 7.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9961250 1182 LSGGQKQRIAIARALIRQPQ--ILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1250
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1033-1213 |
7.27e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.17 E-value: 7.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1033 NITFNEvvfnYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTvvqLLERFYDPLAGTVFVDfGFQLLDGQEAKKLNV 1112
Cdd:cd03233 8 NISFTT----GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALANRTEGNVSVE-GDIHYNGIPYKEFAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9961250 1113 QWLRaqlgivsqepilfdcsiaeNIAYgdnsrvVSQDEIvsaakaaniHPFIETLPHKYETRVGDKGTQ----LSGGQKQ 1188
Cdd:cd03233 80 KYPG-------------------EIIY------VSEEDV---------HFPTLTVRETLDFALRCKGNEfvrgISGGERK 125
|
170 180
....*....|....*....|....*
gi 9961250 1189 RIAIARALIRQPQILLLDEATSALD 1213
Cdd:cd03233 126 RVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| |
