|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
739-1316 |
1.29e-165 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 506.62 E-value: 1.29e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 739 APVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPdkeEQRSQINGVCLLFVAMGCVSLFTQFLQGY 818
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG---GDLSALLLLLLLLLGLALLRALLSYLQRY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 819 AFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSW 898
Cdd:COG1132 84 LLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 899 KLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKA 978
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 979 NIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQ 1058
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1059 PPISVYNTAGEKwDNFQGKIDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVM 1138
Cdd:COG1132 322 PEIPDPPGAVPL-PPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1139 IDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQ 1218
Cdd:COG1132 399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGR--PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1219 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKG 1298
Cdd:COG1132 477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
|
570
....*....|....*...
gi 21536378 1299 THEELMAQKGAYYKLVTT 1316
Cdd:COG1132 557 THEELLARGGLYARLYRL 574
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-1314 |
5.17e-161 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 521.51 E-value: 5.17e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 21 ESDKSYNndKKSRLQDEKKGDGVRVGFFQLFRFSSSTDIWLMFVGSLCAFLHGIAQPGVLLIFGtmtdvfidydvelqel 100
Cdd:PTZ00265 23 EVEKELN--KKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFVSVFG---------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 101 qipgkacvnntIVWTNSSLNQNMTNgtrcgllniesemIKFASYYAGIAVAVL--ITGYiqiCFWVIAAarQIQKMRKFY 178
Cdd:PTZ00265 85 -----------VIMKNMNLGENVND-------------IIFSLVLIGIFQFILsfISSF---CMDVVTT--KILKTLKLE 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 179 FRRIMRMEIGWFDCNSVG-ELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAA 257
Cdd:PTZ00265 136 FLKSVFYQDGQFHDNNPGsKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 258 TIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCY 337
Cdd:PTZ00265 216 ICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASY 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 338 ALAFWYGSTLVLDE-------GEYTPGTLVQIFLSVIVGALNLGNASPCLEAFATGRAAATSIFETIDRKPIIDcMSEDG 410
Cdd:PTZ00265 296 AFGFWYGTRIIISDlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVE-NNDDG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 411 YKLDRIKgEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTV-DGHDIRSL 489
Cdd:PTZ00265 375 KKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 490 NIQWLRDQIGIVEQEPVLFSTTIAENIRYG-------------------------------------------------- 519
Cdd:PTZ00265 454 NLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsne 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 520 -----REDATMED--IVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE 592
Cdd:PTZ00265 534 liemrKNYQTIKDseVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 593 SEAMVQEVLSKIQHGH---TIIsVAHRLSTVRAADTI------------------------------------------- 626
Cdd:PTZ00265 614 SEYLVQKTINNLKGNEnriTII-IAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnkennnknnkddnnnnnnn 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 627 ----IGFEHGTAVERGTHEELLERK-GVYFTLVTLQS-QGNQALNEEDIKDATEDDMLARTFSRGSYQDSLRASIRQRSK 700
Cdd:PTZ00265 693 nnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKvSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKHENE 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 701 SqlsylvhepplaVVDHKSTYEEDRKDKDIPVQEEVepAPVRRILKfSAPEWPYML---------------VGSVGAAVN 765
Cdd:PTZ00265 773 S------------ASNKKSCKMSDENASENNAGGKL--PFLRNLFK-RKPKAPNNLrivyreifsykkdvtIIALSILVA 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 766 GTVTPLYAFLFSQILGT-FSIPDKEEQRSQINgvclLFVAMGCVSLF-TQFLQGYAFAKSGELLTKRLRKFGFRAMLGQD 843
Cdd:PTZ00265 838 GGLYPVFALLYAKYVSTlFDFANLEANSNKYS----LYILVIAIAMFiSETLKNYYNNVIGEKVEKTMKRRLFENILYQE 913
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 844 IAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVIL-CFFPFLALSgATQTRmL 922
Cdd:PTZ00265 914 ISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTgTYFIFMRVF-AIRAR-L 991
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 923 TGFASRDKQALEMVGQI----------------TNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFA 986
Cdd:PTZ00265 992 TANKDVEKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWG 1071
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 987 FAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPISVYNT 1066
Cdd:PTZ00265 1072 FSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDN 1151
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1067 AGEKWDN---FQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD------------ 1131
Cdd:PTZ00265 1152 GGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkne 1231
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1132 ------------------------------------------PDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACS 1169
Cdd:PTZ00265 1232 htndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMS 1311
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PTZ00265 1312 IYENIKFG--KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1389
|
1450 1460 1470 1480 1490 1500 1510
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1250 DTESEKTVQVAL----DKAreGRTCIVIAHRLSTIQNADIIAVMAQ-----GVVIEKGTHEELM-AQKGAYYKLV 1314
Cdd:PTZ00265 1390 DSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVYKKYV 1462
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
136-660 |
1.29e-153 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 475.42 E-value: 1.29e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 136 SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAD 215
Cdd:COG1132 58 SALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAH 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 216 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 295
Cdd:COG1132 138 GLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFG 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 296 GEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSV--IVGALN- 372
Cdd:COG1132 218 REERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLS-GSLTVGDLVAFILYLlrLFGPLRq 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 373 LGNAspcLEAFATGRAAATSIFETIDRKPIIDCmSEDGYKLDRIKGEIEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTA 452
Cdd:COG1132 297 LANV---LNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 453 LVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAA 532
Cdd:COG1132 371 LVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAA 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 533 KEANAYNFIMDLPQQFDTLVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIIS 612
Cdd:COG1132 451 KAAQAHEFIEALPDGYDTVVgergvnlsggqrqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIV 530
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 21536378 613 VAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQG 660
Cdd:COG1132 531 IAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1078-1317 |
3.55e-140 |
|
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: 426.19 E-value: 3.55e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKP--DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTG 1317
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
745-1061 |
3.69e-131 |
|
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: 405.68 E-value: 3.69e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 745 LKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSG 824
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 825 ELLTKRLRKFGFRAMLGQDIAWFDDLRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVI 904
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 905 LCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFC 984
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 985 FAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPI 1061
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
420-657 |
1.54e-127 |
|
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: 392.67 E-value: 1.54e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 579
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 657
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
146-657 |
5.99e-123 |
|
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: 398.05 E-value: 5.99e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQIC-FWVIA-AARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQMALFIQ 222
Cdd:COG2274 200 IGLLLALLFEGLLRLLrSYLLLrLGQRIDlRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTALL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 223 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 302
Cdd:COG2274 279 DLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 303 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV--QIFLSVIVGAL-NLGNAspc 379
Cdd:COG2274 359 RWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVID-GQLTLGQLIafNILSGRFLAPVaQLIGL--- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 380 LEAFATGRAAATSIFETIDRKPiiDCMSEDGYK-LDRIKGEIEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSG 458
Cdd:COG2274 435 LQRFQDAKIALERLDDILDLPP--EREEGRSKLsLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSG 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 459 AGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAY 538
Cdd:COG2274 512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLH 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 539 NFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLS 618
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
490 500 510
....*....|....*....|....*....|....*....
gi 21536378 619 TVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 657
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
733-1314 |
2.15e-121 |
|
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: 393.82 E-value: 2.15e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 733 QEEVEPAPVRRILKFSAPEWPYM---LVGSVGAAVNGTVTPLyaflFSQILGTFSIPDKeeQRSQINGVCLLFVAMGCVS 809
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLlqvLLASLLINLLALATPL----FTQVVIDRVLPNQ--DLSTLWVLAIGLLLALLFE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 810 LFTQFLQGYAFAKSGELLTKRL-RKFgFRAMLGQDIAWFDdlRNSPGALTTRLaTDASQVQGAAGSQIGMIVNSFTNVTV 888
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLsSRF-FRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLI 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 889 AMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLtgfASRDKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALET 965
Cdd:COG2274 286 FLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL---RRLSREESEASAKRQSllvETLRGIETIKALGAESRFRRRWEN 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 966 ELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHF-------SYVFRVISAVvlsatalGRAFSYT 1038
Cdd:COG2274 363 LLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLgqliafnILSGRFLAPV-------AQLIGLL 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1039 PSYAKAKISAARFFQLLDrQPPISVYNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCG 1118
Cdd:COG2274 436 QRFQDAKIALERLDDILD-LPPEREEGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSG 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1119 KSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLH 1198
Cdd:COG2274 514 KSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLAGLH 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1199 DFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLS 1278
Cdd:COG2274 592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
|
570 580 590
....*....|....*....|....*....|....*.
gi 21536378 1279 TIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 1314
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
733-1314 |
5.02e-120 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 390.24 E-value: 5.02e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 733 QEEVEPAP-VRRILKFSAPEWPYMLVGSVG---AAVNGTVTPLY-AFLFSQILGTFSIPDkeeQRSQINGVCLLFVAmgc 807
Cdd:TIGR00958 140 QGQSETADlLFRLLGLSGRDWPWLISAFVFltlSSLGEMFIPFYtGRVIDTLGGDKGPPA---LASAIFFMCLLSIA--- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 808 vSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVT 887
Cdd:TIGR00958 214 -SSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 888 VAMIIAFSFSWKLSLVILCFFPFLALSG---ATQTRMLtgfASRDKQALEMVGQITNEALSNIRTVAGIGKE----RRFI 960
Cdd:TIGR00958 291 GLLGFMLWLSPRLTMVTLINLPLVFLAEkvfGKRYQLL---SEELQEAVAKANQVAEEALSGMRTVRSFAAEegeaSRFK 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 961 EALETELEKPFKTAIQKAniyGFCFAFAQCIMFIANSASYrYGGYLI-----SNEGLhfsyvfrviSAVVLSATALGRAF 1035
Cdd:TIGR00958 368 EALEETLQLNKRKALAYA---GYLWTTSVLGMLIQVLVLY-YGGQLVltgkvSSGNL---------VSFLLYQEQLGEAV 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1036 SYT----PSYAKAKISAARFFQLLDRQPPISvyNTAGEKWDNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAF 1111
Cdd:TIGR00958 435 RVLsyvySGMMQAVGASEKVFEYLDRKPNIP--LTGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVAL 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1112 VGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKeiPMERVIAA 1191
Cdd:TIGR00958 513 VGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDT--PDEEIMAA 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1192 AKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQValDKAREGRTCI 1271
Cdd:TIGR00958 591 AKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVL 668
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 21536378 1272 VIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 1314
Cdd:TIGR00958 669 LIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
165-654 |
4.64e-114 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 374.06 E-value: 4.64e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 165 IAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLV 244
Cdd:TIGR00958 227 YTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 245 IISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVmgf 324
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALA--- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 325 FTGFVWC------LIFLcyaLAFWYGSTLVLdEGEYTPGTLVqiflSVIVGALNLGNASPCLEAFATGR----AAATSIF 394
Cdd:TIGR00958 384 YAGYLWTtsvlgmLIQV---LVLYYGGQLVL-TGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSGMmqavGASEKVF 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 395 ETIDRKPiidCMSEDG-YKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD 473
Cdd:TIGR00958 456 EYLDRKP---NIPLTGtLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 474 PCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVG 553
Cdd:TIGR00958 533 PTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVG 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 554 EGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEvlSKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 633
Cdd:TIGR00958 613 EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGS 690
|
490 500
....*....|....*....|.
gi 21536378 634 AVERGTHEELLERKGVYFTLV 654
Cdd:TIGR00958 691 VVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
62-393 |
4.56e-110 |
|
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: 348.31 E-value: 4.56e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 62 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVELQELQipgkacvnntivwtnsslnqnmtngtrcgllNIESEMIKF 141
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPD-------------------------------EFLDDVNKY 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 142 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 221
Cdd:cd18577 50 ALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLI 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 222 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 301
Cdd:cd18577 130 QSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 302 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVIVGALNLGNASPCLE 381
Cdd:cd18577 210 KRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRD-GEISPGDVLTVFFAVLIGAFSLGQIAPNLQ 288
|
330
....*....|..
gi 21536378 382 AFATGRAAATSI 393
Cdd:cd18577 289 AFAKARAAAAKI 300
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
739-1315 |
1.32e-109 |
|
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: 357.47 E-value: 1.32e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 739 APVRRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQrsqINGVCLLFVAMGCVSLFTQFLQGY 818
Cdd:TIGR02204 4 RPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGL---LNRYFAFLLVVALVLALGTAARFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 819 AFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSW 898
Cdd:TIGR02204 81 LVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 899 KLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKA 978
Cdd:TIGR02204 159 KLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 979 NIYGFCFAFAQCIMFIANSASYRYGGY-LISNE---GLHFSYVFrvisAVVLSATALGRAFSYTPSYAKAKISAARFFQL 1054
Cdd:TIGR02204 239 RTRALLTAIVIVLVFGAIVGVLWVGAHdVIAGKmsaGTLGQFVF----YAVMVAGSIGTLSEVWGELQRAAGAAERLIEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1055 LDRQPPISVYNTAGEKWDNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQ 1134
Cdd:TIGR02204 315 LQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQS 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1135 GKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYG--DNTKEipmeRVIAAAKQAQLHDFVMSLPEKYETNV 1212
Cdd:TIGR02204 395 GRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDATDE----EVEAAARAAHAHEFISALPEGYDTYL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1213 GSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQG 1292
Cdd:TIGR02204 471 GERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQG 550
|
570 580
....*....|....*....|...
gi 21536378 1293 VVIEKGTHEELMAQKGAYYKLVT 1315
Cdd:TIGR02204 551 RIVAQGTHAELIAKGGLYARLAR 573
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
130-657 |
3.12e-108 |
|
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: 353.62 E-value: 3.12e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 130 GLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIA-AARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINK 208
Cdd:TIGR02204 48 GFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWlGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 209 INDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSM 288
Cdd:TIGR02204 128 LQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAI 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 289 RTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQ-IFLSVI 367
Cdd:TIGR02204 208 RTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVI-AGKMSAGTLGQfVFYAVM 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 368 VGAlNLGNASPCLEAFATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKP 447
Cdd:TIGR02204 287 VAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRP 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 448 GEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMED 527
Cdd:TIGR02204 366 GETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEE 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 528 IVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHG 607
Cdd:TIGR02204 446 VEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKG 525
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 21536378 608 HTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 657
Cdd:TIGR02204 526 RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
742-1313 |
8.60e-105 |
|
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: 344.39 E-value: 8.60e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 742 RRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQIL-GTFSipdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAF 820
Cdd:TIGR02203 3 RRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFG----GRDRSVLWWVPLVVIGLAVLRGICSFVSTYLL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 821 AKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKL 900
Cdd:TIGR02203 79 SWVSNKVVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 901 SLVILCFFPFLALSGATQTRMLTGFaSRDKQalEMVGQITN---EALSNIRTVAGIGKE----RRFIEALETELEKPFKT 973
Cdd:TIGR02203 157 TLIVVVMLPVLSILMRRVSKRLRRI-SKEIQ--NSMGQVTTvaeETLQGYRVVKLFGGQayetRRFDAVSNRNRRLAMKM 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 974 AiQKANIYGfcfAFAQCIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQ 1053
Cdd:TIGR02203 234 T-SAGSISS---PITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1054 LLDRQPPIsvyNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD 1133
Cdd:TIGR02203 310 LLDSPPEK---DTGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1134 QGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVG 1213
Cdd:TIGR02203 386 SGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1214 SQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGV 1293
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
|
570 580
....*....|....*....|
gi 21536378 1294 VIEKGTHEELMAQKGAYYKL 1313
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1078-1313 |
5.41e-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: 326.50 E-value: 5.41e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFACSIMDNIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYG--RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
147-657 |
1.34e-102 |
|
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: 338.23 E-value: 1.34e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 147 GIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTS 226
Cdd:TIGR02203 62 GLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 227 TICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK 306
Cdd:TIGR02203 142 VIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 307 NLVFAQRWGIRKGIVMGFFTGFVWCLIFLcyALAFWYGSTLVL-DEGEYTPGTLVQIFLSVIVGALNLGNASPCLEAFAT 385
Cdd:TIGR02203 222 VSNRNRRLAMKMTSAGSISSPITQLIASL--ALAVVLFIALFQaQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQR 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 386 GRAAATSIFETIDRKPIIDcmsEDGYKLDRIKGEIEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTAL 465
Cdd:TIGR02203 300 GLAAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLV 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 466 QLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGR-EDATMEDIVQAAKEANAYNFIMDL 544
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 545 PQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAAD 624
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535
|
490 500 510
....*....|....*....|....*....|...
gi 21536378 625 TIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 657
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1078-1313 |
1.61e-100 |
|
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: 319.95 E-value: 1.61e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFACSIMDNIKYGD-NTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRD 1236
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRpDATD---EEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1237 PKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1050-1313 |
1.94e-99 |
|
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: 330.63 E-value: 1.94e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1050 RFFQLLDRQPPISVYNTAGE-KWDnfQGKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLER 1128
Cdd:COG5265 331 RMFDLLDQPPEVADAPDAPPlVVG--GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1129 FYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLPEKY 1208
Cdd:COG5265 407 FYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPDGY 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1209 ETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAV 1288
Cdd:COG5265 485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564
|
250 260
....*....|....*....|....*
gi 21536378 1289 MAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:COG5265 565 LEAGRIVERGTHAELLAQGGLYAQM 589
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1076-1308 |
3.51e-99 |
|
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: 315.70 E-value: 3.51e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1076 GKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN 1155
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1156 IGIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVR 1235
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1236 DPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKG 1308
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
290-663 |
1.80e-97 |
|
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: 325.24 E-value: 1.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 290 TVAAFGGEKREVERYEKNLvfaQRW---GIRKGIVMGFFtGFVWCLIF-LCYALAFWYGSTLVLDeGEYTPGTLVQI--F 363
Cdd:COG5265 230 TVKYFGNEAREARRYDEAL---ARYeraAVKSQTSLALL-NFGQALIIaLGLTAMMLMAAQGVVA-GTMTVGDFVLVnaY 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 364 LSVIVGALN-LGNAspcleaFATGRAAATSI---FETIDRKP-IIDcmSEDGYKLDRIKGEIEFHNVTFHY-PSRPevkI 437
Cdd:COG5265 305 LIQLYIPLNfLGFV------YREIRQALADMermFDLLDQPPeVAD--APDAPPLVVGGGEVRFENVSFGYdPERP---I 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIR 517
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIA 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 518 YGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMV 597
Cdd:COG5265 454 YGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVgerglklsggekqRVAIARTLLKNPPILIFDEATSALDSRTERAI 533
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 598 QEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQA 663
Cdd:COG5265 534 QAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEA 599
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
420-653 |
3.55e-96 |
|
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: 307.62 E-value: 3.55e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 579
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTL 653
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
154-657 |
3.98e-93 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 312.34 E-value: 3.98e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 154 ITGYIQ-ICF-WViaAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIndAIADQMALF-IQRMTSTICG 230
Cdd:PRK11176 80 ITSFISsYCIsWV--SGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQV--ASSSSGALItVVREGASIIG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 231 -FLLGFFRGWKLTLVIISVSPLIGIgaaTIGLsVSK-FTDYELKAYAKAGVV---ADEVISSMRTVAAFGGEKREVERYE 305
Cdd:PRK11176 156 lFIMMFYYSWQLSLILIVIAPIVSI---AIRV-VSKrFRNISKNMQNTMGQVttsAEQMLKGHKEVLIFGGQEVETKRFD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 306 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLcyALAF-WYGSTLVLDEGEYTPGTLVQIFLSVIvgAL-----NLGNASpc 379
Cdd:PRK11176 232 KVSNRMRQQGMKMVSASSISDPIIQLIASL--ALAFvLYAASFPSVMDTLTAGTITVVFSSMI--ALmrplkSLTNVN-- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 380 lEAFATGRAAATSIFETIDRKPIIDcmsEDGYKLDRIKGEIEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGA 459
Cdd:PRK11176 306 -AQFQRGMAACQTLFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGS 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 460 GKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDA-TMEDIVQAAKEANAY 538
Cdd:PRK11176 381 GKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAM 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 539 NFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLS 618
Cdd:PRK11176 461 DFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLS 540
|
490 500 510
....*....|....*....|....*....|....*....
gi 21536378 619 TVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 657
Cdd:PRK11176 541 TIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
62-393 |
1.40e-92 |
|
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: 301.12 E-value: 1.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 62 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIdydvelqelqipgkacvnnTIVWTNSSLNQNMTNGTRCGLLNIESEMIKF 141
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFT-------------------NGGMTNITGNSSGLNSSAGPFEKLEEEMTLY 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 142 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 221
Cdd:cd18558 62 AYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 222 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 301
Cdd:cd18558 142 QNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 302 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDEgEYTPGTLVQIFLSVIVGALNLGNASPCLE 381
Cdd:cd18558 222 TRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQ-EYSIGEVLTVFFSVLIGAFSAGQQVPSIE 300
|
330
....*....|..
gi 21536378 382 AFATGRAAATSI 393
Cdd:cd18558 301 AFANARGAAYHI 312
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
827-1313 |
4.11e-87 |
|
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: 295.14 E-value: 4.11e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 827 LTKRLRKFGFRAMLGQDIAWFDDLRNspGALTTRLATDASQVQGA-------AGSQIGMIVnsftnvtVAMIIAFSFSWK 899
Cdd:COG4987 86 LLADLRVRLYRRLEPLAPAGLARLRS--GDLLNRLVADVDALDNLylrvllpLLVALLVIL-------AAVAFLAFFSPA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 900 LSLVILCFFPFLALSGATQTRMLTGFASRDKQAL--EMVGQITnEALSNIRTVAGIGKERRF---IEALETELekpfkTA 974
Cdd:COG4987 157 LALVLALGLLLAGLLLPLLAARLGRRAGRRLAAAraALRARLT-DLLQGAAELAAYGALDRAlarLDAAEARL-----AA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 975 IQK--ANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHFSYvfrvISAVVLSA-------TALGRAFSYTPSYAKAk 1045
Cdd:COG4987 231 AQRrlARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPL----LALLVLAAlalfealAPLPAAAQHLGRVRAA- 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1046 isAARFFQLLDRQPPISvyNTAGEKWDNFQGKIDFVDCKFTYPSRPdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL 1125
Cdd:COG4987 306 --ARRLNELLDAPPAVT--EPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1126 LERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNtkEIPMERVIAAAKQAQLHDFVMSLP 1205
Cdd:COG4987 381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1206 EKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADI 1285
Cdd:COG4987 459 DGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDR 538
|
490 500
....*....|....*....|....*...
gi 21536378 1286 IAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:COG4987 539 ILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
742-1308 |
7.97e-85 |
|
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: 288.58 E-value: 7.97e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 742 RRILKFSAPEWPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIpdKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFA 821
Cdd:COG4988 6 KRLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLII--GGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 822 KSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIA-FSFSWKL 900
Cdd:COG4988 84 RAAARVKRRLRRRLLEKLLALGPAWLR--GKSTGELATLLTEGVEALDGYFARYLPQLFLAAL-VPLLILVAvFPLDWLS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 901 SLVILCFFP----FLALSG-ATQTRMltgfasrDKQALEMvgqitnEALSN--IRTVAGI------GKERRFIEALETEL 967
Cdd:COG4988 161 GLILLVTAPliplFMILVGkGAAKAS-------RRQWRAL------ARLSGhfLDRLRGLttlklfGRAKAEAERIAEAS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 968 EKpFKTA------IQKANIYGFCFAFAQCIMFIANSASYRYggyliSNEGLHFsyvFRVISAVVLSA------TALGRAF 1035
Cdd:COG4988 228 ED-FRKRtmkvlrVAFLSSAVLEFFASLSIALVAVYIGFRL-----LGGSLTL---FAALFVLLLAPefflplRDLGSFY 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1036 sytpsYAKAK-ISAA-RFFQLLDRQPPISVYNTAGEKWDNfQGKIDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVG 1113
Cdd:COG4988 299 -----HARANgIAAAeKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVG 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1114 SSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAK 1193
Cdd:COG4988 371 PSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1194 QAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVI 1273
Cdd:COG4988 449 AAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILI 528
|
570 580 590
....*....|....*....|....*....|....*
gi 21536378 1274 AHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKG 1308
Cdd:COG4988 529 THRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
420-657 |
1.03e-84 |
|
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: 276.03 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKI 579
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 657
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
418-648 |
1.18e-84 |
|
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: 275.64 E-value: 1.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYpsRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 497
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 577
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 578 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 648
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1047-1317 |
1.41e-84 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 288.40 E-value: 1.41e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1047 SAAR---FFQLLDRQPPISVYNTAGEKwDNFQGKIDFVDCKFTYPSRpdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSI 1123
Cdd:PRK13657 302 AAPKleeFFEVEDAVPDVRDPPGAIDL-GRVKGAVEFDDVSFSYDNS--RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1124 QLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYG--DNTKEipmeRVIAAAKQAQLHDFV 1201
Cdd:PRK13657 379 NLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGrpDATDE----EMRAAAERAQAHDFI 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1202 MSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQ 1281
Cdd:PRK13657 455 ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVR 534
|
250 260 270
....*....|....*....|....*....|....*.
gi 21536378 1282 NADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTG 1317
Cdd:PRK13657 535 NADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
142-648 |
1.07e-82 |
|
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: 282.42 E-value: 1.07e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 142 ASYYAGIAVAVL---ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADQMA 218
Cdd:COG4988 58 LPLLGLLLAVLLlraLLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGV----EALDGYFA 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 219 LFI-QRM-TSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAA 293
Cdd:COG4988 134 RYLpQLFlAALVPLLILVavFPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRRQWRALARlSGHFLD-RLRGLTTLKL 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 294 FGGEKREVERYEKNlvfAQRWgiRK------------GIVMGFFTgfvwcliFLCYALAfwygstlvldegeytpgtLVQ 361
Cdd:COG4988 213 FGRAKAEAERIAEA---SEDF--RKrtmkvlrvaflsSAVLEFFA-------SLSIALV------------------AVY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 362 IFLSVIVGALNLGNA------SPclEAF-------------ATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIkGEIEF 422
Cdd:COG4988 263 IGFRLLGGSLTLFAAlfvlllAP--EFFlplrdlgsfyharANGIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIEL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 423 HNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVE 502
Cdd:COG4988 340 EDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVP 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 503 QEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLL 582
Cdd:COG4988 418 QNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLL 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 583 DMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 648
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1078-1314 |
1.16e-81 |
|
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: 267.43 E-value: 1.16e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYpsRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNI 1156
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1157 GIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRD 1236
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1237 PKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 1314
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1072-1294 |
1.75e-81 |
|
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: 266.64 E-value: 1.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1072 DNFQGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 1151
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIVSQEPVLFACSIMDNIKYGDNTKeiPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIAR 1231
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSC--SFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1232 AIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVV 1294
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
800-1313 |
2.59e-80 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 276.13 E-value: 2.59e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 800 LLFVAMGCVSLFTQFLQGYAFA-KSGELLTkRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGM 878
Cdd:PRK11176 69 LVVIGLMILRGITSFISSYCISwVSGKVVM-TMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGALIT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 879 IVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS-GATQTRmltgFASRDKQALEMVGQITNEA---LSNIRTVAGIG 954
Cdd:PRK11176 146 VVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVVSKR----FRNISKNMQNTMGQVTTSAeqmLKGHKEVLIFG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 955 ----KERRFIEALETELEKPFKTAIQKAniygfcfAFAQCIMFIAnSASYRYGGYLISneglhFSYVFRVISA----VVL 1026
Cdd:PRK11176 222 gqevETKRFDKVSNRMRQQGMKMVSASS-------ISDPIIQLIA-SLALAFVLYAAS-----FPSVMDTLTAgtitVVF 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1027 SAT-ALGRAF----SYTPSYAKAKISAARFFQLLDRQPPIsvyNTAGEKWDNFQGKIDFVDCKFTYPSRpDSQVLNGLSV 1101
Cdd:PRK11176 289 SSMiALMRPLksltNVNAQFQRGMAACQTLFAILDLEQEK---DEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINF 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1102 SISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGdNTK 1181
Cdd:PRK11176 365 KIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYA-RTE 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1182 EIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVAL 1261
Cdd:PRK11176 444 QYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL 523
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1262 DKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:PRK11176 524 DELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQL 575
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
771-1313 |
3.86e-80 |
|
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: 278.93 E-value: 3.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 771 LYAFLFSQILGTFS------IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQG---YAFAKSGELLTKRLRKFGFRAMLG 841
Cdd:TIGR01846 145 LLISLALQLFALVTpllfqvVIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGlrtYLFAHLTSRIDVELGARLYRHLLG 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 842 QDIAWFDDLRNspGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFPFLAL-----SGA 916
Cdd:TIGR01846 225 LPLGYFESRRV--GDTVARVRELEQIRNFLTGSALTVVLDLLF-VVVFLAVMFFYSPTLTGVVIGSLVCYALlsvfvGPI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 917 TQTRMLTGFaSRDKQALEMVgqitNEALSNIRTVAGIGKERRFIEALETELEKPFKT---AIQKANIYGFCFAFAQCIMF 993
Cdd:TIGR01846 302 LRKRVEDKF-ERSAAATSFL----VESVTGIETIKATATEPQFQNRWDRQLAAYVAAsfrVTNLGNIAGQAIELIQKLTF 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 994 IAN---SASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTpsyakaKISAARFFQLLDRqpPISVYNTAGEK 1070
Cdd:TIGR01846 377 AILlwfGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQT------GIALERLGDILNS--PTEPRSAGLAA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1071 WDNFQGKIDFVDCKFTYpsRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV 1149
Cdd:TIGR01846 449 LPELRGAITFENIRFRY--APDSpEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADP 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1150 QFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAI 1229
Cdd:TIGR01846 527 AWLRRQMGVVLQENVLFSRSIRDNIALCN--PGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAI 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1230 ARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGA 1309
Cdd:TIGR01846 605 ARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGL 684
|
....
gi 21536378 1310 YYKL 1313
Cdd:TIGR01846 685 YARL 688
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
420-657 |
1.42e-77 |
|
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: 256.26 E-value: 1.42e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHY-PSRPEvkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 498
Cdd:cd03252 1 ITFEHVRFRYkPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPK 578
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 579 ILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQ 657
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
413-657 |
1.03e-75 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 263.36 E-value: 1.03e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 413 LDRIKGEIEFHNVTFHYP-SRPEVKilnDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI 491
Cdd:PRK13657 328 LGRVKGAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 492 QWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIAR 571
Cdd:PRK13657 405 ASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 572 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYF 651
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFA 564
|
....*.
gi 21536378 652 TLVTLQ 657
Cdd:PRK13657 565 ALLRAQ 570
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
715-1321 |
2.69e-74 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 272.29 E-value: 2.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 715 VDHKSTYEEDRKDKD--IP--VQEEVEPAPVRRILkfsapewpymLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDkee 790
Cdd:PTZ00265 28 LNKKGTFELYKKIKTqkIPffLPFKCLPASHRKLL----------GVSFVCATISGGTLPFFVSVFGVIMKNMNLGE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 791 qrsQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlrNSPGA-LTTRLATDASQVQ 869
Cdd:PTZ00265 95 ---NVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHD---NNPGSkLTSDLDFYLEQVN 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 870 GAAGSQIgMIVNSFTNVTVAMIIAFSF-SWKLSLVILCFFPFLALSGATQTRMLTgfaSRDKQAL---EMVGQITNEALS 945
Cdd:PTZ00265 169 AGIGTKF-ITIFTYASAFLGLYIWSLFkNARLTLCITCVFPLIYICGVICNKKVK---INKKTSLlynNNTMSIIEEALV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 946 NIRTVAGIGKERRFIEALETElEKPFKTAIQKAN---------IYGF-----CFAFAQCIMFIANSASYRYggyliSNEG 1011
Cdd:PTZ00265 245 GIRTVVSYCGEKTILKKFNLS-EKLYSKYILKANfmeslhigmINGFilasyAFGFWYGTRIIISDLSNQQ-----PNND 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1012 LHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQLLDRQPPISvYNTAGEKWDNFQgKIDFVDCKFTYPSRP 1091
Cdd:PTZ00265 319 FHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVE-NNDDGKKLKDIK-KIQFKNVRFHYDTRK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI-DGHDSKKVNVQFLRSNIGIVSQEPVLFACSI 1170
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSI 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYG----------------------------------------------DNTKEIPMER---------VIAAAKQA 1195
Cdd:PTZ00265 477 KNNIKYSlyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttDSNELIEMRKnyqtikdseVVDVSKKV 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1196 QLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALD--KAREGRTCIVI 1273
Cdd:PTZ00265 557 LIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIII 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1274 AHRLSTIQNADIIAVM-----------------------------------------------AQGVVIEKGTHEELMAQ 1306
Cdd:PTZ00265 637 AHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSYIIEQGTHDALMKN 716
|
730
....*....|....*
gi 21536378 1307 KGAYYKLVTTGSPIS 1321
Cdd:PTZ00265 717 KNGIYYTMINNQKVS 731
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
166-656 |
4.77e-74 |
|
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: 257.77 E-value: 4.77e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 166 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADqmaLFIqR---------MTSTICGFLLGFF 236
Cdd:COG4987 82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV----DALDN---LYL-RvllpllvalLVILAAVAFLAFF 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 237 rGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAyAKAGVVAD--EVISSMRTVAAFGGEKREVERY---EKNLVFA 311
Cdd:COG4987 154 -SPALALVLALGLLLAGLLLPLLAARLGRRAGRRLAA-ARAALRARltDLLQGAAELAAYGALDRALARLdaaEARLAAA 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 312 QRwgiRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVIVGALNLGNASPCLEAFATGRAAAT 391
Cdd:COG4987 232 QR---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAA-GALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAAR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 392 SIFETIDRKPIIDcMSEDGYKLDRiKGEIEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRF 471
Cdd:COG4987 308 RLNELLDAPPAVT-EPAEPAPAPG-GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRF 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 472 YDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTL 551
Cdd:COG4987 385 LDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTW 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 552 VGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEH 631
Cdd:COG4987 465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLED 544
|
490 500
....*....|....*....|....*
gi 21536378 632 GTAVERGTHEELLERKGVYFTLVTL 656
Cdd:COG4987 545 GRIVEQGTHEELLAQNGRYRQLYQR 569
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
58-403 |
1.77e-73 |
|
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: 247.75 E-value: 1.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 58 DIWLMFVGSLCAFLHGIAQPGVLLIFGTMTDVFidydvelqelqipgkacvnntivwtnsslnqnmtngTRCGLLNIESE 137
Cdd:cd18578 7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVF------------------------------------SLPDDDELRSE 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 138 MIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFD--CNSVGELNTRFSDDINKINDAIAD 215
Cdd:cd18578 51 ANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 216 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 295
Cdd:cd18578 131 RLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 296 GEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVIVGALNLGN 375
Cdd:cd18578 211 LEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVAN-GEYTFEQFFIVFMALIFGAQSAGQ 289
|
330 340
....*....|....*....|....*...
gi 21536378 376 ASPCLEAFATGRAAATSIFETIDRKPII 403
Cdd:cd18578 290 AFSFAPDIAKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
755-1050 |
3.59e-71 |
|
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: 240.45 E-value: 3.59e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 755 MLVGSVGAAVNGTVTPLYAFLFSQILGTFS-----IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTK 829
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 830 RLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 909
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 910 FLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQ 989
Cdd:cd18577 159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 990 CIMFIANSASYRYGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAAR 1050
Cdd:cd18577 239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAK 299
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
414-632 |
1.32e-70 |
|
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: 235.83 E-value: 1.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 414 DRIKGEIEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW 493
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 494 LRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARAL 573
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHG 632
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1078-1292 |
1.65e-70 |
|
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: 233.04 E-value: 1.65e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQG 1292
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
1075-1314 |
5.00e-70 |
|
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: 249.86 E-value: 5.00e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1075 QGKIDFVDCKFTYpSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 1154
Cdd:TIGR03796 475 SGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAN 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIV 1234
Cdd:TIGR03796 554 SVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALV 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1235 RDPKILLLDEATSALDTESEKTVQVALdkAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLV 1314
Cdd:TIGR03796 632 RNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
420-632 |
1.87e-69 |
|
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: 230.35 E-value: 1.87e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENIRYGREdatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKI 579
Cdd:cd03228 80 YVPQDPFLFSGTIRENILSGGQ------------------------RQ------------------RIAIARALLRDPPI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHG 632
Cdd:cd03228 118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
741-1313 |
2.80e-65 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 233.07 E-value: 2.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 741 VRRILKFSAPeWP-------YMLVGSVGAAVNGTVtpLYAFLFSQILGTFSIPDKeeqrsQINGVCLLFVAMGCVSLFTQ 813
Cdd:PRK10790 11 LKRLLAYGSP-WRkplglavLMLWVAAAAEVSGPL--LISYFIDNMVAKGNLPLG-----LVAGLAAAYVGLQLLAAGLH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 814 FLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlrNSP-GALTTRLATDASQVQGAAGSQIGMIVNSFTNVtVAMII 892
Cdd:PRK10790 83 YAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD---TQPvGQLISRVTNDTEVIRDLYVTVVATVLRSAALI-GAMLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 893 A-FSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPF 971
Cdd:PRK10790 159 AmFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFGERMGEASRSHY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 972 KTAIQKANIYGFC--------FAFAQCIMFIAnsasyrYGgylISNEGlhfsyvfrVISAVVLSA--TALGRA------- 1034
Cdd:PRK10790 239 MARMQTLRLDGFLlrpllslfSALILCGLLML------FG---FSASG--------TIEVGVLYAfiSYLGRLnepliel 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1035 FSYTPSYAKAKISAARFFQLLDRqpPISVYNTAGEKWDnfQGKIDFVDCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGS 1114
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFELMDG--PRQQYGNDDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGH 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1115 SGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGdntKEIPMERVIAAAKQ 1194
Cdd:PRK10790 376 TGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALET 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1195 AQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIA 1274
Cdd:PRK10790 453 VQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA 532
|
570 580 590
....*....|....*....|....*....|....*....
gi 21536378 1275 HRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:PRK10790 533 HRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
755-1048 |
1.13e-64 |
|
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: 222.15 E-value: 1.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 755 MLVGSVGAAVNGTVTPLYAFLFSQILGTF-------------SIPDK----EEQRSQINGVCLLFVAMGCVSLFTQFLQG 817
Cdd:cd18558 1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssGLNSSagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 818 YAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFS 897
Cdd:cd18558 81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 898 WKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQK 977
Cdd:cd18558 159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 978 ANIYGFCFAFAQCIMFIANSASYRYGGYLI-SNEGLHFSYVFRVISAVVLSATALGRAFSYTPsYAKAKISA 1048
Cdd:cd18558 239 AITFNISMGAAFLLIYASYALAFWYGTYLVtQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAA 309
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
882-1317 |
1.97e-63 |
|
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: 227.46 E-value: 1.97e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 882 SFTNVTVAMIIAFSFSWKLSLVILCF-FPFLALSGATQTRMLTGFASRDKQALEMVGQITnEALSNIRTVAGIGKERRFI 960
Cdd:TIGR01192 140 TFVALFLLIPTAFAMDWRLSIVLMVLgILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVS-DSISNVSVVHSYNRIEAET 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 961 EALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHfsyVFRVISAVVLSATALGR-----AF 1035
Cdd:TIGR01192 219 SALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELS---VGEVIAFIGFANLLIGRldqmsGF 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1036 SYTPSYAKAKISaaRFFQLLDRQPPISVYNTAGEkWDNFQGKIDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSS 1115
Cdd:TIGR01192 296 ITQIFEARAKLE--DFFDLEDSVFQREEPADAPE-LPNVKGAVEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPT 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1116 GCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTKEipMERVIAAAKQA 1195
Cdd:TIGR01192 371 GAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGAT--DEEVYEAAKAA 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1196 QLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAH 1275
Cdd:TIGR01192 449 AAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAH 528
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 21536378 1276 RLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTG 1317
Cdd:TIGR01192 529 RLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRRS 570
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
178-654 |
1.01e-62 |
|
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: 228.29 E-value: 1.01e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 178 YFRRIMRMEIGWFDCNSVGELNTRFSddinkINDAIADQMAlfiQRMTSTICGFLLGFFRG-------WKLTLVIISvsp 250
Cdd:TIGR03796 233 FLWHILRLPVRFFAQRHAGDIASRVQ-----LNDQVAEFLS---GQLATTALDAVMLVFYAllmllydPVLTLIGIA--- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 251 LIGIGAATIGLSVSKFTDYELKA---YAKAGVVADEVISSMRTVAAFGGEKREVER---YEKNLVFAQRwgiRKGIVMGF 324
Cdd:TIGR03796 302 FAAINVLALQLVSRRRVDANRRLqqdAGKLTGVAISGLQSIETLKASGLESDFFSRwagYQAKLLNAQQ---ELGVLTQI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 325 FTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV------QIFLSVIVGALNLGNASPCLEA----------FATGRA 388
Cdd:TIGR03796 379 LGVLPTLLTSLNSALILVVGGLRVME-GQLTIGMLVafqslmSSFLEPVNNLVGFGGTLQELEGdlnrlddvlrNPVDPL 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 389 AatsifetIDRKPIIDCMSEDGykldRIKGEIEFHNVTFHYpSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI 468
Cdd:TIGR03796 458 L-------EEPEGSAATSEPPR----RLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLV 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 469 QRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGreDATM--EDIVQAAKEANAYNFIMDLPQ 546
Cdd:TIGR03796 526 AGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLW--DPTIpdADLVRACKDAAIHDVITSRPG 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 547 QFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSkiQHGHTIISVAHRLSTVRAADTI 626
Cdd:TIGR03796 604 GYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLR--RRGCTCIIVAHRLSTIRDCDEI 681
|
490 500
....*....|....*....|....*...
gi 21536378 627 IGFEHGTAVERGTHEELLERKGVYFTLV 654
Cdd:TIGR03796 682 IVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
181-657 |
2.47e-62 |
|
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: 226.76 E-value: 2.47e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 181 RIMRMEIGWFDCNSVGELNTRfSDDINKINDAIADqmALFIQRMTSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAAT 258
Cdd:TIGR03797 218 RLLRLPVSFFRQYSTGDLASR-AMGISQIRRILSG--STLTTLLSGIFALLNLGlmFYYSWKLALVAVALALVAIAVTLV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 259 IGLsvsKFTDYELKAYAKAGVVADEV------ISSMRTVAAfggEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCL 332
Cdd:TIGR03797 295 LGL---LQVRKERRLLELSGKISGLTvqlingISKLRVAGA---ENRAFARWAKLFSRQRKLELSAQRIENLLTVFNAVL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 333 IFLCYALAFWYGSTLvLDEGEYTPGTLVQ---IFLSVIVGALNLGNAspcleafATGRAAATSIFETIdrKPIIDCMSE- 408
Cdd:TIGR03797 369 PVLTSAALFAAAISL-LGGAGLSLGSFLAfntAFGSFSGAVTQLSNT-------LISILAVIPLWERA--KPILEALPEv 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 409 DGYKLD--RIKGEIEFHNVTFHY-PSRPevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHD 485
Cdd:TIGR03797 439 DEAKTDpgKLSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQD 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 486 IRSLNIQWLRDQIGIVEQEPVLFSTTIAENIrYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQ 565
Cdd:TIGR03797 517 LAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQ 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 566 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLE 645
Cdd:TIGR03797 596 RLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK--VTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMA 673
|
490
....*....|..
gi 21536378 646 RKGVYFTLVTLQ 657
Cdd:TIGR03797 674 REGLFAQLARRQ 685
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
126-656 |
3.92e-62 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 233.77 E-value: 3.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 126 GTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFD--CNSVGELNTRFS 203
Cdd:PTZ00265 853 STLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHIN 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 204 DDINKINDAIADQMALFIQRMTSTICGFLLGFFRgWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVV--- 280
Cdd:PTZ00265 933 RDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYF-CPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVfay 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 281 -------------ADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTL 347
Cdd:PTZ00265 1012 nsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFL 1091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 348 VldegeyTPGT-LVQIFLSVIVGALNLGNASPCLEAFATGRAAATSIFET----IDRKPIIDCMSEDGYKL---DRIKGE 419
Cdd:PTZ00265 1092 I------RRGTiLVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKyyplIIRKSNIDVRDNGGIRIknkNDIKGK 1165
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-------------------------- 473
Cdd:PTZ00265 1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgd 1245
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 474 ----------------------------PCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATM 525
Cdd:PTZ00265 1246 eeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 526 EDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ 605
Cdd:PTZ00265 1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1405
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 606 H--GHTIISVAHRLSTVRAADTIIGFEH----GTAVE-RGTHEELLE-RKGVYFTLVTL 656
Cdd:PTZ00265 1406 DkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
395-1313 |
9.04e-62 |
|
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: 232.91 E-value: 9.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 395 ETIDRKPIIDcmsEDGYKldrikgeIEFHNVTFHYpSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP 474
Cdd:TIGR00957 622 DSIERRTIKP---GEGNS-------ITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK 690
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 475 CEGMVTVDGhdirslniqwlrdQIGIVEQEPVLFSTTIAENIRYGRedATMEDIVQAAKEANAynFIMDL---PQQFDTL 551
Cdd:TIGR00957 691 VEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACA--LLPDLeilPSGDRTE 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 552 VGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE-SEAMVQEVLSK--IQHGHTIISVAHRLSTVRAADTIIG 628
Cdd:TIGR00957 754 IGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPegVLKNKTRILVTHGISYLPQVDVIIV 833
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 629 FEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQALNEEDI---------KDA--TEDDMLARTFSRGSYQDSLRASirq 697
Cdd:TIGR00957 834 MSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSwtalvsgegKEAklIENGMLVTDVVGKQLQRQLSAS--- 910
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 698 rSKSQLSYLVHEPPLAVVDHKSTYEEDRKdkdipvQEEVEPAPVRRIlKFSApEWPYMlvgsvgAAVNGTVTPLYAFLF- 776
Cdd:TIGR00957 911 -SSDSGDQSRHHGSSAELQKAEAKEETWK------LMEADKAQTGQV-ELSV-YWDYM------KAIGLFITFLSIFLFv 975
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 777 --------SQILGTFSIPDKEEQRSQINGVCLLFV--AMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAW 846
Cdd:TIGR00957 976 cnhvsalaSNYWLSLWTDDPMVNGTQNNTSLRLSVygALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSF 1055
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 847 FDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVIlcffPFLALSGATQTRMLTGfA 926
Cdd:TIGR00957 1056 FE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVII----PPLGLLYFFVQRFYVA-S 1128
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 927 SRDKQALEMVGQIT-----NEALSNIRTVAGIGKERRFIEALETELEkpfktAIQKAniygfcfafaqCIMFIANSASYR 1001
Cdd:TIGR00957 1129 SRQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQERFIHQSDLKVD-----ENQKA-----------YYPSIVANRWLA 1192
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1002 YGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYT-------------PSYAKAKISAA---RFFQLLDRQPPISVYN 1065
Cdd:TIGR00957 1193 VRLECVGNCIVLFAALFAVISRHSLSAGLVGLSVSYSlqvtfylnwlvrmSSEMETNIVAVerlKEYSETEKEAPWQIQE 1272
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1066 TAG-EKWDNfQGKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD 1143
Cdd:TIGR00957 1273 TAPpSGWPP-RGRVEFRNYCLRY--REDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1144 SKKVNVQFLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGE 1223
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQ 1426
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1224 KQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:TIGR00957 1427 RQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
|
970
....*....|
gi 21536378 1304 MAQKGAYYKL 1313
Cdd:TIGR00957 1507 LQQRGIFYSM 1516
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1076-1299 |
1.07e-60 |
|
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: 207.35 E-value: 1.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1076 GKIDFVDCKFTYpsRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 1154
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQEPVLFACSIMDNI----KYGDntkeipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIA 1230
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNLdpfgEYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1231 RAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGT 1299
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1076-1298 |
1.55e-59 |
|
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: 203.98 E-value: 1.55e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1076 GKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN 1155
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1156 IGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVR 1235
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1236 DPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKG 1298
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
62-371 |
1.68e-59 |
|
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: 205.95 E-value: 1.68e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 62 MFVGSLCAFLHGIAQPGVLLIFGTMTDVFIDYDVelqelqipgkacvnntivwtnsslnqnmtngtrcgllNIESEMIKF 141
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGD-------------------------------------PETQALNVY 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 142 ASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFI 221
Cdd:pfam00664 44 SLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLF 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 222 QRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREV 301
Cdd:pfam00664 124 QSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYEL 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 302 ERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQI--FLSVIVGAL 371
Cdd:pfam00664 204 EKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVIS-GELSVGDLVAFlsLFAQLFGPL 274
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
146-627 |
1.83e-58 |
|
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: 211.38 E-value: 1.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADQMALFI-QRM 224
Cdd:TIGR02857 51 ALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGV----EALDGYFARYLpQLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 225 TSTICGFLLG---FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAAFGGEKRE 300
Cdd:TIGR02857 127 LAVIVPLAILaavFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRlSGHFLD-RLRGLPTLKLFGRAKAQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 301 VER-YEKNLVFAQRwgirkgiVMGfftgfVWCLIFLcyalafwygSTLVLdegEY-----TPGTLVQIFLSVIVGALNLG 374
Cdd:TIGR02857 206 AAAiRRSSEEYRER-------TMR-----VLRIAFL---------SSAVL---ELfatlsVALVAVYIGFRLLAGDLDLA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 375 NASPCL----EAF-------------ATGRAAATSIFETIDRKPIIDCMSEDGYKLDRIkgEIEFHNVTFHYPSRPEVki 437
Cdd:TIGR02857 262 TGLFVLllapEFYlplrqlgaqyharADGVAAAEALFAVLDAAPRPLAGKAPVTAAPAS--SLEFSGVSVAYPGRRPA-- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIR 517
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 518 YGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMV 597
Cdd:TIGR02857 418 LARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEV 497
|
490 500 510
....*....|....*....|....*....|
gi 21536378 598 QEVLSKIQHGHTIISVAHRLSTVRAADTII 627
Cdd:TIGR02857 498 LEALRALAQGRTVLLVTHRLALAALADRIV 527
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1047-1313 |
3.69e-58 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 211.61 E-value: 3.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1047 SAARFFQLLDRQPPISVYNTAGEKWDnfQGKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL 1126
Cdd:PRK11160 310 SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1127 ERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDNTkeIPMERVIAAAKQAQLHDFVMSlPE 1206
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPN--ASDEALIEVLQQVGLEKLLED-DK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1207 KYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADII 1286
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260
....*....|....*....|....*..
gi 21536378 1287 AVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
148-676 |
1.49e-56 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 206.87 E-value: 1.49e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 148 IAVAVLITGYIQIcFWVIAAARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIN-----------DAIAD 215
Cdd:PRK10789 45 IAVVVYLLRYVWR-VLLFGASYQLAvELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVfaagegvltlvDSLVM 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 216 QMALFIQrMTSTIcgfllgffrGWKLTLVIISVSPLIGIGAATIGLSV-SKFTDYElKAYAKAGVVADEVISSMRTVAAF 294
Cdd:PRK10789 124 GCAVLIV-MSTQI---------SWQLTLLALLPMPVMAIMIKRYGDQLhERFKLAQ-AAFSSLNDRTQESLTSIRMIKAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 295 GGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQ--IFLSVIVGaln 372
Cdd:PRK10789 193 GLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAIGMANLLAIGGGSWMVV-NGSLTLGQLTSfvMYLGLMIW--- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 373 lgnasPCLeAFA-------TGRAAATSIFETIDRKPIIdcmsEDGYK-LDRIKGEIEFHNVTFHYPSRpEVKILNDLNMV 444
Cdd:PRK10789 269 -----PML-ALAwmfniveRGSAAYSRIRAMLAEAPVV----KDGSEpVPEGRGELDVNIRQFTYPQT-DHPALENVNFT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 445 IKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDAT 524
Cdd:PRK10789 338 LKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDAT 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 525 MEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI 604
Cdd:PRK10789 418 QQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 605 QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQsQGNQALNEEDIKDATEDD 676
Cdd:PRK10789 498 GEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ-QLEAALDDAPEIREEAVD 568
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
409-654 |
2.83e-56 |
|
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: 206.28 E-value: 2.83e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 409 DGYKLDRIKGEIEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS 488
Cdd:TIGR01192 324 DAPELPNVKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINT 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 489 LNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVA 568
Cdd:TIGR01192 402 VTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 569 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKG 648
Cdd:TIGR01192 482 IARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDG 561
|
....*.
gi 21536378 649 VYFTLV 654
Cdd:TIGR01192 562 RFYKLL 567
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
753-1289 |
1.06e-54 |
|
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: 200.21 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 753 PYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDkeEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLR 832
Cdd:TIGR02857 3 RALALLALLGVLGALLIIAQAWLLARVVDGLISAG--EPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 833 KFGFRAMLGQDIAWFddLRNSPGALTTRLATDASQVQG-AAGSQIGMIVNSFtnVTVAMIIA-FSFSWKLSLVILCFFP- 909
Cdd:TIGR02857 81 ERLLEAVAALGPRWL--QGRPSGELATLALEGVEALDGyFARYLPQLVLAVI--VPLAILAAvFPQDWISGLILLLTAPl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 910 ---FLALSG-ATQTRmltgfASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELE-------KPFKTAIQKA 978
Cdd:TIGR02857 157 ipiFMILIGwAAQAA-----ARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEeyrertmRVLRIAFLSS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 979 NIYGFcFAfAQCIMFIANSASYRY-GGYLISNEGLhfsYVFRVISAVVLSATALGRAFSYTpsyAKAKISAARFFQLLDR 1057
Cdd:TIGR02857 232 AVLEL-FA-TLSVALVAVYIGFRLlAGDLDLATGL---FVLLLAPEFYLPLRQLGAQYHAR---ADGVAAAEALFAVLDA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1058 QPPIsVYNTAGEKWDNFQGkIDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV 1137
Cdd:TIGR02857 304 APRP-LAGKAPVTAAPASS-LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1138 MIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGS 1217
Cdd:TIGR02857 380 AVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGA 457
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1218 QLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVM 1289
Cdd:TIGR02857 458 GLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1095-1306 |
1.91e-54 |
|
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: 200.36 E-value: 1.91e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 1174
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENI 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1175 -KYGDntkeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1253
Cdd:COG4618 427 aRFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEG 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1254 EKTVQVALDKARE-GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:COG4618 503 EAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
418-638 |
9.36e-53 |
|
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: 184.33 E-value: 9.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 497
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 577
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 578 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 638
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
418-639 |
1.99e-52 |
|
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: 183.46 E-value: 1.99e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYpsRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 496
Cdd:cd03244 1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFSTTIAENIrygreD----ATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARA 572
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL-----DpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 573 LIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 639
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
850-1310 |
2.75e-52 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 194.16 E-value: 2.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 850 LRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFT-NVTVAMIIAFSFSWKLSLVILCFFPFLALsgaTQTRMLTGFASR 928
Cdd:PRK10789 88 LRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVmGCAVLIVMSTQISWQLTLLALLPMPVMAI---MIKRYGDQLHER 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 929 DKQALEMVGQITN---EALSNIRTVAGIGKE----RRFIEALETELEKPFKTAIQKA----NIYgfcFAFAqcimfIANS 997
Cdd:PRK10789 165 FKLAQAAFSSLNDrtqESLTSIRMIKAFGLEdrqsALFAADAEDTGKKNMRVARIDArfdpTIY---IAIG-----MANL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 998 ASYRYGGYLISNEGLHF----SYVFrVISAVVLSATALGRAFSYTpsyakAKISAA--RFFQLLDRQPpisVYNTAGEKW 1071
Cdd:PRK10789 237 LAIGGGSWMVVNGSLTLgqltSFVM-YLGLMIWPMLALAWMFNIV-----ERGSAAysRIRAMLAEAP---VVKDGSEPV 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1072 DNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 1151
Cdd:PRK10789 308 PEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIVSQEPVLFACSIMDNIKYG--DNTKEipmeRVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAI 1229
Cdd:PRK10789 387 WRSRLAVVSQTPFLFSDTVANNIALGrpDATQQ----EIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1230 ARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGA 1309
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGW 542
|
.
gi 21536378 1310 Y 1310
Cdd:PRK10789 543 Y 543
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
755-1009 |
8.92e-51 |
|
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: 180.92 E-value: 8.92e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 755 MLVGSVGAAVNGTVTPLYAFLFSQILGTFsIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 834
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVL-LPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 835 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 914
Cdd:pfam00664 80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 915 GATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFI 994
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
|
250
....*....|....*
gi 21536378 995 ANSASYRYGGYLISN 1009
Cdd:pfam00664 238 SYALALWFGAYLVIS 252
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1091-1313 |
1.50e-50 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 189.29 E-value: 1.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVLNG-LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACS 1169
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYGDntKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PRK11174 439 LRDNVLLGN--PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1250 DTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
154-655 |
3.78e-49 |
|
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: 187.64 E-value: 3.78e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 154 ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQM-ALFIQRMTSTICGFL 232
Cdd:TIGR01193 211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTIlSLFLDMWILVIVGLF 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 233 LGFfRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKrevERY-------- 304
Cdd:TIGR01193 290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEA---ERYskidsefg 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 305 ---EKNLVFAQRWGIRKGIVMGFftgfvwCLIFLCYALafWYGSTLVLdEGEYTPGTLV--QIFLSVIVGAL-NLGNASP 378
Cdd:TIGR01193 366 dylNKSFKYQKADQGQQAIKAVT------KLILNVVIL--WTGAYLVM-RGKLTLGQLItfNALLSYFLTPLeNIINLQP 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 379 CLEAfatGRAAATSIFETIdrkpIIDCMSEDGYKLD---RIKGEIEFHNVTFHYPSRPEvkILNDLNMVIKPGEMTALVG 455
Cdd:TIGR01193 437 KLQA---ARVANNRLNEVY----LVDSEFINKKKRTelnNLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 456 PSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYG-REDATMEDIVQAAKE 534
Cdd:TIGR01193 508 MSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEI 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 535 ANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHgHTIISVA 614
Cdd:TIGR01193 588 AEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVA 666
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 21536378 615 HRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVT 655
Cdd:TIGR01193 667 HRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1020-1306 |
5.81e-49 |
|
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: 183.70 E-value: 5.81e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1020 VISAVVLSATALG---RAFSYTPSYAKAKISAARFFQLLDRQPPisvyNTAGEKWDNFQGKIDfVDCKFTYPSRPDSQVL 1096
Cdd:TIGR01842 260 MIAGSILVGRALApidGAIGGWKQFSGARQAYKRLNELLANYPS----RDPAMPLPEPEGHLS-VENVTIVPPGGKKPTL 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1097 NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI-K 1175
Cdd:TIGR01842 335 RGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaR 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1176 YGDNTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 1255
Cdd:TIGR01842 415 FGENADP---EKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQ 491
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1256 TVQVALDKAR-EGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:TIGR01842 492 ALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
855-1315 |
4.66e-47 |
|
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: 181.09 E-value: 4.66e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 855 GALTTRLaTDASQVQGAAGSqigMIVNSFTNVTVAMIIAFSFSW---KLSLVILCFFPFLALSGATQTRMLTGFASRDKQ 931
Cdd:TIGR01193 253 GEIVSRF-TDASSIIDALAS---TILSLFLDMWILVIVGLFLVRqnmLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQ 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 932 ALEMVGQITNEALSNIRTVAGIGKERRFIEALETE----LEKPFKTAIQKANIYgfcfAFAQCIMFIANSASYRYGGYLI 1007
Cdd:TIGR01193 329 ANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEfgdyLNKSFKYQKADQGQQ----AIKAVTKLILNVVILWTGAYLV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1008 SNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQ--LLDRQPPISVYNTAGEkwdNFQGKIDFVDCKF 1085
Cdd:TIGR01193 405 MRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSEFINKKKRTELN---NLNGDIVINDVSY 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL 1165
Cdd:TIGR01193 482 SYGY--GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYI 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 FACSIMDNIKYGDNTKeIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:TIGR01193 560 FSGSILENLLLGAKEN-VSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1246 TSALDTESEKTVQVALDKAREgRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVT 1315
Cdd:TIGR01193 639 TSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1019-1277 |
2.07e-45 |
|
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: 172.93 E-value: 2.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1019 RVISAVVLSATALGRAFSYTP----SYAKAKISAARFFQLLDRQPPISVYNTAGEKwDNFQGKIDFV--DCKFTYPsrPD 1092
Cdd:TIGR02868 271 VTLAVLVLLPLAAFEAFAALPaaaqQLTRVRAAAERIVEVLDAAGPVAEGSAPAAG-AVGLGKPTLElrDLSAGYP--GA 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1093 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMD 1172
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKYGdnTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:TIGR02868 428 NLRLA--RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
250 260
....*....|....*....|....*
gi 21536378 1253 SEKTVQVALDKAREGRTCIVIAHRL 1277
Cdd:TIGR02868 506 TADELLEDLLAALSGRTVVLITHHL 530
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
420-1319 |
2.60e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 179.79 E-value: 2.60e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdghdirslniqwLRDQIG 499
Cdd:PLN03232 615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVA 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENIRYGrEDATMEDIVQAAkEANAYNFIMDL-PQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPK 578
Cdd:PLN03232 683 YVPQVSWIFNATVRENILFG-SDFESERYWRAI-DVTALQHDLDLlPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 579 ILLLDMATSALDNESEAMVQEvlSKIQH---GHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVT 655
Cdd:PLN03232 761 IYIFDDPLSALDAHVAHQVFD--SCMKDelkGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLME 838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 656 lqsqgNQALNEEDIKDATEDDMLARTFSRGSYQDSLR--ASIRQrSKSQLSYLVHepplavvdhkstyeedrkdkdipvQ 733
Cdd:PLN03232 839 -----NAGKMDATQEVNTNDENILKLGPTVTIDVSERnlGSTKQ-GKRGRSVLVK------------------------Q 888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 734 EEVEPAPVrrilkfsapEWPYMLvgSVGAAVNG--TVTPLYA-FLFSQILGTFSIP------DKEEQRSQINGVCLLFVA 804
Cdd:PLN03232 889 EERETGII---------SWNVLM--RYNKAVGGlwVVMILLVcYLTTEVLRVSSSTwlsiwtDQSTPKSYSPGFYIVVYA 957
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 805 M-GCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSF 883
Cdd:PLN03232 958 LlGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHT--NPTGRVINRFSKDIGDIDRNVANLMNMFMNQL 1035
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 884 -----TNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQ--------TR---------MLTGFAS-RDKQALEMVGQIT 940
Cdd:PLN03232 1036 wqllsTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTSRevrrldsvTRspiyaqfgeALNGLSSiRAYKAYDRMAKIN 1115
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 941 NEAL-SNIR-TVAGIGKERRFIEALETelekpfktaiqkanIYGFCFAFAQCIMFIANSASYRYGGYlISNEGLHFSY-- 1016
Cdd:PLN03232 1116 GKSMdNNIRfTLANTSSNRWLTIRLET--------------LGGVMIWLTATFAVLRNGNAENQAGF-ASTMGLLLSYtl 1180
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1017 --------VFRVISAVVLSATALGRAFSYT--PSYAKAKISAARffqlldrqPPISvyntagekWDNfQGKIDFVDCKFT 1086
Cdd:PLN03232 1181 nittllsgVLRQASKAENSLNSVERVGNYIdlPSEATAIIENNR--------PVSG--------WPS-RGSIKFEDVHLR 1243
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1087 YpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL 1165
Cdd:PLN03232 1244 Y--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVL 1321
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 FACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:PLN03232 1322 FSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1246 TSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKG-AYYKLVTTGSP 1319
Cdd:PLN03232 1399 TASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHSTGP 1473
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
146-662 |
3.76e-45 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 173.37 E-value: 3.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITG-------YIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 218
Cdd:PRK10790 65 AGLAAAYVGLQllaaglhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 219 LFIqRMTSTICGFLLGFFR-GWKLTLVIISVSPLIgIGAATIGLSVSKFTDYELKAYakagvVAD------EVISSM--- 288
Cdd:PRK10790 145 TVL-RSAALIGAMLVAMFSlDWRMALVAIMIFPAV-LVVMVIYQRYSTPIVRRVRAY-----LADindgfnEVINGMsvi 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 289 ---RTVAAFGGEKREVER--YEKNLVFAQRWGIRKGIVMGFFTGFVWC-LIFLcyalaFWYGSTLVLDEGeytpgtLVQI 362
Cdd:PRK10790 218 qqfRQQARFGERMGEASRshYMARMQTLRLDGFLLRPLLSLFSALILCgLLML-----FGFSASGTIEVG------VLYA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 363 FLSVIvGALNlgnaSPCLEaFATGRA-------AATSIFETIDRkpiidcmSEDGYKLDRI---KGEIEFHNVTFHYpsR 432
Cdd:PRK10790 287 FISYL-GRLN----EPLIE-LTTQQSmlqqavvAGERVFELMDG-------PRQQYGNDDRplqSGRIDIDNVSFAY--R 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 433 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTI 512
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTF 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 513 AENIRYGReDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE 592
Cdd:PRK10790 432 LANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSG 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 593 SEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQGNQ 662
Cdd:PRK10790 511 TEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEE 580
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
294-653 |
1.38e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 171.16 E-value: 1.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 294 FGGEKR---EVERYEKNLVFAQRwgirkgiVMGFFTGFVWCLIFLCYALA----FWYGSTLVldEGEYTPGTLVQIF--- 363
Cdd:PRK11160 216 FGAEDRyrqQLEQTEQQWLAAQR-------RQANLTGLSQALMILANGLTvvlmLWLAAGGV--GGNAQPGALIALFvfa 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 364 -------LSVIVGA-LNLGNaspCLeafatgrAAATSIFETIDRKPIIDCMSEDGYKLDRikGEIEFHNVTFHYPSRPEv 435
Cdd:PRK11160 287 alaafeaLMPVAGAfQHLGQ---VI-------ASARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ- 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAEN 515
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDN 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 516 IRYGREDATMEDIVQAAKEANAYNFIMDlPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEA 595
Cdd:PRK11160 434 LLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETER 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 596 MVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTL 653
Cdd:PRK11160 513 QILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
344-646 |
2.61e-44 |
|
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: 170.31 E-value: 2.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 344 GSTLVLdEGEYTPGTLvqIFLSVIVG-ALnlgnaSPcLE-------AFATGRAAATSIFETIDRKPiidcMSEDGYKLDR 415
Cdd:COG4618 260 GAYLVI-QGEITPGAM--IAASILMGrAL-----AP-IEqaiggwkQFVSARQAYRRLNELLAAVP----AEPERMPLPR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 416 IKGEIEFHNVTFHYPSRPEVkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRslniQWLR 495
Cdd:COG4618 327 PKGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----QWDR 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 496 DQ----IGIVEQEPVLFSTTIAENI-RYGreDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIA 570
Cdd:COG4618 402 EElgrhIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 571 RALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 646
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1076-1299 |
9.97e-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: 157.96 E-value: 9.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1076 GKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 1154
Cdd:cd03369 5 GEIEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQEPVLFACSIMDNI----KYGDntkeipmERVIAAAKqaqlhdfvmslpekyetnVGSQGSQLSRGEKQRIAIA 1230
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdpfdEYSD-------EEIYGALR------------------VSEGGLNLSQGQRQLLCLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1231 RAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGT 1299
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1092-1303 |
1.72e-43 |
|
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: 158.11 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-----PDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1164
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiyDLDVDVLELRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFACSIMDNIKYGDN-----TKEIPMERVIAAAKQAQLHDfvmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd03260 92 PFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKAALWD---------EVKDRLHALGLSGGQQQRLCLARALANEPEV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 1303
Cdd:cd03260 163 LLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
166-617 |
2.72e-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: 166.38 E-value: 2.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 166 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDInkinDAIADqmaLFIQRMTSTICGFLLG-------FFRG 238
Cdd:TIGR02868 80 AALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGaaavaaiAVLS 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 239 WKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAyaKAGVVADEVISSMRTVA---AFGGEKREVERYEKnlvfAQRWG 315
Cdd:TIGR02868 153 VPAALILAAGLLLAGFVAPLVSLRAARAAEQALAR--LRGELAAQLTDALDGAAelvASGALPAALAQVEE----ADREL 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 316 IRKGIVMGFFTGFVWCLIFLCYALAFWygSTLVLDEGEYTPGTLVQIFLSVIV-GALNLGNA----SPCLEAFATGRAAA 390
Cdd:TIGR02868 227 TRAERRAAAATALGAALTLLAAGLAVL--GALWAGGPAVADGRLAPVTLAVLVlLPLAAFEAfaalPAAAQQLTRVRAAA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 391 TSIFETIDRKPIIDCMS---EDGYKLDRIKgeIEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQL 467
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSapaAGAVGLGKPT--LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLAT 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 468 IQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQ 547
Cdd:TIGR02868 381 LAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDG 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 548 FDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRL 617
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
420-643 |
1.23e-42 |
|
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: 155.80 E-value: 1.23e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQ-- 492
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 493 WLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAA-------KEANAYNFIMDLP---QQfdtlvgegg 556
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlrkaalwDEVKDRLHALGLSggqQQ--------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 557 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAV 635
Cdd:cd03260 149 ---------RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLV 219
|
....*...
gi 21536378 636 ERGTHEEL 643
Cdd:cd03260 220 EFGPTEQI 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
433-659 |
4.27e-42 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 164.25 E-value: 4.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 433 PEVKILND-LNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTT 511
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 512 IAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDN 591
Cdd:PRK11174 439 LRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 592 ESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLVTLQSQ 659
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQE 586
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1085-1294 |
3.60e-41 |
|
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: 149.29 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYP--SRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQE 1162
Cdd:cd03246 8 FRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 PVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:cd03246 85 DELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1243 DEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQNADIIAVMAQGVV 1294
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1096-1247 |
3.76e-41 |
|
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: 148.56 E-value: 3.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLF-ACSIMDNI 1174
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1175 KYGdntkeIPMERVIAAAKQAQLHDFV--MSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1078-1298 |
4.20e-41 |
|
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: 149.39 E-value: 4.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIG 1157
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFACSIMDNIkygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKG 1298
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
420-647 |
4.70e-41 |
|
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: 151.33 E-value: 4.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPV--LFSTTIAENI-----RYGREDATMEDIV-QAAKEANAYNF----IMDLP---QQfdtlvgegggqmsggqk 564
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVafgpeNLGLPREEIRERVeEALELVGLEHLadrpPHELSggqKQ----------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 565 qRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEE 642
Cdd:COG1122 142 -RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPRE 220
|
....*
gi 21536378 643 LLERK 647
Cdd:COG1122 221 VFSDY 225
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1078-1307 |
4.89e-41 |
|
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: 150.95 E-value: 4.89e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPV--LFACSIMDNIKYG----DNTKEIPMERVIAAAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIAR 1231
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGpenlGLPREEIRERVEEALELVGLEHL-------ADRPP----HELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1232 AIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
140-390 |
8.09e-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: 152.71 E-value: 8.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 140 KFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMAL 219
Cdd:cd18557 37 ELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 220 FIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKR 299
Cdd:cd18557 117 LLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 300 EVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQIFLSVIVGALNLGNASPC 379
Cdd:cd18557 197 EIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVL-SGQLTVGELTSFILYTIMVASSVGGLSSL 275
|
250
....*....|.
gi 21536378 380 LEAFATGRAAA 390
Cdd:cd18557 276 LADIMKALGAS 286
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
420-634 |
3.27e-40 |
|
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: 146.59 E-value: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENIRYGREdatmediVQaakeanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIRNPKI 579
Cdd:cd03246 80 YLPQDDELFSGSIAENILSGGQ-------RQ-----------------------------------RLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRAADTIIGFEHGTA 634
Cdd:cd03246 118 LVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1092-1303 |
5.18e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 148.60 E-value: 5.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 A-CSIMDNIKYG---------DNTKEIPME---RViaaakqaQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAI 1233
Cdd:COG1126 90 PhLTVLENVTLApikvkkmskAEAEERAMElleRV-------GLADKADAYP-----------AQLSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1234 VRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 1303
Cdd:COG1126 152 AMEPKVMLFDEPTSALDPELVGEVlDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1078-1306 |
7.05e-40 |
|
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: 155.83 E-value: 7.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDS--QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVNVQFL 1152
Cdd:COG1123 261 LEVRNLSKRYPVRGKGgvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDltkLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1153 RSNIGIVSQEPV--LFAC-SIMDNI-----KYGDNTKEIPMERVIAAAKQAQLH-DFVMSLPekyetnvgsqgSQLSRGE 1223
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRmTVGDIIaeplrLHGLLSRAERRERVAELLERVGLPpDLADRYP-----------HELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1224 KQRIAIARAIVRDPKILLLDEATSALDTesekTVQVA-LD-----KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIE 1296
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDV----SVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485
|
250
....*....|
gi 21536378 1297 KGTHEELMAQ 1306
Cdd:COG1123 486 DGPTEEVFAN 495
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1095-1275 |
1.24e-39 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 146.50 E-value: 1.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 1174
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1175 KYGDNTKEIP--MERVIAAAKQAQLHDFVMslpekyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:COG4619 95 PFPFQLRERKfdRERALELLERLGLPPDIL------DKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPE 164
|
170 180
....*....|....*....|....*
gi 21536378 1253 SEKTVQVALDK--AREGRTCIVIAH 1275
Cdd:COG4619 165 NTRRVEELLREylAEEGRAVLWVSH 189
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1094-1306 |
9.67e-39 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 144.82 E-value: 9.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIVSQEPVLFA-CSIMD 1172
Cdd:COG1131 14 TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVPQEPALYPdLTVRE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIK-----YGDNTKEIPmERVIAAAKQAQLHDFvmslpekYETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:COG1131 93 NLRffarlYGLPRKEAR-ERIDELLELFGLTDA-------ADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1248 ALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:COG1131 161 GLDPEARRELwELLRELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1078-1306 |
2.32e-38 |
|
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: 143.49 E-value: 2.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQ---LLERfydPDQGKVMIDGHDSKKVN---VQ 1150
Cdd:cd03258 2 IELKNVSKVFGDTGGKvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1151 FLRSNIGIVSQEPVLFAC-SIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEK 1224
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVALpleiaGVPKAEIE-ERVLELLELVGLEDKADAYP-----------AQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1225 QRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHE 1301
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 21536378 1302 ELMAQ 1306
Cdd:cd03258 227 EVFAN 231
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1095-1316 |
5.91e-38 |
|
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: 143.13 E-value: 5.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 1174
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1175 kygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESE 1254
Cdd:cd03288 116 ---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1255 KTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQK-GAYYKLVTT 1316
Cdd:cd03288 193 NILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
420-615 |
7.14e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.11 E-value: 7.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENI----RYGREDATMEDIVQAAKEANAYNFIMDLP--------QQfdtlvgegggqmsggqkqRV 567
Cdd:COG4619 78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKPverlsggeRQ------------------RL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536378 568 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 615
Cdd:COG4619 140 ALIRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSH 189
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
144-360 |
1.38e-37 |
|
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: 143.07 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 144 YYAGIAVAVLITGYIQ-ICFWvIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQ 222
Cdd:cd18572 41 LLLLLSVLSGLFSGLRgGCFS-YAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 223 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 302
Cdd:cd18572 120 NLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREAR 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 303 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLV 360
Cdd:cd18572 200 RYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVL-SGRMSAGQLV 256
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1080-1292 |
1.65e-37 |
|
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: 140.29 E-value: 1.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1080 FVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIV 1159
Cdd:cd03225 2 LKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1160 SQEP--VLFACSIMDNIKYG-----DNTKEIPmERVIAAAKQAQLHDFvmslpEKYETnvgsqgSQLSRGEKQRIAIARA 1232
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGlenlgLPEEEIE-ERVEEALELVGLEGL-----RDRSP------FTLSGGQKQRVAIAGV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1233 IVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQG 1292
Cdd:cd03225 149 LAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1086-1298 |
2.97e-37 |
|
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: 140.33 E-value: 2.97e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL---RSNIGIVSQ 1161
Cdd:cd03257 10 SFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1162 EPvlFAC-----SIMDNIK-----YGDNTKEipmerviAAAKQAQLHDFV-MSLPEKYETnvgSQGSQLSRGEKQRIAIA 1230
Cdd:cd03257 90 DP--MSSlnprmTIGEQIAeplriHGKLSKK-------EARKEAVLLLLVgVGLPEEVLN---RYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1231 RAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 1298
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
420-633 |
5.22e-37 |
|
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: 137.70 E-value: 5.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW--LRDQ 497
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFST-TIAENIRYGredatmedivqaakeanaynfimdLP---QQfdtlvgegggqmsggqkqRVAIARAL 573
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG------------------------LSggqQQ------------------RVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGT 633
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1094-1296 |
6.81e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 139.02 E-value: 6.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHD----SKKVNVQFLRSNIGIVSQE---- 1162
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDisslSERELARLRRRHIGFVFQFfnll 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 PVLfacSIMDNI----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPK 1238
Cdd:COG1136 99 PEL---TALENValplLLAGVSRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1239 ILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQNADIIAVMAQGVVIE 1296
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
421-633 |
7.66e-37 |
|
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: 138.37 E-value: 7.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 421 EFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 500
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 501 VEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEANAYNFIMDLP-----------QQfdtlvgegggqmsggqkq 565
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENLGLpeEEIEERVEEALELVGLEGLRdrspftlsggqKQ------------------ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 566 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRA-ADTIIGFEHGT 633
Cdd:cd03225 142 RVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
145-359 |
7.73e-37 |
|
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: 141.23 E-value: 7.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 145 YAGIAVAVLITGYiqiCFwVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 224
Cdd:cd18780 52 VLIGSIATFLRSW---LF-TLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 225 TSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY 304
Cdd:cd18780 128 VQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 305 EKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTL 359
Cdd:cd18780 208 SEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVID-GELTTGLL 261
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1092-1298 |
4.03e-36 |
|
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: 136.50 E-value: 4.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 1170
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYG-----DNTKEIPmERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:cd03259 90 AENIAFGlklrgVPKAEIR-ARVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREPSLLLLDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1246 TSALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKG 1298
Cdd:cd03259 158 LSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
420-638 |
4.21e-36 |
|
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: 135.13 E-value: 4.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIG 499
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENIryGREDATMEdivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKI 579
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--GRRFSGGE-------------------RQ------------------RLALARILLQDAPI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERG 638
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
420-646 |
6.06e-36 |
|
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: 144.28 E-value: 6.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRP--EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWL 494
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 495 RDQIGIVEQEPV--LF-STTIAENIRYG---REDATMEDIVQAAKE-----------ANAYnfimdlPQQFdtlvgeggg 557
Cdd:COG1123 341 RRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEllervglppdlADRY------PHELsgg------ 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 558 qmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTA 634
Cdd:COG1123 409 -----qrqRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|..
gi 21536378 635 VERGTHEELLER 646
Cdd:COG1123 484 VEDGPTEEVFAN 495
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1080-1292 |
1.57e-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: 132.75 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1080 FVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIV 1159
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1160 SQepvlfacsimdnikygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd00267 79 PQ---------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQNA-DIIAVMAQG 1292
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1078-1306 |
2.08e-35 |
|
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: 142.73 E-value: 2.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFLRS 1154
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQEP--VLFACSIMDNI----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 1228
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIaealENLGLSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1229 IARAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 21536378 1306 Q 1306
Cdd:COG1123 233 A 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
420-627 |
2.22e-35 |
|
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: 134.52 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSR-PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlrDQI 498
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFS-TTIAENIRYGREDATM-----EDIVQAAKE-------ANAYnfimdlP-------QQfdtlvgegggq 558
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVpkaeaRERAEELLElvglsgfENAY------PhqlsggmRQ----------- 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 559 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTII 627
Cdd:cd03293 139 -------RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVV 203
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1092-1303 |
2.62e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.55 E-value: 2.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PDQ---GKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1164
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDiyDPDVDVVELRRRVGMVFQKPN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFACSIMDNIKYG-----DNTKEIPMERVIAAAKQAQLHDFVmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:COG1117 103 PFPKSIYDNVAYGlrlhgIKSKSELDEIVEESLRKAALWDEV-------KDRLKKSALGLSGGQQQRLCIARALAVEPEV 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDKAREgRTCIVI-------AHRLStiqnaDIIAVMAQGVVIEKGTHEEL 1303
Cdd:COG1117 176 LLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1076-1317 |
2.75e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 147.19 E-value: 2.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1076 GKIDFVDCKFTYpsRPD-SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS 1154
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIV 1234
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1235 RDPKILLLDEATSALDTESEKTVQVALDKarEGRTC--IVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKG-AYY 1311
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGsAFS 1468
|
....*..
gi 21536378 1312 KLV-TTG 1317
Cdd:PLN03130 1469 KMVqSTG 1475
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1078-1308 |
2.92e-35 |
|
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: 134.99 E-value: 2.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFlRSNIG 1157
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFA-CSIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIAR 1231
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYfaelyGLFDEELK-KRIEELIELLGLEEF---LDRRVGE--------LSTGMKKKVALAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1232 AIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIA-HRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQKG 1308
Cdd:COG4555 146 ALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1089-1292 |
3.06e-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: 132.70 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG--HDSKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedLTDLEDELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 A-CSIMDNIKYGdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:cd03229 89 PhLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536378 1246 TSALDTESEKTVQVALD--KAREGRTCIVIAHRLSTIQN-ADIIAVMAQG 1292
Cdd:cd03229 128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
420-644 |
3.45e-35 |
|
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: 135.17 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVL-FSTTIAENIRYGR---------EDATMEDIVQAA-KEANAYNFIMdlpQQFDTLvgegggqmsggqkqRVA 568
Cdd:COG1120 79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAVEEAlERTGLEHLAD---RPVDELsgg--------erqRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 569 IARALIRNPKILLLDMATSALD--NESEAMvqEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEEL 643
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDlaHQLEVL--ELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 21536378 644 L 644
Cdd:COG1120 226 L 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
421-633 |
3.48e-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: 3.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 421 EFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 500
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 501 VEQepvlFSttiaeniryGREdatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 580
Cdd:cd00267 78 VPQ----LS---------GGQ------------------------RQ------------------RVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 581 LLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGT 633
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
772-1009 |
3.56e-35 |
|
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: 136.15 E-value: 3.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 772 YAFLFSQILGTFSIP-------D---KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLG 841
Cdd:cd18557 2 LLFLLISSAAQLLLPyligrliDtiiKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 842 QDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRM 921
Cdd:cd18557 82 QEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 922 LTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYR 1001
Cdd:cd18557 160 IRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLW 239
|
....*...
gi 21536378 1002 YGGYLISN 1009
Cdd:cd18557 240 YGGYLVLS 247
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
418-639 |
5.34e-35 |
|
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: 132.92 E-value: 5.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHY-PSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 496
Cdd:cd03369 5 GEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFSTTIAENI-RYGREDAtmEDIVQAAKEANAYNfimDLPQQFDTLVgegggqmsggqkqrvAIARALIR 575
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNLdPFDEYSD--EEIYGALRVSEGGL---NLSQGQRQLL---------------CLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 576 NPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 639
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
420-644 |
7.81e-35 |
|
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: 133.48 E-value: 7.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLR 495
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 496 DQIGIVEQEPVLFST-TIAENIRYGREDATMEDIVQAAK------------EANAYnfimdlPQQFdtlvgegggqmSGG 562
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERvlellelvgledKADAY------PAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 563 QKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGT 639
Cdd:cd03258 145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGT 224
|
....*
gi 21536378 640 HEELL 644
Cdd:cd03258 225 VEEVF 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1078-1289 |
1.24e-34 |
|
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: 132.21 E-value: 1.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflrsnI 1156
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1157 GIVSQEPVLFA-CSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIAR 1231
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKaearERAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALAR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1232 AIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVM 1289
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVL 205
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
420-632 |
1.34e-34 |
|
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: 132.23 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPE-VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL 494
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 495 RDQIGIVEQEPVLFST-TIAENIRY-----GREDATMEDIVQAAKE-----ANAYNFIMDLP---QQfdtlvgegggqms 560
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEELLErvglgDRLNHYPSELSggqQQ------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 561 ggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEHG 632
Cdd:cd03255 148 -----RVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
420-636 |
1.71e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.09 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPS-RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI---QRfydPCEGMVTVDGHDIRSLNI---- 491
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSErela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 492 QWLRDQIGIVEQEPVLFST-TIAENI----RYGREDAtmEDIVQAAKEA--------NAYNFIMDLP---QQfdtlvgeg 555
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPElTALENValplLLAGVSR--KERRERARELlervglgdRLDHRPSQLSggqQQ-------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 556 ggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGT 633
Cdd:COG1136 152 ----------RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAARADRVIRLRDGR 221
|
...
gi 21536378 634 AVE 636
Cdd:COG1136 222 IVS 224
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
420-648 |
2.22e-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: 2.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqWLRDQIG 499
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIRYgreDATMEDIVQAAKEANAYNFI--MDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRN 576
Cdd:COG4555 78 VLPDERGLYDRlTVRENIRY---FAELYGLFDEELKKRIEELIelLGLEEFLDRRV----GELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 577 PKILLLDMATSALDNES-EAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERKG 648
Cdd:COG4555 151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
438-587 |
2.50e-34 |
|
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: 128.92 E-value: 2.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFS-TTIAENI 516
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 517 RYGREdatMEDIVQAAKEANAYNFI--MDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATS 587
Cdd:pfam00005 81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1072-1307 |
2.96e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 133.19 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1072 DNFQGKIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF 1151
Cdd:PRK13632 2 KNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIP---MERVIA-AAKQAQLHDFVMSLPEKyetnvgsqgsqLSRGEKQ 1225
Cdd:PRK13632 81 IRKKIGIIFQNPdnQFIGATVEDDIAFGLENKKVPpkkMKDIIDdLAKKVGMEDYLDKEPQN-----------LSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
|
....
gi 21536378 1304 MAQK 1307
Cdd:PRK13632 230 LNNK 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
420-646 |
6.94e-34 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 130.88 E-value: 6.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLRDQ 497
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFS-TTIAENIRYG--------REDAT---ME--DIVQAAKEANAYnfimdlP-------QQfdtlvgegg 556
Cdd:COG1126 79 VGMVFQQFNLFPhLTVLENVTLApikvkkmsKAEAEeraMEllERVGLADKADAY------PaqlsggqQQ--------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 557 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQH----GHTIISVAHRLSTVR-AADTIIGFEH 631
Cdd:COG1126 144 ---------RVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDVMRDlakeGMTMVVVTHEMGFAReVADRVVFMDG 211
|
250
....*....|....*
gi 21536378 632 GTAVERGTHEELLER 646
Cdd:COG1126 212 GRIVEEGPPEEFFEN 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
420-644 |
8.38e-34 |
|
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: 130.88 E-value: 8.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFS-TTIAENI-------RYGRedatmEDIVQAAKEANAynfIMDLPQQfdTLVGEGGGQMSGGQKQRVAIAR 571
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIalvpkllKWPK-----EKIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 572 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRL-STVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1078-1305 |
8.46e-34 |
|
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: 130.88 E-value: 8.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFA-CSIMDNIKYGDNTKEIPMERVIAAAKQAqLHDfvMSLPEkyETNVGSQGSQLSRGEKQRIAIARAIVRD 1236
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIALVPKLLKWPKEKIRERADEL-LAL--VGLDP--AEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1237 PKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRL-STIQNADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1092-1303 |
1.11e-33 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 133.68 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 1170
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFPhLTV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:COG3842 95 AENVAFGLRMRGVPKaeirARVAELLELVGLEGLADRYP-----------HQLSGGQQQRVALARALAPEPRVLLLDEPL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1247 SALDTESEKTVQVALDK--AREGRTCIVIAHRLS---TIqnADIIAVMAQGVVIEKGTHEEL 1303
Cdd:COG3842 164 SALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1092-1294 |
1.41e-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: 129.19 E-value: 1.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTllrCINLLEE---PDSGTIIIDGLklTDDKKNINELRQKVGMVFQQFNLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 A-CSIMDNIKYGD-NTKEIPMERVIAAAKQA----QLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:cd03262 89 PhLTVLENITLAPiKVKGMSKAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1241 LLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVV 1294
Cdd:cd03262 158 LFDEPTSALDPELVGEVlDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1086-1305 |
1.69e-33 |
|
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: 129.92 E-value: 1.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP- 1163
Cdd:COG1124 10 SYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1164 ---------------VLFACSIMDNikygdntkeipMERVIAAAKQAQLHDfvmSLPEKYetnvgsqGSQLSRGEKQRIA 1228
Cdd:COG1124 90 aslhprhtvdrilaePLRIHGLPDR-----------EERIAELLEQVGLPP---SFLDRY-------PHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1229 IARAIVRDPKILLLDEATSALDTesekTVQVA-LD-----KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHE 1301
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDV----SVQAEiLNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVA 224
|
....
gi 21536378 1302 ELMA 1305
Cdd:COG1124 225 DLLA 228
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1078-1305 |
2.72e-33 |
|
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: 129.16 E-value: 2.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV---QFLRS 1154
Cdd:cd03261 1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQEPVLF-ACSIMDNI-----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 1228
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVafplrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYP-----------AELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1229 IARAIVRDPKILLLDEATSALD-TESEKTVQVALD-KAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1092-1294 |
3.11e-33 |
|
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: 126.74 E-value: 3.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVLFA-CSI 1170
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYEnLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYgdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgsqlSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:cd03230 91 RENLKL-------------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 1251 TESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVV 1294
Cdd:cd03230 128 PESRREFwELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
420-645 |
4.37e-33 |
|
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: 128.56 E-value: 4.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 496
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFST-TIAENIRYG-RE-----DATMEDIVQAAKEAnaynfiMDLPQQFDTLvgegggqmsggqkqRVAI 569
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREhtdlsEAEIRELVLEKLEL------VGLPGAADKMpsels----ggmrkRVAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 645
Cdd:COG1127 153 ARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
420-636 |
5.50e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.86 E-value: 5.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 496
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQE-PVLFSTTIAENIRY-----GREDATMEDIVQAA--------KeanAYNFIMDLP---QQfdtlvgegggqm 559
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVldlvglsdK---AKALPHELSggeQQ------------ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 560 sggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADT-IIGFEHGTAVE 636
Cdd:COG2884 145 ------RVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1086-1306 |
6.03e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 131.35 E-value: 6.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVNVQFL---RSNIGI 1158
Cdd:COG1135 10 TFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELraaRRKIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1159 VSQEPVLF-ACSIMDNIKY-----GDNTKEIPmERViaaakqAQLHDFVmSLPEK---YEtnvgsqgSQLSRGEKQRIAI 1229
Cdd:COG1135 87 IFQHFNLLsSRTVAENVALpleiaGVPKAEIR-KRV------AELLELV-GLSDKadaYP-------SQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1230 ARAIVRDPKILLLDEATSALDTESekTVQVA--LDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELM 1304
Cdd:COG1135 152 ARALANNPKVLLCDEATSALDPET--TRSILdlLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVLDVF 229
|
..
gi 21536378 1305 AQ 1306
Cdd:COG1135 230 AN 231
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
420-638 |
6.04e-33 |
|
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: 127.25 E-value: 6.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 499
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRN-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIRYGREDATM--EDIVQAAKEANAynfIMDLP--------------QQfdtlvgegggqmsgg 562
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEgllnryphelsggqQQ--------------- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 563 qkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHGTAVERG 638
Cdd:cd03259 138 ---RVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
420-646 |
6.67e-33 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 127.87 E-value: 6.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIG 499
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIR-----YGREDATMEDIVQAAKEAnaynfiMDLPQQFDTLVgegggqmsggqKQ-------R 566
Cdd:COG1131 77 YVPQEPALYPDlTVRENLRffarlYGLPRKEARERIDELLEL------FGLTDAADRKV-----------GTlsggmkqR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 567 VAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 644
Cdd:COG1131 140 LGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELK 219
|
..
gi 21536378 645 ER 646
Cdd:COG1131 220 AR 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1092-1303 |
7.98e-33 |
|
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: 127.74 E-value: 7.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSkkVNVQFLRSNIGIVSQEPVLFA-CSI 1170
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPhLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:cd03300 90 FENIAFGLRLKKLPKaeikERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1247 SALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:cd03300 159 GALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
420-638 |
1.22e-32 |
|
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: 126.85 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD-- 496
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 -QIGIVEQEPvlFST-----TIAENIRYGREDATMEDIVQAAKEANAYNFI-MDLP---------------QQfdtlvge 554
Cdd:cd03257 82 kEIQMVFQDP--MSSlnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgVGLPeevlnryphelsggqRQ------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 555 gggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEH 631
Cdd:cd03257 153 -----------RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQeeLGLTLLFITHDLGVVAKiADRVAVMYA 221
|
....*..
gi 21536378 632 GTAVERG 638
Cdd:cd03257 222 GKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1092-1305 |
2.19e-32 |
|
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: 126.63 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV---QFLRSNIGIVSQEPVLF-A 1167
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFdS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNI-----KYGDNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:COG1127 97 LTVFENVafplrEHTDLSEAEIRELVLEKLELVGLPGAADKMP-----------SELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1243 DEATSALD--TeSEKTVQVALD-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:COG1127 166 DEPTAGLDpiT-SAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
420-646 |
2.58e-32 |
|
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: 133.10 E-value: 2.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQWLRD 496
Cdd:COG1123 5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEP--VLFSTTIAENIRYGRE--DATMEDIVQAAKEANAYNFIMDL----PQQFdtlvgegggqmSGGQKQRVA 568
Cdd:COG1123 84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLEAVGLERRldryPHQL-----------SGGQRQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 569 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLE 645
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQreRGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
.
gi 21536378 646 R 646
Cdd:COG1123 233 A 233
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
139-390 |
2.87e-32 |
|
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: 128.05 E-value: 2.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 139 IKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 218
Cdd:cd07346 39 LWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 219 LFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEK 298
Cdd:cd07346 119 QLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEE 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 299 REVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV------QIFLSVIVGALN 372
Cdd:cd07346 199 REIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQ-GSLTIGELVaflaylGMLFGPIQRLAN 277
|
250
....*....|....*...
gi 21536378 373 LGNaspcleAFATGRAAA 390
Cdd:cd07346 278 LYN------QLQQALASL 289
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
146-370 |
2.96e-32 |
|
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: 127.60 E-value: 2.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 225
Cdd:cd18576 43 LGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 226 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYE 305
Cdd:cd18576 123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 306 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQ-IFLSVIVGA 370
Cdd:cd18576 203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLA-GELTAGDLVAfLLYTLFIAG 267
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1078-1298 |
4.27e-32 |
|
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: 124.83 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDS---KKVNVQFLRS 1154
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQE-PVLFACSIMDNIKY-----GDNTKEIPmERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIA 1228
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFalevtGVPPREIR-KRVPAALELVGLSHKHRALPA-----------ELSGGEQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1229 IARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAhrlstIQNADIIAVMAQGV-VIEKG 1298
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA-----THAKELVDTTRHRViALERG 212
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1078-1294 |
5.05e-32 |
|
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: 124.91 E-value: 5.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVN----V 1149
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSekelA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1150 QFLRSNIGIVSQE----PVLfacSIMDNIkygdntkEIPMErvIAAAKQAQLHDFVMSLPEKyetnVGSQG------SQL 1219
Cdd:cd03255 78 AFRRRHIGFVFQSfnllPDL---TALENV-------ELPLL--LAGVPKKERRERAEELLER----VGLGDrlnhypSEL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1220 SRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIA-HRLSTIQNADIIAVMAQGVV 1294
Cdd:cd03255 142 SGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVmELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
420-643 |
5.65e-32 |
|
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: 125.37 E-value: 5.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL---NIQWLRD 496
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkgkALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFS-TTIAENIRYGREDA-----------TMEDIVQAAKEANAYNFIMDLPQQFDTLvgegggqmSGGQK 564
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGRrstwrslfglfPKEEKQRALAALERVGLLDKAYQRADQL--------SGGQQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 565 QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHE 641
Cdd:cd03256 151 QRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPA 230
|
..
gi 21536378 642 EL 643
Cdd:cd03256 231 EL 232
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1078-1292 |
6.81e-32 |
|
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: 123.73 E-value: 6.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDSQ--VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ErfYDPDQGKVmidghdskkvnvqFLR 1153
Cdd:cd03250 1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSV-------------SVP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1154 SNIGIVSQEPVLFACSIMDNIKYGdntKEIPMERVIAAAKQAQLH-DFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARA 1232
Cdd:cd03250 66 GSIAYVSQEPWIQNGTIRENILFG---KPFDEERYEKVIKACALEpDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1233 IVRDPKILLLDEATSALDTESEKTV--QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQG 1292
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1078-1298 |
1.18e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 124.01 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRS 1154
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQE-PVLFACSIMDNIKY-----GDNTKEIpMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIA 1228
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEI-RRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1229 IARAIVRDPKILLLDEATSALDTE-SEKTVQVaLDKAREGRTCIVIA-HrlstiqNADIIAVMAQGVV-IEKG 1298
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPEtSWEIMEL-LEEINRRGTTVLIAtH------DLELVDRMPKRVLeLEDG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
420-615 |
1.62e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 124.82 E-value: 1.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqwLRDQI 498
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFS-TTIAENIRYGREDATM-----EDIVQAAKE-------ANAYnfimdlP-------QQfdtlvgegggq 558
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVpkaerRERARELLElvglagfEDAY------PhqlsggmRQ----------- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 559 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 615
Cdd:COG1116 146 -------RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTH 197
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
420-646 |
1.79e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 127.14 E-value: 1.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 499
Cdd:COG3842 6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFS-TTIAENIRYG----------REDATME--DIVQAAKEANAYnfIMDLP---QQfdtlvgegggqmsggq 563
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGlrmrgvpkaeIRARVAEllELVGLEGLADRY--PHQLSggqQQ---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 564 kqRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQH--GHTIISVAHRLS---TVraADTIIGFEHGTAVER 637
Cdd:COG3842 143 --RVALARALAPEPRVLLLDEPLSALDAKLrEEMREE-LRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQV 217
|
....*....
gi 21536378 638 GTHEELLER 646
Cdd:COG3842 218 GTPEEIYER 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1096-1306 |
2.23e-31 |
|
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: 124.68 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRSN-IGIVSQEPVLFA-CSI 1170
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKkISMVFQSFALLPhRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:cd03294 120 LENVAFGLEVQGVPraerEERAAEALELVGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1247 SALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:cd03294 189 SALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1095-1302 |
4.10e-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: 122.83 E-value: 4.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDN 1173
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1174 IKYG-----DNTKEIPmERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:cd03299 92 IAYGlkkrkVDKKEIE-RKVLEIAEMLGIDHL---LNRKPET--------LSGGEQQRVAIARALVVNPKILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1249 LDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEE 1302
Cdd:cd03299 160 LDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1085-1304 |
4.56e-31 |
|
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: 123.23 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPV 1164
Cdd:COG1120 9 VGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 L-FACSIMDNIKYG---------DNTKEipMERVIAAA-KQAQLHDFVmslpekyETNVgsqgSQLSRGEKQRIAIARAI 1233
Cdd:COG1120 86 ApFGLTVRELVALGryphlglfgRPSAE--DREAVEEAlERTGLEHLA-------DRPV----DELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1234 VRDPKILLLDEATSALDtesektV--QVAL-----DKARE-GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 1304
Cdd:COG1120 153 AQEPPLLLLDEPTSHLD------LahQLEVlellrRLARErGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
165-359 |
4.71e-31 |
|
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: 124.55 E-value: 4.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 165 IAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLV 244
Cdd:cd18573 67 IAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 245 IISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGF 324
Cdd:cd18573 147 MLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGL 226
|
170 180 190
....*....|....*....|....*....|....*...
gi 21536378 325 F---TGFVWCLIFLCyalAFWYGSTLVLdEGEYTPGTL 359
Cdd:cd18573 227 FfgsTGFSGNLSLLS---VLYYGGSLVA-SGELTVGDL 260
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
429-1320 |
5.37e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 132.98 E-value: 5.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 429 YPSRPEVkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVtvdghdirslniqWLRDQIGIVEQEPVLF 508
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 STTIAENIRYGRED--ATMEDIVQAAK-EANaynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMA 585
Cdd:PTZ00243 734 NATVRGNILFFDEEdaARLADAVRVSQlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 586 TSALDNE-SEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLeRKGVYFTLVTlQSQGNQAL 664
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAA-ELKENKDS 887
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 665 NEEDiKDATEDDMLArtfSRGSYQDSLRASIRQRSKSQLSYLVHEPPlavVDHKSTYEEDRKDKDIPVQEEVE------- 737
Cdd:PTZ00243 888 KEGD-ADAEVAEVDA---APGGAVDHEPPVAKQEGNAEGGDGAALDA---AAGRLMTREEKASGSVPWSTYVAylrfcgg 960
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 738 -PAPVRRILKFSAPE--------WPYMLvgSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEqrsqingVCLLFVAMGCV 808
Cdd:PTZ00243 961 lHAAGFVLATFAVTElvtvssgvWLSMW--STRSFKLSAATYLYVYLGIVLLGTFSVPLRFF-------LSYEAMRRGSR 1031
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 809 SLFTQFLQGYAFAKsgelltkrlrkfgframlgqdIAWFDdlRNSPGALTTRLATDAsqvqGAAGSQIGMIVNSFTNVTV 888
Cdd:PTZ00243 1032 NMHRDLLRSVSRGT---------------------MSFFD--TTPLGRILNRFSRDI----DILDNTLPMSYLYLLQCLF 1084
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 889 AM---IIAFSFSWKLSLVIL--CFFPFLAL-----SGATQTRMLTGFASRDkqalemVGQITNEALSNIRTVAGIGKERR 958
Cdd:PTZ00243 1085 SIcssILVTSASQPFVLVALvpCGYLYYRLmqfynSANREIRRIKSVAKSP------VFTLLEEALQGSATITAYGKAHL 1158
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 959 FI-EALEtELEKPFKTAIQK--------------ANIYGFCFAFAQCIMFIANSASYRYGgyLIS---------NEGLhf 1014
Cdd:PTZ00243 1159 VMqEALR-RLDVVYSCSYLEnvanrwlgvrveflSNIVVTVIALIGVIGTMLRATSQEIG--LVSlsltmamqtTATL-- 1233
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1015 SYVFRVISAVVLSATALGRAFSYTPSYAKAKISA--ARFFQLLDRQ------------PPISVYNTAGEkwdNFQ-GKID 1079
Cdd:PTZ00243 1234 NWLVRQVATVEADMNSVERLLYYTDEVPHEDMPEldEEVDALERRTgmaadvtgtvviEPASPTSAAPH---PVQaGSLV 1310
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1080 FVDCKFTY----PsrpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN 1155
Cdd:PTZ00243 1311 FEGVQMRYreglP-----LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1156 IGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIV- 1234
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLk 1462
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1235 RDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL-MAQKGAYYKL 1313
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSM 1542
|
....*..
gi 21536378 1314 VTTGSPI 1320
Cdd:PTZ00243 1543 VEALGRS 1549
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
420-647 |
7.28e-31 |
|
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: 122.92 E-value: 7.28e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL-NIQWLRDQI 498
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEP--VLFSTTIAENIRYGRED-----ATMEDIVQ-AAKEANAYNFIMDLPQ-------Qfdtlvgegggqmsggq 563
Cdd:TIGR04520 80 GMVFQNPdnQFVGATVEDDVAFGLENlgvprEEMRKRVDeALKLVGMEDFRDREPHllsggqkQ---------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 564 kqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHE 641
Cdd:TIGR04520 144 --RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
....*.
gi 21536378 642 ELLERK 647
Cdd:TIGR04520 222 EIFSQV 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1077-1292 |
7.47e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 122.89 E-value: 7.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1077 KIDFVDCKFTYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSN 1155
Cdd:COG1116 7 ALELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1156 IGIVSQEPVLFA-CSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIA 1230
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKaerrERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1231 RAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAH------RLstiqnADIIAVMAQG 1292
Cdd:COG1116 151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
755-1012 |
9.29e-31 |
|
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: 123.43 E-value: 9.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 755 MLVGSVGAAVNGTVTPLYAFLFSQILGTFsIPDKeeQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 834
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDDV-IPAG--DLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 835 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 914
Cdd:cd07346 78 LFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 915 GATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFI 994
Cdd:cd07346 156 LRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL 235
|
250
....*....|....*...
gi 21536378 995 ANSASYRYGGYLISNEGL 1012
Cdd:cd07346 236 GTALVLLYGGYLVLQGSL 253
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1077-1306 |
9.50e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.20 E-value: 9.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1077 KIDFVDCKFTYPSRpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNI 1156
Cdd:PRK13635 5 IIRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1157 GIVSQEP--VLFACSIMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIA 1230
Cdd:PRK13635 84 GMVFQNPdnQFVGATVQDDVAFGLENIGVPreemVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1231 RAIVRDPKILLLDEATSALDTESEKTV--QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVleTVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
420-643 |
1.44e-30 |
|
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: 121.07 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 496
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLF-STTIAENIRYG-RE-----DATMEDIVQAAKEAnaynfiMDLPQQFDTLVgeggGQMSGGQKQRVAI 569
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPlREhtrlsEEEIREIVLEKLEA------VGLRGAEDLYP----AELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 643
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
420-632 |
1.69e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 121.32 E-value: 1.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 496
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFS-TTIAENI----------------RYGREDatmediVQAAKEANAynfIMDLP-------------- 545
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagrlgrtstwrsllgLFPPED------RERALEALE---RVGLAdkayqradqlsggq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 546 QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA- 622
Cdd:COG3638 152 QQ------------------RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRy 213
|
250
....*....|
gi 21536378 623 ADTIIGFEHG 632
Cdd:COG3638 214 ADRIIGLRDG 223
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
113-660 |
1.74e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 131.25 E-value: 1.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 113 VWTNSSLNQNMtngtRCGLLNIESEMIKFASyyagiaVAVLITGyiqiCFWVIAAARQIQK-MRKFYFRRIMRMEIGWFD 191
Cdd:PLN03232 937 IWTDQSTPKSY----SPGFYIVVYALLGFGQ------VAVTFTN----SFWLISSSLHAAKrLHDAMLNSILRAPMLFFH 1002
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 192 CNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLgffRGWKLTLVIISVSPLIGIGAATIGLSVSkfTDYEL 271
Cdd:PLN03232 1003 TNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFAL---IGTVSTISLWAIMPLLILFYAAYLYYQS--TSREV 1077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 272 K---------AYAKAGVvADEVISSMRTVAAFGGEKREVERY-EKNLVF------AQRW-GIRKGIVMGFftgfvwcLIF 334
Cdd:PLN03232 1078 RrldsvtrspIYAQFGE-ALNGLSSIRAYKAYDRMAKINGKSmDNNIRFtlantsSNRWlTIRLETLGGV-------MIW 1149
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 335 LCYALA-FWYGSTlvldEGEYTPGTLVQIFLSVIVgalnlgNASPCLEAFATGRAAATSIFETIDR-KPIIDCMSE--DG 410
Cdd:PLN03232 1150 LTATFAvLRNGNA----ENQAGFASTMGLLLSYTL------NITTLLSGVLRQASKAENSLNSVERvGNYIDLPSEatAI 1219
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 411 YKLDR------IKGEIEFHNVTFHYpsRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG 483
Cdd:PLN03232 1220 IENNRpvsgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD 1297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 484 HDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYGRE--DAtmeDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSG 561
Cdd:PLN03232 1298 CDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEhnDA---DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSV 1374
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 562 GQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHE 641
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQ 1454
|
570 580
....*....|....*....|
gi 21536378 642 ELLERKG-VYFTLVtlQSQG 660
Cdd:PLN03232 1455 ELLSRDTsAFFRMV--HSTG 1472
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
420-646 |
2.23e-30 |
|
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: 121.06 E-value: 2.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPE-VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 498
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVL-----FS--TTIAENIRYGREDATMEDIVQAAKEanaynfiMDLP---------------QQfdtlvgegg 556
Cdd:COG1124 82 QMVFQDPYAslhprHTvdRILAEPLRIHGLPDREERIAELLEQ-------VGLPpsfldryphqlsggqRQ--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 557 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGT 633
Cdd:COG1124 146 ---------RVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVaHLCDRVAVMQNGR 216
|
250
....*....|...
gi 21536378 634 AVERGTHEELLER 646
Cdd:COG1124 217 IVEELTVADLLAG 229
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
113-653 |
2.29e-30 |
|
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: 130.84 E-value: 2.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 113 VWTNSSLNQNMTNGTRcgllniESEMIKFASYYA-GIAVAVLITGY-IQICFWVIAAARQIQKMrkfYFRRIMRMEIGWF 190
Cdd:TIGR00957 986 YWLSLWTDDPMVNGTQ------NNTSLRLSVYGAlGILQGFAVFGYsMAVSIGGIQASRVLHQD---LLHNKLRSPMSFF 1056
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 191 DCNSVGELNTRFSDDINKINDAIADQMALFIQrmtsticgfllGFFRGWKLTLVIISVSPLIGIGAATIGLS---VSKF- 266
Cdd:TIGR00957 1057 ERTPSGNLVNRFSKELDTVDSMIPPVIKMFMG-----------SLFNVIGALIVILLATPIAAVIIPPLGLLyffVQRFy 1125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 267 --TDYELK---AYAKAGVVA--DEVISSMRTVAAFGGEKR-------EVERYEKNL---VFAQRW-GIRKGIVMGfftgf 328
Cdd:TIGR00957 1126 vaSSRQLKrleSVSRSPVYShfNETLLGVSVIRAFEEQERfihqsdlKVDENQKAYypsIVANRWlAVRLECVGN----- 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 329 vwCLIFLCYALAfwygstlVLDEGEYTPGtLVQIFLSV---IVGALN-LGNASPCLEA--FATGRAAATSIFETIDRKPI 402
Cdd:TIGR00957 1201 --CIVLFAALFA-------VISRHSLSAG-LVGLSVSYslqVTFYLNwLVRMSSEMETniVAVERLKEYSETEKEAPWQI 1270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 403 IDCMSEDGYKLdriKGEIEFHNVTFHYpsRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTV 481
Cdd:TIGR00957 1271 QETAPPSGWPP---RGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 482 DGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAENI----RYGREDATMedivqAAKEANAYNFIMDLPQQFDTLVGEGGG 557
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEVWW-----ALELAHLKTFVSALPDKLDHECAEGGE 1420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 558 QMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVER 637
Cdd:TIGR00957 1421 NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEF 1500
|
570
....*....|....*.
gi 21536378 638 GTHEELLERKGVYFTL 653
Cdd:TIGR00957 1501 GAPSNLLQQRGIFYSM 1516
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
418-654 |
2.95e-30 |
|
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: 121.17 E-value: 2.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYPS--RPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLR 495
Cdd:cd03288 18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 496 DQIGIVEQEPVLFSTTIAENIRYGREdATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIR 575
Cdd:cd03288 95 SRLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 576 NPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERK-GVYFTLV 654
Cdd:cd03288 174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
420-644 |
3.01e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 123.26 E-value: 3.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD-- 496
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 -QIGIVEQEPVLFST-TIAENIRYGREDATM--EDIVQAAKE----------ANAYnfimdlP-------QQfdtlvgeg 555
Cdd:COG1135 82 rKIGMIFQHFNLLSSrTVAENVALPLEIAGVpkAEIRKRVAEllelvglsdkADAY------PsqlsggqKQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 556 ggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHG 632
Cdd:COG1135 148 ----------RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInrELGLTIVLITHEMDVVRRiCDRVAVLENG 217
|
250
....*....|..
gi 21536378 633 TAVERGTHEELL 644
Cdd:COG1135 218 RIVEQGPVLDVF 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1094-1303 |
9.87e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 122.10 E-value: 9.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLF-ACSIMD 1172
Cdd:COG3839 17 EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYpHMTVYE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKYG-----DNTKEIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:COG3839 95 NIAFPlklrkVPKAEI-DRRVREAAELLGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPLS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1248 ALD------TESE-KTVQvaldkAREGRTCIVIAHRLS---TIqnADIIAVMAQGVVIEKGTHEEL 1303
Cdd:COG3839 163 NLDaklrveMRAEiKRLH-----RRLGTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1086-1306 |
1.03e-29 |
|
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: 121.31 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDP---DQGKVMIDGHD----SKKVNVQFLRSNIG 1157
Cdd:COG0444 10 YFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDllklSEKELRKIRGREIQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPvlFAC---------SIMDNIKY-GDNTKEIPMERVIAAAKQAQLHDfvmslPEKYetnVGSQGSQLSRGEKQRI 1227
Cdd:COG0444 90 MIFQDP--MTSlnpvmtvgdQIAEPLRIhGGLSKAEARERAIELLERVGLPD-----PERR---LDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1228 AIARAIVRDPKILLLDEATSALDTesekTVQVA-LD-----KAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTH 1300
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDV----TIQAQiLNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEGPV 235
|
....*.
gi 21536378 1301 EELMAQ 1306
Cdd:COG0444 236 EELFEN 241
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1078-1306 |
1.35e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 119.84 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEP--VLFACSIMDNIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIAR 1231
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHeemkERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1232 AIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1092-1302 |
1.79e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 121.98 E-value: 1.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSI 1170
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPhMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:PRK09452 104 FENVAFGLRMQKTPaaeiTPRVMEALRMVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1247 SALDTESEKTVQVALdKA--RE-GRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHEE 1302
Cdd:PRK09452 173 SALDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
420-632 |
1.93e-29 |
|
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: 117.25 E-value: 1.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLRDQ 497
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFS-TTIAENIRYG--------REDAT---ME--DIVQAAKEANAYnfimdlP-------QQfdtlvgegg 556
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLApikvkgmsKAEAEeraLEllEKVGLADKADAY------PaqlsggqQQ--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 557 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKI----QHGHTIISVAHRLSTVR-AADTIIGFEH 631
Cdd:cd03262 143 ---------RVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMkdlaEEGMTMVVVTHEMGFAReVADRVIFMDD 210
|
.
gi 21536378 632 G 632
Cdd:cd03262 211 G 211
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
406-646 |
2.28e-29 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 118.22 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 406 MSEDGYKLDRIkgeIEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD--P---CEGMVT 480
Cdd:COG1117 1 MTAPASTLEPK---IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 481 VDGHDI--RSLNIQWLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAA-KEA------------NAyn 539
Cdd:COG1117 75 LDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKAalwdevkdrlkkSA-- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 540 fiMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR 616
Cdd:COG1117 153 --LGLSggqQQ------------------RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHN 212
|
250 260 270
....*....|....*....|....*....|.
gi 21536378 617 LS-TVRAADTIIGFEHGTAVERGTHEELLER 646
Cdd:COG1117 213 MQqAARVSDYTAFFYLGELVEFGPTEQIFTN 243
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
420-643 |
3.36e-29 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 117.40 E-value: 3.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 496
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRgkkLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFS-TTIAENIRYGREDA-----------TMEDIvQAAKEANAYNFIMDLP-QQFDTLvgegggqmSGGQ 563
Cdd:TIGR02315 80 RIGMIFQHYNLIErLTVLENVLHGRLGYkptwrsllgrfSEEDK-ERALSALERVGLADKAyQRADQL--------SGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 564 KQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTH 640
Cdd:TIGR02315 151 QQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInkEDGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGAP 230
|
...
gi 21536378 641 EEL 643
Cdd:TIGR02315 231 SEL 233
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
420-645 |
3.49e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.50 E-value: 3.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqwLRDQIG 499
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVL---FSTTIAENI------------RYGREDatmEDIVQAA-KEANAYNF----IMDLP---QQfdtlvgegg 556
Cdd:COG1121 79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRAD---REAVDEAlERVGLEDLadrpIGELSggqQQ--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 557 gqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTII-----GF 629
Cdd:COG1121 147 ---------RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREyFDRVLllnrgLV 217
|
250
....*....|....*.
gi 21536378 630 EHGTAVERGTHEELLE 645
Cdd:COG1121 218 AHGPPEEVLTPENLSR 233
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
418-660 |
4.98e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 126.78 E-value: 4.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYpsRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 496
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFSTTIAENIRYGRE--DAtmeDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALI 574
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNLDPFNEhnDA---DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 575 RNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVYFTLV 654
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
....*.
gi 21536378 655 tLQSQG 660
Cdd:PLN03130 1471 -VQSTG 1475
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
420-647 |
6.07e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 117.78 E-value: 6.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEP---VLFSTT---IA---ENIRYGREDatMEDIV-QAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 569
Cdd:PRK13632 87 IIFQNPdnqFIGATVeddIAfglENKKVPPKK--MKDIIdDLAKKVGMEDYLDKEPQNL-----------SGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
421-638 |
7.43e-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: 114.45 E-value: 7.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 421 EFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGI 500
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 501 VEqepvlfsttiaenirygredatmedivQAAKEANAYNFIMdlpQQFDTLvgegggqmsggqkqRVAIARALIRNPKIL 580
Cdd:cd03214 78 VP---------------------------QALELLGLAHLAD---RPFNELsgg--------erqRVLLARALAQEPPIL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 581 LLDMATSALD--NESEAMvqEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERG 638
Cdd:cd03214 120 LLDEPTSHLDiaHQIELL--ELLRRLarERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
420-627 |
8.67e-29 |
|
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: 114.03 E-value: 8.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIG 499
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIRY--GredatMedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRN 576
Cdd:cd03230 77 YLPEEPSLYENlTVRENLKLsgG-----M--------------------KQ------------------RLALAQALLHD 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 577 PKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTII 627
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAeRLCDRVA 166
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1091-1303 |
9.14e-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: 116.28 E-value: 9.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CS 1169
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFRhMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYGDNTKEIPmERVIAAAKQAQLHDFVM-----SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:cd03296 91 VFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLKlvqldWLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1245 ATSALDTESEKTVQVALDKARE--GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1082-1294 |
1.17e-28 |
|
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: 114.94 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1082 DCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqflRSNIGIVSQ 1161
Cdd:cd03235 4 DLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1162 EPVL---FACSIMDNIKYGDNTKEIPMERVIAAAKQA--QLHDFV-MSlpEKYETNVGsqgsQLSRGEKQRIAIARAIVR 1235
Cdd:cd03235 76 RRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKvdEALERVgLS--ELADRQIG----ELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1236 DPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVV 1294
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1078-1303 |
1.42e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.71 E-value: 1.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHDSKkVNVQFLRS 1154
Cdd:COG1118 3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLF-TNLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQEPVLFA-CSIMDNIKYGdntkeIPMERVIAAAKQAQlhdfVMSLPEKyetnVGSQG------SQLSRGEKQRI 1227
Cdd:COG1118 76 RVGFVFQHYALFPhMTVAENIAFG-----LRVRPPSKAEIRAR----VEELLEL----VQLEGladrypSQLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1228 AIARAIVRDPKILLLDEATSALDTESEKTVQVALdkaRE-----GRTCIVIAH------RLstiqnADIIAVMAQGVVIE 1296
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDAKVRKELRRWL---RRlhdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQ 214
|
....*..
gi 21536378 1297 KGTHEEL 1303
Cdd:COG1118 215 VGTPDEV 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
421-627 |
2.39e-28 |
|
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: 114.17 E-value: 2.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 421 EFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdirsLNIQWLRDQIGI 500
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-----KPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 501 VEQEPVL---FSTTIAENI------------RYGREDatMEDIVQAAKEANAYNFImdlPQQFDTLvgegggqmSGGQKQ 565
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVlmglyghkglfrRLSKAD--KAKVDEALERVGLSELA---DRQIGEL--------SGGQQQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 566 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTII 627
Cdd:cd03235 140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVL 203
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
420-632 |
3.98e-28 |
|
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: 113.27 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRD 496
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFST-TIAENIRYGRE--DATMEDIVQAAKEANAynfIMDLPQQFDTLvgegGGQMSGGQKQRVAIARAL 573
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHG 632
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVdTTRHRVIALERG 212
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
436-643 |
9.30e-28 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 113.72 E-value: 9.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQW--LRDQIGIVEQEPVLF 508
Cdd:PRK14239 19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 STTIAENIRYG------REDATMEDIVQAA-KEANAYNFIMDlpQQFDTLVGEGGGQMSggqkqRVAIARALIRNPKILL 581
Cdd:PRK14239 99 PMSIYENVVYGlrlkgiKDKQVLDEAVEKSlKGASIWDEVKD--RLHDSALGLSGGQQQ-----RVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 582 LDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEEL 643
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1095-1298 |
1.76e-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: 111.58 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkVN-VQFLRSNIGIVSQEPVLFA-CSIMD 1172
Cdd:cd03301 15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRD---VTdLPPKDRDIAMVFQNYALYPhMTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKYGDNTKEIPM----ERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:cd03301 92 NIAFGLKLRKVPKdeidERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1249 LDTESEKTVQVALDK--AREGRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKG 1298
Cdd:cd03301 161 LDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1085-1298 |
1.78e-27 |
|
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: 110.22 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQepv 1164
Cdd:cd03214 7 VGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 lfacsimdnikygdntkeipmerviaAAKQAQLHDFVmslpekyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:cd03214 81 --------------------------ALELLGLAHLA-------DRPF----NELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1245 ATSALDTESektvQVALDK------AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKG 1298
Cdd:cd03214 124 PTSHLDIAH----QIELLEllrrlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1095-1305 |
2.61e-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: 111.76 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIVS--QEPVLFA-CSIM 1171
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPeLTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 DNI--------KYGDNTKEIPMERVIAAAKQAQLHDFVmSLPEKYETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:cd03219 94 ENVmvaaqartGSGLLLARARREEREARERAEELLERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1244 EATSAL-DTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:cd03219 169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1085-1305 |
2.91e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 112.88 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP- 1163
Cdd:PRK13642 12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPd 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1164 -VLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK13642 92 nQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-------EPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1243 DEATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
770-1007 |
4.33e-27 |
|
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: 112.73 E-value: 4.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 770 PLYAFLFSQILGTFSIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDd 849
Cdd:cd18780 16 PYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFD- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 850 lRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRD 929
Cdd:cd18780 95 -VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 930 KQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFcfaFAQCIMFIANSA---SYRYGGYL 1006
Cdd:cd18780 174 QDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGG---FNGFMGAAAQLAivlVLWYGGRL 250
|
.
gi 21536378 1007 I 1007
Cdd:cd18780 251 V 251
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1086-1303 |
4.44e-27 |
|
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: 111.12 E-value: 4.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVNVQFLRSNIGIVSQE 1162
Cdd:cd03256 9 TYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinkLKGKALRQLRRQIGMIFQQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 PVLFA-CSIMDNIKYGdNTKEIPMERVIA-----AAKQAQLH--DFVmSLPEKYETNVgsqgSQLSRGEKQRIAIARAIV 1234
Cdd:cd03256 87 FNLIErLSVLENVLSG-RLGRRSTWRSLFglfpkEEKQRALAalERV-GLLDKAYQRA----DQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1235 RDPKILLLDEATSALDTESEKTV-QVALDKARE-GRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVmDLLKRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGPPAEL 232
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1090-1306 |
4.73e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.52 E-value: 4.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1090 RPDSQV--LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN---VQFLRSNIGIVSQEPv 1164
Cdd:PRK11308 23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 lFAcSIMDNIKYGD--------NTKEIPMERviaAAKQAQLHDFVMSLPEKYetnvGSQGSQLSRGEKQRIAIARAIVRD 1236
Cdd:PRK11308 102 -YG-SLNPRKKVGQileeplliNTSLSAAER---REKALAMMAKVGLRPEHY----DRYPHMFSGGQRQRIAIARALMLD 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1237 PKILLLDEATSALDTESEKTV-QVALDKAREGRTCIV-IAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:PRK11308 173 PDVVVADEPVSALDVSVQAQVlNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1096-1306 |
7.38e-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: 116.71 E-value: 7.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFyDPDQGKVMIDGHD----SKKVNvQFLRSNIGIVSQEPvlFAC--- 1168
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDldglSRRAL-RPLRRRMQVVFQDP--FGSlsp 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 --SIMDNIKYGDNTKEIPM------ERVIAAAKQAQLHDFVMslpEKYETnvgsqgsQLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:COG4172 378 rmTVGQIIAEGLRVHGPGLsaaerrARVAEALEEVGLDPAAR---HRYPH-------EFSGGQRQRIAIARALILEPKLL 447
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1241 LLDEATSALDteseKTVQ---VALDK---AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:COG4172 448 VLDEPTSALD----VSVQaqiLDLLRdlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1086-1303 |
1.82e-26 |
|
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: 108.75 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRPdSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVL 1165
Cdd:cd03263 9 TYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 F-ACSIMDNIKY-----GDNTKEIPMErviaaakQAQLHDfVMSLPEKYETNVGsqgsQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd03263 87 FdELTVREHLRFyarlkGLPKSEIKEE-------VELLLR-VLGLTDKANKRAR----TLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 1303
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
420-646 |
2.63e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 109.03 E-value: 2.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR--SLNIQWLRDQ 497
Cdd:PRK09493 2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFSTTIA-ENIRYG--------REDA-----TMEDIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsggq 563
Cdd:PRK09493 79 AGMVFQQFYLFPHLTAlENVMFGplrvrgasKEEAekqarELLAKVGLAERAHHYPSELSGGQQ---------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 564 kQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQ----HGHTIISVAHRLSTVR-AADTIIGFEHGTAVERG 638
Cdd:PRK09493 143 -QRVAIARALAVKPKLMLFDEPTSALDPE---LRHEVLKVMQdlaeEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDG 218
|
....*...
gi 21536378 639 THEELLER 646
Cdd:PRK09493 219 DPQVLIKN 226
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
148-376 |
2.75e-26 |
|
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: 110.48 E-value: 2.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 148 IAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIqRMTST 227
Cdd:cd18784 45 LAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFL-RSLVK 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 228 ICGFLLGFFR-GWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK 306
Cdd:cd18784 124 AIGVIVFMFKlSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSE 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 307 NLVFAQRWGIRKGIVMGfftGFVWCLIFLCYALA---FWYGSTLVLdEGEYTPGTLVqiflSVIVGALNLGNA 376
Cdd:cd18784 204 KLKDTYKLKIKEALAYG---GYVWSNELTELALTvstLYYGGHLVI-TGQISGGNLI----SFILYQLELGSC 268
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1085-1306 |
3.06e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 109.02 E-value: 3.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqflRSNIGIVSQEPV 1164
Cdd:COG1121 14 VSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVPQRAE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 L---FACSIMDNIKYGdNTKEIPM---------ERVIAAAKQAQLHDFVmslpekyetnvGSQGSQLSRGEKQRIAIARA 1232
Cdd:COG1121 86 VdwdFPITVRDVVLMG-RYGRRGLfrrpsradrEAVDEALERVGLEDLA-----------DRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1233 IVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEkGTHEELMAQ 1306
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLLNRGLVAH-GPPEEVLTP 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1085-1319 |
3.55e-26 |
|
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: 117.35 E-value: 3.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYpSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflrsNIGIVSQEPV 1164
Cdd:TIGR00957 644 FTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:TIGR00957 710 IQNDSLRENILFGKALNEKYYQQVLEAC--ALLPDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1245 ATSALDTESEKTV---QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKLVTTGSP 1319
Cdd:TIGR00957 787 PLSAVDAHVGKHIfehVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAP 864
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1089-1306 |
3.56e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 110.98 E-value: 3.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQV--LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD----SKKVNVQfLRSNIGIVSQE 1162
Cdd:COG4608 25 GRTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitglSGRELRP-LRRRMQMVFQD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 PvlFAC-----SIMDNIK-----YGDNTKEIPMERViaaakqAQLHDFVMSLPEKYETNVGsqgsQLSRGEKQRIAIARA 1232
Cdd:COG4608 104 P--YASlnprmTVGDIIAeplriHGLASKAERRERV------AELLELVGLRPEHADRYPH----EFSGGQRQRIGIARA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1233 IVRDPKILLLDEATSALDteseKTVQ---VAL--D-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:COG4608 172 LALNPKLIVCDEPVSALD----VSIQaqvLNLleDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYA 247
|
.
gi 21536378 1306 Q 1306
Cdd:COG4608 248 R 248
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
419-619 |
3.63e-26 |
|
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: 107.25 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 419 EIEFHNVTF---HYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI--QRFYDPCEGMVTVDGHDIRslnIQW 493
Cdd:cd03213 3 TLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 494 LRDQIGIVEQEPVLFST-TIAENIRYgredatmedivqAAK-------EAnaynfimdlpqqfdtlvgegggqmsggqkQ 565
Cdd:cd03213 80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAKlrglsggER-----------------------------K 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 566 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLST 619
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLaDTGRTIICSIHQPSS 173
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1091-1295 |
4.22e-26 |
|
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: 105.97 E-value: 4.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflrsnigivsqEPVLFAcSI 1170
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG--------------------KEVSFA-SP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYGdntkeipmervIAaakqaqlhdFVMslpekyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSAL- 1249
Cdd:cd03216 70 RDARRAG-----------IA---------MVY---------------QLSVGERQMVEIARALARNARLLILDEPTAALt 114
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536378 1250 DTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVI 1295
Cdd:cd03216 115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1078-1315 |
5.54e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.05 E-value: 5.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEP--VLFACSIMDNIKYGD-----NTKEIpMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIA 1230
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPvnmglDKDEV-ERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1231 RAIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKG-----THEEL 1303
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDI 230
|
250
....*....|..
gi 21536378 1304 MAQKGAYYKLVT 1315
Cdd:PRK13647 231 VEQAGLRLPLVA 242
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1094-1298 |
8.29e-26 |
|
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: 107.07 E-value: 8.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPVLFA-CSIMD 1172
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKY--------GDNTKEipmeRVIAAAKQAQLHDFVmslpekyETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:cd03266 98 NLEYfaglyglkGDELTA----RLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIARALVHDPPVLLLDE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1245 ATSALDTESEKTVQVALDKAREGRTCIVIA-HRLSTIQN-ADIIAVMAQGVVIEKG 1298
Cdd:cd03266 163 PTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
789-1013 |
8.43e-26 |
|
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: 108.78 E-value: 8.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 789 EEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQV 868
Cdd:cd18572 29 DGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 869 qgaaGSQIGMIVNSFTN----VTVAMIIAFSFSWKLSLVILCFFPFLALS----GATQTRMltgfASRDKQALEMVGQIT 940
Cdd:cd18572 107 ----SDPLSTNLNVFLRnlvqLVGGLAFMFSLSWRLTLLAFITVPVIALItkvyGRYYRKL----SKEIQDALAEANQVA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 941 NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLH 1013
Cdd:cd18572 179 EEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMS 251
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1082-1292 |
9.48e-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: 106.19 E-value: 9.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1082 DCKFTYpsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNVQFLRSNIGIVSQ 1161
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1162 EP--VLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1240 LLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQG 1292
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVgELIRELAAQGKAVIVITHDYEFLAKvCDRVLLLANG 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1096-1306 |
1.06e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.89 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKVMIDGHDSKKVNVQFLRS---NIGIVSQEPVLFAC- 1168
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQHFNLLSSr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNIKygdntkeIPMErvIAAAKQAQLHDFVMSLPE---------KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:PRK11153 98 TVFDNVA-------LPLE--LAGTPKAEIKARVTELLElvglsdkadRYP-------AQLSGGQKQRVAIARALASNPKV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1240 LLLDEATSALDTEsekTVQVALDKARE-----GRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:PRK11153 162 LLCDEATSALDPA---TTRSILELLKDinrelGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGTVSEVFSH 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
438-646 |
1.11e-25 |
|
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: 107.04 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIGIVEQEPVLF-STTIAENI 516
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 517 RYGREdatMEDIVQAAKEANAYNFIMDLpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAM 596
Cdd:cd03299 93 AYGLK---KRKVDKKEIERKVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 597 VQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 646
Cdd:cd03299 168 LREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1105-1298 |
1.20e-25 |
|
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: 106.23 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1105 PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG---HDS-KKVNVQFLRSNIGIVSQEPVLFA-CSIMDNIKYGDN 1179
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSrKKINLPPQQRKIGLVFQQYALFPhLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1180 TKEiPMERVIAAAKQAQLHDfVMSLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQV 1259
Cdd:cd03297 102 RKR-NREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536378 1260 ALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 1298
Cdd:cd03297 173 ELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1089-1288 |
1.36e-25 |
|
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: 106.02 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFlRSNIGIVSQEPVLF-A 1167
Cdd:COG4133 11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIK-----YGDntkEIPMERVIAAAKQAQLHDFvMSLPekyetnvgsqGSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:COG4133 90 LTVRENLRfwaalYGL---RADREAIDEALEAVGLAGL-ADLP----------VRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536378 1243 DEATSALDTESEKTVQVALDKAREGRTCIVIA-HRLSTIQNADIIAV 1288
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1092-1304 |
1.57e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.17 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PD---QGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1164
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNiySPRTDTVDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFACSIMDNIKYG-----DNTKEIPMERVIAAAKQAQLHDFVMSlpEKYETNVGsqgsqLSRGEKQRIAIARAIVRDPKI 1239
Cdd:PRK14239 97 PFPMSIYENVVYGlrlkgIKDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIARVLATSPKI 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRL---STIqnADIIAVMAQGVVIEKG-THEELM 1304
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNdTKQMFM 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1100-1306 |
1.59e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 106.38 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1100 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnvqFLRSNIG-----IVSQEPVLFA-CSIMDN 1173
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-------LTALPPAerpvsMLFQENNLFPhLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1174 I--------KYGDNTKEipmeRVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:COG3840 92 IglglrpglKLTAEQRA----QVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1246 TSALDTesektvqvAL---------DKARE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:COG3840 157 FSALDP--------ALrqemldlvdELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1078-1307 |
1.79e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.47 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL--RSN 1155
Cdd:PRK13639 2 LETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1156 IGIVSQEP--VLFACSIMDNIKYGDNTKEIPME----RVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAI 1229
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLNLGLSKEevekRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1230 ARAIVRDPKILLLDEATSALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTIQ-NADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1092-1304 |
1.87e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.72 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLFA-C 1168
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvnDPKVDERLIRQEAGMVFQQFYLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNIKYGdntkeiPMeRVIAAAKqAQLHDFVMSLPEK--YETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:PRK09493 93 TALENVMFG------PL-RVRGASK-EEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1247 SALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELM 1304
Cdd:PRK09493 165 SALDPELRHEVlKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
420-646 |
3.63e-25 |
|
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: 105.40 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrsLNIQWLRDQIG 499
Cdd:cd03300 1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFS-TTIAENIRYG------------REDATMEDIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsggqkQR 566
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGlrlkklpkaeikERVAEALDLVQLEGYANRKPSQLSGGQQ-----------------QR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 567 VAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 643
Cdd:cd03300 139 VAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218
|
...
gi 21536378 644 LER 646
Cdd:cd03300 219 YEE 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
420-645 |
4.41e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.37 E-value: 4.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEP--VLFSTTIAENIRYGREDAT-----MEDIV-QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIAR 571
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAvpydeMHRRVsEALKQVDMLERADYEPNALS-----------GGQKQRVAIAG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 572 ALIRNPKILLLDMATSALDNESEA----MVQEVlsKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLE 645
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFD 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
420-639 |
5.44e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 107.96 E-value: 5.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYP-SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---R 495
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 496 DQIGIVEQE-PVLFSTTIAENIRYGREDATME------------DIVQAAKEANAYnfimdlPQQFdtlvgegggqmSGG 562
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVALPLELAGTPkaeikarvtellELVGLSDKADRY------PAQL-----------SGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 563 QKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGT 639
Cdd:PRK11153 145 QKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
438-645 |
7.92e-25 |
|
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: 105.42 E-value: 7.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL----RDQIGIVEQEPVLF-STTI 512
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 513 AENIRYG----------REDATMEDIVQAAKEANAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKI 579
Cdd:cd03294 120 LENVAFGlevqgvpraeREERAAEALELVGLEGWEHKYPDELSggmQQ------------------RVGLARALAVDPDI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLE 645
Cdd:cd03294 182 LLMDEAFSALDPLIRREMQDELLRLQaeLQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
420-646 |
8.08e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 104.45 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkiLNdLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlrDQ-- 497
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFS-TTIAENI--------RYGREDAtmEDIVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsg 561
Cdd:COG3840 73 VSMLFQENNLFPhLTVAQNIglglrpglKLTAEQR--AQVEQALERVGLAGLLDRLPgqlsggqRQ-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 562 gqkqRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSkiQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVE 636
Cdd:COG3840 137 ----RVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAaRIADRVLLVADGRIAA 210
|
250
....*....|
gi 21536378 637 RGTHEELLER 646
Cdd:COG3840 211 DGPTAALLDG 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
419-646 |
8.54e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 107.54 E-value: 8.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 419 EIEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniqWL--RD 496
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLppRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 -QIGIVEQEPVLF-STTIAENIRYG-----------REDAtME--DIVQAAKEANAYnfimdlP-------QQfdtlvge 554
Cdd:COG1118 75 rRVGFVFQHYALFpHMTVAENIAFGlrvrppskaeiRARV-EEllELVQLEGLADRY------PsqlsggqRQ------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 555 gggqmsggqkqRVAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSKIqhGHTIISVAH-RLSTVRAADTIIGF 629
Cdd:COG1118 141 -----------RVALARALAVEPEVLLLDEPFGALDakvrKELRRWLRRLHDEL--GGTTVFVTHdQEEALELADRVVVM 207
|
250
....*....|....*..
gi 21536378 630 EHGTAVERGTHEELLER 646
Cdd:COG1118 208 NQGRIEQVGTPDEVYDR 224
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
752-1307 |
1.20e-24 |
|
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: 112.31 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 752 WPYMLVGSV--GAAVNGTVTPLyafLFSQILGTFSiPDKEEQRSQIN----GVCLLFVAMgcvslfTQFLQGYAFAKSGE 825
Cdd:TIGR01271 80 WRFVFYGILlyFGEATKAVQPL---LLGRIIASYD-PFNAPEREIAYylalGLCLLFIVR------TLLLHPAIFGLHHL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 826 LLTKRLRKFG--FRAMLGQDIAWFDDLrnSPGALTTRLATDASQVQGaagsqiGMIVNSFTNVT-VAMIIAFSFSWKL-- 900
Cdd:TIGR01271 150 GMQMRIALFSliYKKTLKLSSRVLDKI--STGQLVSLLSNNLNKFDE------GLALAHFVWIApLQVILLMGLIWELle 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 901 --SLVILCFFPFLALSGATQTRMLTGFasRDKQAlEMVGQ---ITNEALSNIRTVAGIGKErrfiEALETELEKPFKTAI 975
Cdd:TIGR01271 222 vnGFCGLGFLILLALFQACLGQKMMPY--RDKRA-GKISErlaITSEIIENIQSVKAYCWE----EAMEKIIKNIRQDEL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 976 QKANIYGFCFAFaqcimfiaNSASYRYGGYLIS---------NEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKI 1046
Cdd:TIGR01271 295 KLTRKIAYLRYF--------YSSAFFFSGFFVVflsvvpyalIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSL 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1047 SAARFFQ-LLDRQPPISV-YN-TAGE--------KWDNFQGKIdFVDCK----------------FTYPSRPDSQVLNGL 1099
Cdd:TIGR01271 367 GAITKIQdFLCKEEYKTLeYNlTTTEvemvnvtaSWDEGIGEL-FEKIKqnnkarkqpngddglfFSNFSLYVTPVLKNI 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1100 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrsnIGIVSQEPVLFACSIMDNIKYGDN 1179
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGLS 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1180 TKEIPMERVIAAAkqaQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-Q 1258
Cdd:TIGR01271 513 YDEYRYTSVIKAC---QLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfE 589
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 21536378 1259 VALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:TIGR01271 590 SCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1094-1305 |
1.51e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.06 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERfydPDQGKV-----MIDGHDS---KKVNVQFLRSNIGIVSQE 1162
Cdd:PRK11264 17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTllrCINLLEQ---PEAGTIrvgdiTIDTARSlsqQKGLIRQLRQHVGFVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 PVLFAC-SIMDNIKYGDN-TKEIPMERVIAAAKQaqlhdfvmsLPEKyetnVGSQGSQ------LSRGEKQRIAIARAIV 1234
Cdd:PRK11264 94 FNLFPHrTVLENIIEGPViVKGEPKEEATARARE---------LLAK----VGLAGKEtsyprrLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1235 RDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
420-642 |
1.53e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.13 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI--RSLNIQWLR 495
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 496 DQIGIVEQEP--VLFSTTIAENIRYGREDATMED--IVQAAKEAnaynfiMDLPQ-QFDTLVGEGGGQMSGGQKQRVAIA 570
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEeeIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 571 RALIRNPKILLLDMATSALDNESEamvQEVLSKIQHGH-----TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 642
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGR---DEILNKIKELHkeynmTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1079-1306 |
2.08e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 106.34 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1079 DFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGI 1158
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1159 VSQEPVLFA-CSIMDNIKYGDNTKEIPMERVIAAAKQA-QLHDFVmSLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRD 1236
Cdd:PRK11432 83 VFQSYALFPhMSLGENVGYGLKMLGVPKEERKQRVKEAlELVDLA-GFEDRYV-------DQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1237 PKILLLDEATSALDTESEKTVQvalDKARE-----GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMR---EKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
774-1009 |
2.24e-24 |
|
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: 104.90 E-value: 2.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 774 FLFSQILGTFS--IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlR 851
Cdd:cd18573 17 FAIGKLIDVASkeSGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD--K 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 852 NSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQ 931
Cdd:cd18573 95 NKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 932 ALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQcimFIANSASYR---YGGYLIS 1008
Cdd:cd18573 175 ALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTG---FSGNLSLLSvlyYGGSLVA 251
|
.
gi 21536378 1009 N 1009
Cdd:cd18573 252 S 252
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1094-1298 |
2.44e-24 |
|
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: 102.30 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdSKKVNVQFLRSNIGIVSQEPVLF-ACSIMD 1172
Cdd:cd03268 14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG--KSYQKNIEALRRIGALIEAPGFYpNLTARE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKYGDNTKEIPMERViaaakqAQLHDFV-MSLPEKYETnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDT 1251
Cdd:cd03268 92 NLRLLARLLGIRKKRI------DEVLDVVgLKDSAKKKV------KGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536378 1252 ESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 1298
Cdd:cd03268 160 DGIKELrELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1093-1301 |
2.83e-24 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 2.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1093 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---SKKVN---VQFLRSNIGIVSQE---- 1162
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdfSKTPSdkaIRELRRNVGMVFQQynlw 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 PVLfacSIMDN-----IKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK11124 95 PHL---TVQQNlieapCRVLGLSKDQALARAEKLLERLRLKPYADRFPL-----------HLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1238 KILLLDEATSALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHE 1301
Cdd:PRK11124 161 QVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1078-1303 |
3.50e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 103.68 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIG 1157
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPV-LFACSIMD-NIKYGDNTKEIPMERVIAAAKQAqLHDFVMSLPEKYETNvgsqgsQLSRGEKQRIAIARAIVR 1235
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1236 DPKILLLDEATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1092-1302 |
3.53e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.97 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEP--VLFA 1167
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDIRKKVGLVFQYPeyQLFE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIKYGD-----NTKEIpMERVIAAAKQAQLhdfvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK13637 99 ETIEKDIAFGPinlglSEEEI-ENRVKRAMNIVGL---------DYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1243 DEATSALDTESEKTV--QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEE 1302
Cdd:PRK13637 169 DEPTAGLDPKGRDEIlnKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
420-646 |
3.88e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 104.11 E-value: 3.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQWLRD 496
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEP--VLFSTTIAENIRYGRED-----ATMEDIV-QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVA 568
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENravprPEMIKIVrDVLADVGMLDYIDSEPANLS-----------GGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 569 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 646
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
419-651 |
5.19e-24 |
|
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: 102.42 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 419 EIEFHNVTFHYPSRPEvkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQI 498
Cdd:cd03296 2 SIEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFS-TTIAENIRYGREdatMEDIVQAAKEANAYNFIMDLPQ--QFDTLVGEGGGQMSGGQKQRVAIARALIR 575
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGLR---VKPRSERPPEAEIRAKVHELLKlvQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 576 NPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLERKGVYF 651
Cdd:cd03296 154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1100-1304 |
5.67e-24 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 106.27 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1100 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRS----NIGIVSQEPVLFA-CSIMDNI 1174
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1175 KYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:PRK10070 128 AFGMELAGINaeerREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1251 TESEKTVQVALDK--AREGRTCIVIAHRL-STIQNADIIAVMAQGVVIEKGTHEELM 1304
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1077-1307 |
5.73e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.71 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1077 KIDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG----HDSKKVNVQ 1150
Cdd:PRK13646 2 TIRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1151 FLRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERVIAAAkqaqlHDFVMSLpeKYETNVGSQGS-QLSRGEKQRI 1227
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDL--GFSRDVMSQSPfQMSGGQMRKI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1228 AIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAR--EGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELM 1304
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELF 234
|
...
gi 21536378 1305 AQK 1307
Cdd:PRK13646 235 KDK 237
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
436-641 |
8.61e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 101.33 E-value: 8.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFSTTIAEN 515
Cdd:PRK10247 21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 516 IRYGREdatmedIVQAAKEANAynFIMDLpQQF---DTLVGEGGGQMSGGQKQRVaiarALIRN----PKILLLDMATSA 588
Cdd:PRK10247 101 LIFPWQ------IRNQQPDPAI--FLDDL-ERFalpDTILTKNIAELSGGEKQRI----SLIRNlqfmPKVLLLDEITSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 589 LDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFE-HGTAVERGTHE 641
Cdd:PRK10247 168 LDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQpHAGEMQEARYE 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
420-645 |
8.63e-24 |
|
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: 100.97 E-value: 8.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN-IQWLRDQI 498
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFST-TIAENIRYGREDATMEDIvqAAKEANAYNFIMDLP--------------QQFdtlvgegggqmsggq 563
Cdd:cd03224 78 GYVPEGRRIFPElTVEENLLLGAYARRRAKR--KARLERVYELFPRLKerrkqlagtlsggeQQM--------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 564 kqrVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 638
Cdd:cd03224 141 ---LAIARALMSRPKLLLLDEPSEGL---APKIVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGRVVLEG 214
|
....*..
gi 21536378 639 THEELLE 645
Cdd:cd03224 215 TAAELLA 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1090-1281 |
9.37e-24 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 107.59 E-value: 9.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1090 RPDSQVL-NGLSVSISPGQTLAFVGSSGCGKST--------------SIQLlerfydPDQGKVMidghdskkvnvqFLrs 1154
Cdd:COG4178 372 TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTllraiaglwpygsgRIAR------PAGARVL------------FL-- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 nigivSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEkyetnVGSQGSQLSRGEKQRIAIARAIV 1234
Cdd:COG4178 432 -----PQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQRLAFARLLL 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536378 1235 RDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQ 1281
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAA 548
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1085-1298 |
1.09e-23 |
|
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: 100.35 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRpdsQVLNGLSVSISPGQTlAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIGIVSQEPV 1164
Cdd:cd03264 8 KRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFA-CSIMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFvmslpekYETNVGSqgsqLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd03264 83 VYPnFTVREFLDYIAWLKGIPskevKARVDEVLELVNLGDR-------AKKKIGS----LSGGMRRRVGIAQALVGDPSI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 1298
Cdd:cd03264 152 LIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
420-626 |
1.33e-23 |
|
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: 100.25 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlRDQIG 499
Cdd:COG4133 3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIR-----YGReDATMEDIVQAAKEanaynfiMDLPQQFDTLVGEgggqmsggqkqRVAIARAL 573
Cdd:COG4133 79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVRQlsag----qkrRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAHRLSTVRAADTI 626
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
418-615 |
1.44e-23 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 104.00 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDq 497
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK-DRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLF-STTIAENIRYG----REDAtmEDIVQAAKEANAynfIMDL-------P-------QQfdtlvgegggq 558
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklrKVPK--AEIDRRVREAAE---LLGLedlldrkPkqlsggqRQ----------- 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 559 msggqkqRVAIARALIRNPKILLLDMATSALDNES-EAMVQEvLSKIQH--GHTIISVAH 615
Cdd:COG3839 141 -------RVALGRALVREPKVFLLDEPLSNLDAKLrVEMRAE-IKRLHRrlGTTTIYVTH 192
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1075-1303 |
1.56e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 101.14 E-value: 1.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1075 QGKIDFVDCKFTYPsrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD--PD---QGKVMIDGHDSKKVNV 1149
Cdd:PRK14247 1 MNKIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1150 QFLRSNIGIVSQEP-VLFACSIMDNIKYG-------DNTKEIpMERVIAAAKQAQLHDFVmslpekyETNVGSQGSQLSR 1221
Cdd:PRK14247 78 IELRRRVQMVFQIPnPIPNLSIFENVALGlklnrlvKSKKEL-QERVRWALEKAQLWDEV-------KDRLDAPAGKLSG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1222 GEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAH------RLStiqnaDIIAVMAQGVVI 1295
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIV 224
|
....*...
gi 21536378 1296 EKGTHEEL 1303
Cdd:PRK14247 225 EWGPTREV 232
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1093-1307 |
1.69e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1093 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEP--VLFAC 1168
Cdd:PRK13636 19 THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESVGMVFQDPdnQLFSA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:PRK13636 99 SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1249 LDTES-EKTVQVALDKARE-GRTCIVIAHRLSTIQ-NADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:PRK13636 172 LDPMGvSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
420-644 |
2.03e-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: 100.93 E-value: 2.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGM-VTVDGHDIRSLNIQWLRDQI 498
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVeqepvlfSTTIAENIrygREDATMEDIV-------------------QAAKEanaynfIMDL-------PQQFDTLv 552
Cdd:COG1119 81 GLV-------SPALQLRF---PRDETVLDVVlsgffdsiglyreptdeqrERARE------LLELlglahlaDRPFGTL- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 553 gegggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLStvraaDTIIGFE 630
Cdd:COG1119 144 -------SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVE-----EIPPGIT 211
|
250 260
....*....|....*....|
gi 21536378 631 H------GTAVERGTHEELL 644
Cdd:COG1119 212 HvlllkdGRVVAAGPKEEVL 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
420-646 |
2.29e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 101.73 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAIAR 571
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIphEEMKERVNEAlelvGMQDFKEREPARL-----------SGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 572 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLER 646
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIrdDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1092-1303 |
2.57e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.89 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF---YDPD---QGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL 1165
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 FA-CSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDfvMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK14246 102 FPhLSIYDNIAYPLKSHGIKEKREIKKIVEECLRK--VGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1245 ATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1094-1303 |
2.89e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 2.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQF------LRSNIGIVSQEPVLFA 1167
Cdd:COG1129 18 KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEP-----VRFrsprdaQAAGIAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 C-SIMDNIKYGDNTKE---IPMERVIAAAKQAqLHDFVMSLPEkyETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:COG1129 93 NlSVAENIFLGREPRRgglIDWRAMRRRAREL-LARLGLDIDP--DTPVGD----LSVAQQQLVEIARALSRDARVLILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1244 EATSAL-DTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 1303
Cdd:COG1129 166 EPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
420-626 |
3.65e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 105.10 E-value: 3.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ-I 498
Cdd:COG1129 5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFST-TIAENIRYGRE--------DATMEDivQAAKEANAYNF-------IMDLP---QQFdtlvgegggqm 559
Cdd:COG1129 82 AIIHQELNLVPNlSVAENIFLGREprrgglidWRAMRR--RARELLARLGLdidpdtpVGDLSvaqQQL----------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 560 sggqkqrVAIARALIRNPKILLLDMATSALdNESEAmvqEVLSKI-----QHGHTIISVAHRLSTVRA-ADTI 626
Cdd:COG1129 149 -------VEIARALSRDARVLILDEPTASL-TEREV---ERLFRIirrlkAQGVAIIYISHRLDEVFEiADRV 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1096-1277 |
4.35e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 100.24 E-value: 4.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-----PDQGKVMIDGHD--SKKVNVQFLRSNIGIVSQEPVLFAC 1168
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNIKYGD--NTKEIPM-ERVIAAAKQAQLHDFVmslPEKYETNvgsqGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMdELVERSLRQAALWDEV---KDKLKQS----GLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190
....*....|....*....|....*....|..
gi 21536378 1246 TSALDTESEKTVQVALDKAREGRTCIVIAHRL 1277
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1099-1299 |
4.56e-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: 98.72 E-value: 4.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1099 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDNIKYG 1177
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1178 DNT----KEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDT-- 1251
Cdd:cd03298 95 LSPglklTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPal 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536378 1252 ESEKTVQVALDKAREGRTCIVIAHrlstiQNADIIAVMAQGVVIEKGT 1299
Cdd:cd03298 164 RAEMLDLVLDLHAETKMTVLMVTH-----QPEDAKRLAQRVVFLDNGR 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1092-1301 |
5.21e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 99.02 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIM 1171
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 DNIKYgdnTKEIPMERVIAAAKQAQLHDFvmSLPEK-YETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:PRK10247 99 DNLIF---PWQIRNQQPDPAIFLDDLERF--ALPDTiLTKNI----AELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1251 TESEKTVQVALDK-AREGRTCIV-IAHRLSTIQNAD-IIAVMAQGVVIEKGTHE 1301
Cdd:PRK10247 170 ESNKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADkVITLQPHAGEMQEARYE 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
420-633 |
6.09e-23 |
|
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: 98.31 E-value: 6.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEV--KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHdirslniqwlrdq 497
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFSTTIAENIRYGRE-DATM-EDIVQA-AKEAnaynfimDLpQQFD----TLVGEGGGQMSGGQKQRVAIA 570
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfDEERyEKVIKAcALEP-------DL-EILPdgdlTEIGEKGINLSGGQKQRISLA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 571 RALIRNPKILLLDMATSALDNESEAMVQE--VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 633
Cdd:cd03250 140 RAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1078-1303 |
6.51e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 100.26 E-value: 6.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFLRS 1154
Cdd:PRK13640 6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1155 NIGIVSQEP--VLFACSIMDNIKYGDNTKEIP---MERVIA-AAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIA 1228
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPrpeMIKIVRdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1229 IARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1092-1298 |
7.56e-23 |
|
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: 98.12 E-value: 7.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvNVQFL-RSNIGIVSQEPVLF-ACS 1169
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-----PLDIAaRNRIGYLPEERGLYpKMK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYGDNTKEIPMErviAAAKQAQ--LHDFvmSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:cd03269 87 VIDQLVYLAQLKGLKKE---EARRRIDewLERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1248 ALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 1298
Cdd:cd03269 158 GLDPVNVELLkDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1092-1303 |
8.00e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 8.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvQFLRSnIGIVSQEPVLFA-CS 1169
Cdd:PRK11607 30 DGQhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-INMMFQSYALFPhMT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYGDNTKEIP----MERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:PRK11607 108 VEQNIAFGLKQDKLPkaeiASRVNEMLGLVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1246 TSALDTESEKTVQVALDK--AREGRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
437-644 |
1.02e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 99.05 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI---RSLN-----IQWLRDQIGIVEQEPVLF 508
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 S-TTIAENIRYG--------REDAT------MEDIVQAAKEaNAYNFIMDLPQQfdtlvgegggqmsggqkQRVAIARAL 573
Cdd:PRK11264 98 PhRTVLENIIEGpvivkgepKEEATararelLAKVGLAGKE-TSYPRRLSGGQQ-----------------QRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 574 IRNPKILLLDMATSALDNEseaMVQEVLSKI----QHGHTIISVAHRLSTVR-AADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPE---LVGEVLNTIrqlaQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALF 232
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
148-365 |
1.22e-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: 99.81 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 148 IAVAVL--ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 225
Cdd:cd18542 46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 226 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSK-FTDYElKAYAKAGVVADEVISSMRTVAAFGGEKREVERY 304
Cdd:cd18542 126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPaFEEIR-EQEGELNTVLQENLTGVRVVKAFAREDYEIEKF 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 305 EK-NLVFAQRWgIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQiFLS 365
Cdd:cd18542 205 DKeNEEYRDLN-IKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVIN-GEITLGELVA-FIS 263
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
420-646 |
1.61e-22 |
|
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: 100.13 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPC---EGMVTVDGHDIRSLN---IQ 492
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 493 WLR-DQIGIVEQEPvlFS---------TTIAENIRY----GREDAT------MED--IVQAAKEANAYnfimdlPQQFdt 550
Cdd:COG0444 82 KIRgREIQMIFQDP--MTslnpvmtvgDQIAEPLRIhgglSKAEAReraielLERvgLPDPERRLDRY------PHELsg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 551 lvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTII 627
Cdd:COG0444 154 g-----------mrqRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQreLGLAILFITHDLGVVAEiADRVA 222
|
250
....*....|....*....
gi 21536378 628 GFEHGTAVERGTHEELLER 646
Cdd:COG0444 223 VMYAGRIVEEGPVEELFEN 241
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
420-674 |
1.62e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEP--VLFSTTIAENIRYG------REDATMEDIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAIAR 571
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPYHL-----------SYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 572 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERG-----THEELL 644
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250 260 270
....*....|....*....|....*....|....*
gi 21536378 645 ERKGVYFTLVT-----LQSQGNQALnEEDIKDATE 674
Cdd:PRK13647 232 EQAGLRLPLVAqifedLPELGQSKL-PLTVKEAVQ 265
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1078-1298 |
1.85e-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: 96.47 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPDS---QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGKVMIDGHDSKKVNvqfL 1152
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRS---F 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1153 RSNIGIVSQEPVLFAC-SIMDNIKYgdntkeipmerviaaakQAQLhdfvmslpekyetnvgsqgSQLSRGEKQRIAIAR 1231
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF-----------------AAKL-------------------RGLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1232 AIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLST--IQNADIIAVMAQGVVIEKG 1298
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
148-393 |
2.11e-22 |
|
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: 99.03 E-value: 2.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 148 IAVAVL--ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 225
Cdd:cd18552 46 IGLFLLrgLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 226 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY- 304
Cdd:cd18552 126 TVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFr 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 305 ---EKNLVFAQRWGIRKGI---VMGFFTGFVwclIflcyALAFWYGSTLVLDeGEYTPGTlvqiFLSVIVGAL------- 371
Cdd:cd18552 206 kanERLRRLSMKIARARALsspLMELLGAIA---I----ALVLWYGGYQVIS-GELTPGE----FISFITALLllyqpik 273
|
250 260
....*....|....*....|..
gi 21536378 372 NLGNASpclEAFATGRAAATSI 393
Cdd:cd18552 274 RLSNVN---ANLQRGLAAAERI 292
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
437-646 |
2.29e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.18 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlRDqIGIVEQEPVLFS-TTIAEN 515
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-RD-ICMVFQSYALFPhMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 516 IRYG--REDATMEDIVQAAKEANAynfIMDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALD-NE 592
Cdd:PRK11432 99 VGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYV----DQISGGQQQRVALARALILKPKVLLFDEPLSNLDaNL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 593 SEAMvQEVLSKIQHGHTIIS--VAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 646
Cdd:PRK11432 172 RRSM-REKIRELQQQFNITSlyVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
420-646 |
2.36e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.55 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYP--SRPEVKilnDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ 497
Cdd:PRK13635 6 IRVEHISFRYPdaATYALK---DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEP--VLFSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 569
Cdd:PRK13635 83 VGMVFQNPdnQFVGATVQDDVAFGLEnigvprEEMVERVDQALRQVGMEDFLNREPHRL-----------SGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEamvQEVLSKI-----QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGR---REVLETVrqlkeQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228
|
..
gi 21536378 645 ER 646
Cdd:PRK13635 229 KS 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1093-1303 |
2.54e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1093 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIM 1171
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRhMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 DNIKYGdnTKEIPM-ERVIAAA---KQAQLHDFVM--SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:PRK10851 93 DNIAFG--LTVLPRrERPNAAAikaKVTQLLEMVQlaHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1246 TSALDTESEKTVQVALDKARE--GRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1085-1280 |
2.71e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 98.19 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD-----QGKVMIDGHD--SKKVNVQFLRSNIG 1157
Cdd:PRK14258 15 FYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNiyERRVNLNRLRRQVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFACSIMDNIKYGDNT----KEIPMERVIAAA-KQAQLHDFVmslpekyETNVGSQGSQLSRGEKQRIAIARA 1232
Cdd:PRK14258 92 MVHPKPNLFPMSVYDNVAYGVKIvgwrPKLEIDDIVESAlKDADLWDEI-------KHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536378 1233 IVRDPKILLLDEATSALDTESEKTVQ--VALDKAREGRTCIVIAHRLSTI 1280
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVEslIQSLRLRSELTMVIVSHNLHQV 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1092-1303 |
3.74e-22 |
|
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: 96.28 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD----SKKVnvqflRSNIGIVSQEPVLfa 1167
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvrePREV-----RRRIGIVFQDLSV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 csimDNIKYGDNTKEI-----PMERVIAAAKQAQLHDFvMSLPEKYETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:cd03265 85 ----DDELTGWENLYIharlyGVPGAERRERIDELLDF-VGLLEAADRLVKT----YSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1243 DEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1092-1305 |
4.17e-22 |
|
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: 96.35 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CS 1169
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDiTGLPPHERARAGIGYVPEGRRIFPeLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYGdntkeipMERVIAAAKQAQLhDFVMSL-PEKYEtNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:cd03224 92 VEENLLLG-------AYARRRAKRKARL-ERVYELfPRLKE-RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1249 LdteSEKTVQV---ALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:cd03224 163 L---APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
420-644 |
4.56e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 97.86 E-value: 4.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEP--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIAR 571
Cdd:PRK13642 85 MVFQNPdnQFVGATVEDDVAFGMENQGIprEEMIKRVDEAllavNMLDFKTREPARLS-----------GGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 572 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK13642 154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1094-1296 |
5.36e-22 |
|
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: 97.18 E-value: 5.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----------VQFL----------R 1153
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqrrafrrdVQLVfqdspsavnpR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1154 SNIGIVSQEPvlfacsiMDNIKYGDNTKEipMERVIAAAKQAQLHDFVMS-LPEkyetnvgsqgsQLSRGEKQRIAIARA 1232
Cdd:TIGR02769 105 MTVRQIIGEP-------LRHLTSLDESEQ--KARIAELLDMVGLRSEDADkLPR-----------QLSGGQLQRINIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1233 IVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIE 1296
Cdd:TIGR02769 165 LAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
420-638 |
5.55e-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: 95.72 E-value: 5.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpevKILNDLNMVIKPGeMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 499
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIRY---------GREDATmedIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 569
Cdd:cd03264 76 YLPQEFGVYPNfTVREFLDYiawlkgipsKEVKAR---VDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 638
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
136-361 |
8.19e-22 |
|
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: 97.48 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 136 SEMIKFASYYAGIAVAVLITGYIQiCFWVIAAARQIQK-MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIA 214
Cdd:cd18541 37 SQLLRYALLILLLALLIGIFRFLW-RYLIFGASRRIEYdLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 215 DQMALFIQrmTSTICGFLLG--FFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVA 292
Cdd:cd18541 116 PGILYLVD--ALFLGVLVLVmmFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIK 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 293 AFGGEKREVER--------YEKNLVFAQrwgirkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQ 361
Cdd:cd18541 194 AFVQEEAEIERfdklneeyVEKNLRLAR--------VDALFFPLIGLLIGLSFLIVLWYGGRLVIR-GTITLGDLVA 261
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
1089-1306 |
9.10e-22 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 96.44 E-value: 9.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL---------------- 1152
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRckhirmifqdpntsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1153 -RSNIGIVSQEPVLFacsimdnikygdNTKEIPMER---VIAAAKQAQLhdfvmsLPEkyETNVGSQgsQLSRGEKQRIA 1228
Cdd:COG4167 102 pRLNIGQILEEPLRL------------NTDLTAEEReerIFATLRLVGL------LPE--HANFYPH--MLSSGQKQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1229 IARAIVRDPKILLLDEATSALDTeSEKT--VQVALD-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELM 1304
Cdd:COG4167 160 LARALILQPKIIIADEALAALDM-SVRSqiINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
|
..
gi 21536378 1305 AQ 1306
Cdd:COG4167 239 AN 240
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1083-1303 |
1.90e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1083 CKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI---------------DGHDSKKV 1147
Cdd:PRK13631 29 CVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnheliTNPYSKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1148 -NVQFLRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPMERviaAAKQAQLHDFVMSLPEKYetnVGSQGSQLSRGEK 1224
Cdd:PRK13631 109 kNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSY---LERSPFGLSGGQK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1225 QRIAIARAIVRDPKILLLDEATSALDTESEK-TVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEE 1302
Cdd:PRK13631 183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYE 262
|
.
gi 21536378 1303 L 1303
Cdd:PRK13631 263 I 263
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
420-646 |
2.01e-21 |
|
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: 99.76 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSR--------PEVKILNDLNMVIKPGEMTALVGPSGAGKST----ALQLIqrfydPCEGMVTVDGHDIR 487
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 488 SLN---IQWLRDQIGIVEQEPvlFST-----TIAENI-------RYGREDATMEDIVQAAKE--------ANAYnfimdl 544
Cdd:COG4172 351 GLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIaeglrvhGPGLSAAERRARVAEALEevgldpaaRHRY------ 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 545 PQQFdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA 622
Cdd:COG4172 423 PHEFsgg-----------qrqRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQreHGLAYLFISHDLAVVRA 491
|
250 260
....*....|....*....|....*
gi 21536378 623 -ADTIIGFEHGTAVERGTHEELLER 646
Cdd:COG4172 492 lAHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
419-643 |
2.63e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 419 EIEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI----RSLNIQ 492
Cdd:PRK13634 2 DITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 493 WLRDQIGIVEQ--EPVLFSTTIAENIRYGRED--ATMEDIVQAAKEANAynfIMDLPQQfdtLVGEGGGQMSGGQKQRVA 568
Cdd:PRK13634 82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLPEE---LLARSPFELSGGQMRRVA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 569 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEEL 643
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREI 233
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1094-1305 |
2.73e-21 |
|
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: 94.72 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD--SKKVnvqFLRSNIGIVS--QEPVLFA-C 1168
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDitGLPP---HRIARLGIARtfQNPRLFPeL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNI------KYGDNTKEIPMERVIAAAKQAQLHDFVMS------LPEKYETNVGSqgsqLSRGEKQRIAIARAIVRD 1236
Cdd:COG0411 95 TVLENVlvaahaRLGRGLLAALLRLPRARREEREARERAEEllervgLADRADEPAGN----LSYGQQRRLEIARALATE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1237 PKILLLDEATSAL-DTESEKTVQVALD-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:COG0411 171 PKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1094-1306 |
3.23e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.65 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-------------SKKVNVQFLRSNIGIVS 1160
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvADKNQLRLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1161 QEPVLFacSIMDNIkygDNTKEIPMErVIAAAKQAQLHDFVmslpeKYETNVG----SQG---SQLSRGEKQRIAIARAI 1233
Cdd:PRK10619 99 QHFNLW--SHMTVL---ENVMEAPIQ-VLGLSKQEARERAV-----KYLAKVGiderAQGkypVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1234 VRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
436-638 |
3.37e-21 |
|
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: 93.51 E-value: 3.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIK---PGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG---HDIR-SLNIQWLRDQIGIVEQEPVLF 508
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRkKINLPPQQRKIGLVFQQYALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 S-TTIAENIRYG-REDATMEDIVQAAKeanaynfIMDLpQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMAT 586
Cdd:cd03297 88 PhLNVRENLAFGlKRKRNREDRISVDE-------LLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 587 SALDNESEAMVQEVLSKIQ---HGHTIIsVAHRLSTV-RAADTIIGFEHGTAVERG 638
Cdd:cd03297 160 SALDRALRLQLLPELKQIKknlNIPVIF-VTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
175-370 |
3.48e-21 |
|
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: 95.24 E-value: 3.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 175 RKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGI 254
Cdd:cd18575 72 RKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 255 GAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERY----EKNLVFAQRW-GIRkgivmGFFTGFV 329
Cdd:cd18575 152 PIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFatavEAAFAAALRRiRAR-----ALLTALV 226
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536378 330 WCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQ-IFLSVIVGA 370
Cdd:cd18575 227 IFLVFGAIVFVLWLGAHDVL-AGRMSAGELSQfVFYAVLAAG 267
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
146-393 |
3.57e-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: 95.19 E-value: 3.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 225
Cdd:cd18551 43 VALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 226 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYE 305
Cdd:cd18551 123 TVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGG 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 306 KNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVlDEGEYTPGTLVQIFLSV--IVGAL-NLGNAspcLEA 382
Cdd:cd18551 203 EAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARV-ASGALTVGTLVAFLLYLfqLITPLsQLSSF---FTQ 278
|
250
....*....|.
gi 21536378 383 FATGRAAATSI 393
Cdd:cd18551 279 LQKALGALERI 289
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
420-649 |
4.50e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.91 E-value: 4.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNIQWLRDQ 497
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEP--VLFSTTIAENIRYGREDATM-EDIVQA----AKEANAYNFIMDLPQQFDTLvgegggqmsgGQKQRVAIA 570
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLpEDEVRKrvdnALKRTGIEHLKDKPTHCLSF----------GQKKRVAIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 571 RALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEK 233
|
..
gi 21536378 648 GV 649
Cdd:PRK13636 234 EM 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1110-1306 |
5.54e-21 |
|
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: 96.32 E-value: 5.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1110 AFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGH---DSKKVnvQFL---RSNIGIVSQEPVLFA-CSIMDNIKYGdn 1179
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqDSARG--IFLpphRRRIGYVFQEARLFPhLSVRGNLLYG-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1180 tkeipMERVIAAAKQAQLHDfVMSL----------PEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:COG4148 102 -----RKRAPRAERRISFDE-VVELlgighlldrrPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1250 DTESEKTVQVALDK-AREGRTCIV-IAH------RLstiqnADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:COG4148 165 DLARKAEILPYLERlRDELDIPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1092-1303 |
5.57e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 5.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQ-----GKVMIDGHD--SKKVNVQFLRSNIGIVSQEPV 1164
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNiySPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFA-CSIMDNIKYG-------DNTKEIPmERVIAAAKQAQLHDFVMSLPEKYETNvgsqgsqLSRGEKQRIAIARAIVRD 1236
Cdd:PRK14267 96 PFPhLTIYDNVAIGvklnglvKSKKELD-ERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALAMK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1237 PKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHrlSTIQNA---DIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK14267 168 PKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVGPTRKV 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
420-635 |
7.49e-21 |
|
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: 90.95 E-value: 7.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQ-I 498
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVlfsttiAEnirygredatmedivqaakeanaynfimdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPK 578
Cdd:cd03216 78 AMVYQLSV------GE-------------------------------RQ------------------MVEIARALARNAR 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 579 ILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRA-ADTIIGFEHGTAV 635
Cdd:cd03216 103 LLILDEPTAALTPAEVERLFKVIRRLRaQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
420-647 |
7.71e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 94.46 E-value: 7.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG----HDIRSLNIQW 493
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 494 LRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEdiVQAAKEaNAYNFIMDLPQQFDTLvGEGGGQMSGGQKQRVAIAR 571
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN--LDEVKN-YAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 572 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1089-1304 |
8.28e-21 |
|
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: 93.23 E-value: 8.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGK-VMIDGHDSKKVNVQFLRSNIGIVSQEpvlfa 1167
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIGLVSPA----- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 csIMDNIKYGDNTKEI--------------PMERVIAAAKQAqLHDFVMSlpEKYETNVGSqgsqLSRGEKQRIAIARAI 1233
Cdd:COG1119 87 --LQLRFPRDETVLDVvlsgffdsiglyrePTDEQRERAREL-LELLGLA--HLADRPFGT----LSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1234 VRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIV-IAHRLStiqnaDIIA------VMAQGVVIEKGTHEELM 1304
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPgithvlLLKDGRVVAAGPKEEVL 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1095-1296 |
8.51e-21 |
|
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: 92.88 E-value: 8.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQL---LERfydPDQGKVMIDGHDSKKVN----VQFLRSNIGIVSQE----P 1163
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1164 VLFAcsiMDNIkygdntkEIPMErvIAAAKQAQlhdfvmSLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVRDP 1237
Cdd:COG4181 104 TLTA---LENV-------MLPLE--LAGRRDAR------ARARALLERVGLGHrldhypAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1238 KILLLDEATSALDTESEKTVQVAL-DKARE-GRTCIVIAHRLSTIQNADIIAVMAQGVVIE 1296
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
420-647 |
1.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 93.74 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR----SLNIQW 493
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 494 LRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEDivQAAKEAnAYNFI--MDLPQQfdtLVGEGGGQMSGGQKQRVAI 569
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE--DEAKEK-ALKWLkkVGLSED---LISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 570 ARALIRNPKILLLDMATSALDNES-EAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1090-1296 |
1.27e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.21 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1090 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----------VQFL------- 1152
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1153 ---RSNIGIVSQEPVLFACSImdnikygdnTKEIPMERVIAAAKQAQLHDFVMS-LPEkyetnvgsqgsQLSRGEKQRIA 1228
Cdd:PRK10419 102 vnpRKTVREIIREPLRHLLSL---------DKAERLARASEMLRAVDLDDSVLDkRPP-----------QLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1229 IARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIE 1296
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-632 |
1.36e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 93.18 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDI--RSLNIQ 492
Cdd:PRK14258 8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 493 WLRDQIGIVEQEPVLFSTTIAENIRYG------REDATMEDIVQAAKEAnaynfiMDLPQQFDTLVGEGGGQMSGGQKQR 566
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 567 VAIARALIRNPKILLLDMATSALDNESEAMVQEVLS--KIQHGHTIISVAHRLSTVRAADTIIGFEHG 632
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
755-975 |
1.49e-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: 93.64 E-value: 1.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 755 MLVGSVGAAVNGTVTPLYAFLFSQILGTFSIpdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 834
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFV---EKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 835 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALs 914
Cdd:cd18552 78 LFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 915 gatqtrmLTGFASR-----DKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAI 975
Cdd:cd18552 155 -------PIRRIGKrlrkiSRRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSM 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
435-642 |
2.06e-20 |
|
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: 91.73 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 435 VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGIVE--QEPVLFST-T 511
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 512 IAENIR-----YGREDATMEDIVQAAKEANAYNF----IMDLPQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLL 582
Cdd:cd03219 92 VLENVMvaaqaRTGSGLLLARARREEREARERAEelleRVGLADLADRPA----GELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 583 DMATSAL-DNESEAMVqEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEE 642
Cdd:cd03219 168 DEPAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDE 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1089-1252 |
2.37e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.00 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQflRSNIGIVSQEPVL 1165
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 FA-CSIMDNIKYG---DNTKEIPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:COG4136 88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDP-----------ATLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|.
gi 21536378 1242 LDEATSALDTE 1252
Cdd:COG4136 157 LDEPFSKLDAA 167
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1094-1280 |
2.41e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.09 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDS---KKVNVQFLRSNIGIVSQEP-VLFACS 1169
Cdd:PRK10908 16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKY-----GDNTKEIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK10908 96 VYDNVAIpliiaGASGDDI-RRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 21536378 1245 ATSALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTI 1280
Cdd:PRK10908 164 PTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
420-644 |
2.52e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 92.10 E-value: 2.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:COG4559 2 LEAENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVL-FSTTIAENIRYGR-----EDATMEDIVQAAKEAnaynfiMDLP--------------QQfdtlvgegggqm 559
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVALGRaphgsSAAQDRQIVREALAL------VGLAhlagrsyqtlsggeQQ------------ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 560 sggqkqRVAIARALI-------RNPKILLLDMATSALDneseamvqevlskIQHGHTIISVAHRLS-------------- 618
Cdd:COG4559 141 ------RVQLARVLAqlwepvdGGPRWLFLDEPTSALD-------------LAHQHAVLRLARQLArrgggvvavlhdln 201
|
250 260
....*....|....*....|....*..
gi 21536378 619 -TVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:COG4559 202 lAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1079-1306 |
2.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 92.46 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1079 DFVDCK---FTYPSRPDSQ---VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKV-NVQF 1151
Cdd:PRK13633 3 EMIKCKnvsYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPME----RVIAAAKQAQLHDFvmslpEKYETNVgsqgsqLSRGEKQ 1225
Cdd:PRK13633 83 IRNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEeireRVDESLKKVGMYEY-----RRHAPHL------LSGGQKQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK13633 152 RVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
...
gi 21536378 1304 MAQ 1306
Cdd:PRK13633 232 FKE 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1086-1306 |
2.73e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.56 E-value: 2.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEP-- 1163
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPdd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1164 VLFACSIMDNIKYGDNT----KEIPMERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:PRK13652 90 QIFSPTVEQDIAFGPINlgldEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1092-1321 |
3.60e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 92.48 E-value: 3.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvqflRSNIGIVSQEPVLFA-CSI 1170
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPkMKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYgdntkeipmerviaaakQAQLHDfvMS----------------LPEKYETNVGSqgsqLSRGEKQRIAIARAIV 1234
Cdd:COG4152 89 GEQLVY-----------------LARLKG--LSkaeakrradewlerlgLGDRANKKVEE----LSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1235 RDPKILLLDEATSALDTES-EKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQKGAYYK 1312
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGRNTL 225
|
....*....
gi 21536378 1313 LVTTGSPIS 1321
Cdd:COG4152 226 RLEADGDAG 234
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1078-1307 |
3.80e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 92.20 E-value: 3.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKKVNVQF 1151
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIVSQ--EPVLFACSIMDNIKYGDN----TKEIPMERVIAAAKQAQLHDFVMSlpekyetnvgSQGSQLSRGEKQ 1225
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKnfgfSEDEAKEKALKWLKKVGLSEDLIS----------KSPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK13641 153 RVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMmQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEI 232
|
....
gi 21536378 1304 MAQK 1307
Cdd:PRK13641 233 FSDK 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
420-647 |
3.92e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPS-RP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL----NIQW 493
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 494 LRDQIGIVEQ--EPVLFSTTIAENIRYGRED--ATMEDIVQAAKEANAYNFIMdlpqqfDTLVGEGGGQMSGGQKQRVAI 569
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGT------HE 641
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKpkdifqDV 236
|
....*.
gi 21536378 642 ELLERK 647
Cdd:PRK13649 237 DFLEEK 242
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1094-1306 |
4.58e-20 |
|
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: 95.52 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTS----IQLLERFYDPDQGKVMIDGHDSKKVNVQFLR----SNIGIVSQEP-- 1163
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEPmt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1164 --------------VLFacsimdnIKYGDNTKEIpMERVIAAAKQAQLHDfvmslPEKyetNVGSQGSQLSRGEKQRIAI 1229
Cdd:COG4172 104 slnplhtigkqiaeVLR-------LHRGLSGAAA-RARALELLERVGIPD-----PER---RLDAYPHQLSGGQRQRVMI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1230 ARAIVRDPKILLLDEATSALDTesekTVQVA-LD-----KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEE 1302
Cdd:COG4172 168 AMALANEPDLLIADEPTTALDV----TVQAQiLDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAE 243
|
....
gi 21536378 1303 LMAQ 1306
Cdd:COG4172 244 LFAA 247
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
430-638 |
4.66e-20 |
|
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: 90.12 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 430 PSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRDQIGIVEQEPVLFS 509
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV-VKEPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 510 -TTIAENIRY-GRedatmediVQAAKEANAYNFIMDLPQQFDT--LVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMA 585
Cdd:cd03266 92 rLTARENLEYfAG--------LYGLKGDELTARLEELADRLGMeeLLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 586 TSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 638
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
420-615 |
6.24e-20 |
|
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: 90.19 E-value: 6.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL 494
Cdd:COG4181 9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 495 RDQIGIVEQ-EPVLFSTTIAENI-----RYGREDATmedivQAAKE----------ANAYnfimdlP-------QQfdtl 551
Cdd:COG4181 89 ARHVGFVFQsFQLLPTLTALENVmlpleLAGRRDAR-----ARARAllervglghrLDHY------PaqlsggeQQ---- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 552 vgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 615
Cdd:COG4181 154 --------------RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnrERGTTLVLVTH 205
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
418-651 |
6.39e-20 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 96.77 E-value: 6.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHY-PSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD 496
Cdd:PTZ00243 1307 GSLVFEGVQMRYrEGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFSTTIAENIRYGREDATMEdiVQAAKE-ANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALI- 574
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLEASSAE--VWAALElVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLk 1462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 575 RNPKILLLDMATS----ALDNESEAMVQEVLSkiqhGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVY 650
Cdd:PTZ00243 1463 KGSGFILMDEATAnidpALDRQIQATVMSAFS----AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSI 1538
|
.
gi 21536378 651 F 651
Cdd:PTZ00243 1539 F 1539
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
420-615 |
6.51e-20 |
|
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: 89.62 E-value: 6.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 499
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLF-STTIAENIRYG------REDATMEDIVQAAKeanaynfIMDLpqqfDTLVGEGGGQMSGGQKQRVAIARA 572
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAE-------LLQI----EHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 573 LIRNPKILLLDMATSALDNE-SEAMVQEvLSKIQ--HGHTIISVAH 615
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKlRVQMRAE-LKRLQqrLGTTTIYVTH 189
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
792-1012 |
7.13e-20 |
|
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: 91.39 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 792 RSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNspGALTTRLATDASQVQGA 871
Cdd:cd18576 32 TASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV--GELTSRLSNDVTQIQDT 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 872 AGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVA 951
Cdd:cd18576 110 LTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVK 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 952 GIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 1012
Cdd:cd18576 190 AFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGEL 250
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
420-638 |
7.22e-20 |
|
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: 89.47 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEvkilnDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 499
Cdd:cd03298 1 VRLDKIRFSYGEQPM-----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFS-TTIAENIRYGREDA---TMED---IVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARA 572
Cdd:cd03298 74 MLFQENNLFAhLTVEQNVGLGLSPGlklTAEDrqaIEVALARVGLAGLEKRLPGELS-----------GGERQRVALARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 573 LIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 638
Cdd:cd03298 143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1094-1298 |
7.44e-20 |
|
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: 90.02 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPD---QGKVMIDGHDSKKVNVQFlrsNIGIVSQEPVLFAC-S 1169
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQK---CVAYVRQDDILLPGlT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYgdnTKEIPMeRVIAAAKQAQLHDFVMSLPEKYETNVGSQG-SQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:cd03234 98 VRETLTY---TAILRL-PRKSSDAIRKKRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1249 LDTESE-KTVQVALDKAREGRTCIVIAH--RLSTIQNADIIAVMAQGVVIEKG 1298
Cdd:cd03234 174 LDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
420-644 |
7.87e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 90.60 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:PRK13548 3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVL-FSTTIAENIRYGR-----EDATMEDIVQAAKEAN-----AYNFIMDLP---QQfdtlvgegggqmsggqkq 565
Cdd:PRK13548 80 VLPQHSSLsFPFTVEEVVAMGRaphglSRAEDDALVAAALAQVdlahlAGRDYPQLSggeQQ------------------ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 566 RVAIARALIR------NPKILLLDMATSALDneseamvqevlskIQHGHTIISVAHRLS----------------TVRAA 623
Cdd:PRK13548 142 RVQLARVLAQlwepdgPPRWLLLDEPTSALD-------------LAHQHHVLRLARQLAherglavivvlhdlnlAARYA 208
|
250 260
....*....|....*....|.
gi 21536378 624 DTIIGFEHGTAVERGTHEELL 644
Cdd:PRK13548 209 DRIVLLHQGRLVADGTPAEVL 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1085-1305 |
8.74e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.82 E-value: 8.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFLRSNIGIVSQEP 1163
Cdd:PRK13644 9 YSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQNP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1164 --VLFACSIMDNIKYG-DNTKEIPME---RVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK13644 87 etQFVGRTVEEDLAFGpENLCLPPIEirkRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALDKA-REGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1078-1299 |
1.01e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.96 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPS-RP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDG----HDSKKVNVQF 1151
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitSTSKNKDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERVIAAAKQaQLHDFVMSlPEKYETNvgsqGSQLSRGEKQRIAI 1229
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALARE-KLALVGIS-ESLFEKN----PFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1230 ARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGT 1299
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1073-1305 |
1.07e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.22 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1073 NFQGKIDFVDCKFTYPSRP--DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKK 1146
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1147 VN-VQFLRSNIGIVSQEP--VLFACSIMDNIKYG-----DNTKEipmerviAAAKQAQLHDFVmSLPEKYetnVGSQGSQ 1218
Cdd:PRK13645 82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpvnlgENKQE-------AYKKVPELLKLV-QLPEDY---VKRSPFE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1219 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK---TVQVALDKaREGRTCIVIAHRLSTI-QNADIIAVMAQGVV 1294
Cdd:PRK13645 151 LSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKV 229
|
250
....*....|.
gi 21536378 1295 IEKGTHEELMA 1305
Cdd:PRK13645 230 ISIGSPFEIFS 240
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1095-1307 |
1.27e-19 |
|
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: 90.68 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDqGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSIMDNI 1174
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1175 K-YGDNTKEipmeRVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1253
Cdd:cd03289 98 DpYGKWSDE----EIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1254 EKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:cd03289 174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
419-641 |
1.36e-19 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 419 EIEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQ 492
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfdfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 493 WLRDQIGIVEQE----PVLfstTIAENI--------RYGREDATMEDI-----VQAAKEANAYNFIMDLPQQfdtlvgeg 555
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMkllarLRLTDKADRFPLHLSGGQQ-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 556 ggqmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVR-AADTIIGFEHGT 633
Cdd:COG4161 148 ---------QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARkVASQVVYMEKGR 218
|
....*...
gi 21536378 634 AVERGTHE 641
Cdd:COG4161 219 IIEQGDAS 226
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
855-1314 |
1.38e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 95.81 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 855 GALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFS----FSWKLSLVILCFFPFLALSGATQTRMLT-GFASRD 929
Cdd:PLN03232 398 GKVTNMITTDANALQQIAEQLHGLWSAPFR-IIVSMVLLYQqlgvASLFGSLILFLLIPLQTLIVRKMRKLTKeGLQWTD 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 930 KQalemVGqITNEALSNIRTVAGIGKERRF---IEALETELEKPFKTAiqkaniyGFCFAFAQcimFIANSASY-----R 1001
Cdd:PLN03232 477 KR----VG-IINEILASMDTVKCYAWEKSFesrIQGIRNEELSWFRKA-------QLLSAFNS---FILNSIPVvvtlvS 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1002 YGGYLISNEGLHFSYVFRVISAVVLSATALGRAFSYTPSYAKAKISAARFFQL-------LDRQPPISVYNTAgekwdnf 1074
Cdd:PLN03232 542 FGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELllseeriLAQNPPLQPGAPA------- 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1075 qgkIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQ-LLERFYDPDQGKVMIdghdskkvnvqflR 1153
Cdd:PLN03232 615 ---ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVI-------------R 678
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1154 SNIGIVSQEPVLFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAI 1233
Cdd:PLN03232 679 GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVT--ALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAV 755
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1234 VRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYK 1312
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKK 835
|
..
gi 21536378 1313 LV 1314
Cdd:PLN03232 836 LM 837
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1092-1307 |
1.52e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 89.69 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---------SKKVNV--QFLRSNIGIVS 1160
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlARRLALlpQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1161 QEPVLFACSIMDNI--KYGDNTKEipmeRVIAAAKQAQLHDFVmslpEKYETNvgsqgsqLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK11231 94 RELVAYGRSPWLSLwgRLSAEDNA----RVNQAMEQTRINHLA----DRRLTD-------LSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1239 ILLLDEATSALDTESektvQVALDK-----AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:PRK11231 159 VVLLDEPTTYLDINH----QVELMRlmrelNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
435-642 |
1.61e-19 |
|
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: 89.71 E-value: 1.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 435 VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiQWLRDQIGIVE--QEPVLFST-T 511
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFPElT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 512 IAENI--------------------RYGREDATMEDIVQA-------AKEANAYnfIMDLP--QQfdtlvgegggqmsgg 562
Cdd:COG0411 96 VLENVlvaaharlgrgllaallrlpRARREEREARERAEEllervglADRADEP--AGNLSygQQ--------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 563 qkQRVAIARALIRNPKILLLD-----MATSaldnESEAMVqEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTA 634
Cdd:COG0411 159 --RRLEIARALATEPKLLLLDepaagLNPE----ETEELA-ELIRRLrdERGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
....*...
gi 21536378 635 VERGTHEE 642
Cdd:COG0411 232 IAEGTPAE 239
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1094-1275 |
2.17e-19 |
|
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: 88.65 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDgHDSKKVNV------QFL---RSNIGIVSQ--- 1161
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLaqasprEILalrRRTIGYVSQflr 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1162 ------------EPVLfacsimdnikygdntkEIPMERVIAAAKQAQLHDFvMSLPEK----YETNvgsqgsqLSRGEKQ 1225
Cdd:COG4778 104 viprvsaldvvaEPLL----------------ERGVDREEARARARELLAR-LNLPERlwdlPPAT-------FSGGEQQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1226 RIAIARAIVRDPKILLLDEATSALDTES-EKTVQVALDKAREGRTCIVIAH 1275
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFH 210
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1089-1304 |
2.36e-19 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 89.06 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FA 1167
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIKYGdntkEIPMERVIAAAKQaqlhdfvmsLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVR------ 1235
Cdd:PRK13548 91 FTVEEVVAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdg 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1236 DPKILLLDEATSALD-TESEKTVQVALDKARE-GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 1304
Cdd:PRK13548 158 PPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
420-643 |
2.47e-19 |
|
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: 88.20 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIG 499
Cdd:cd03265 1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPvlfsttIAENIRYGREDATMEDIVQAAKEANAYNFI------MDLPQQFDTLVgeggGQMSGGQKQRVAIARAL 573
Cdd:cd03265 77 IVFQDL------SVDDELTGWENLYIHARLYGVPGAERRERIdelldfVGLLEAADRLV----KTYSGGMRRRLEIARSL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 643
Cdd:cd03265 147 VHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1090-1303 |
2.65e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.57 E-value: 2.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1090 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLErFYDPD----QGKVMIDGHdskKVNVQFLRSNIGIVSQEPVL 1165
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 F-------ACSIMDNIKYGDN-TKEIPMERViaaakQAQLHDfvMSLPEKYETNVGSQGSQ--LSRGEKQRIAIARAIVR 1235
Cdd:TIGR00955 111 IptltvreHLMFQAHLRMPRRvTKKEKRERV-----DEVLQA--LGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1236 DPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLST--IQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVvQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
420-615 |
2.75e-19 |
|
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: 87.95 E-value: 2.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 499
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIRY-----GREDATMEDIVQAAKEanaynfIMDLPQQFDTLVgeggGQMSGGQKQRVAIARAL 573
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKEEVELLLR------VLGLTDKANKRA----RTLSGGMKRKLSLAIAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAH 615
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1092-1305 |
3.55e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH--DSKKVNVQFLRSNIGIVSQEP--VLFA 1167
Cdd:PRK13638 13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIKYGDNTKEIPMERViaaakqAQLHDFVMSLpekyetnVGSQGSQ------LSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEI------TRRVDEALTL-------VDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1242 LDEATSALDTESeKTVQVALDK--AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PRK13638 160 LDEPTAGLDPAG-RTQMIAIIRriVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
421-649 |
4.57e-19 |
|
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: 87.73 E-value: 4.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 421 EFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-RDQIG 499
Cdd:COG0410 5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIRYGREDATMEDIVQAAKEanaynFIMDL-P-----------------QQFdtlvgegggqms 560
Cdd:COG0410 82 YVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLE-----RVYELfPrlkerrrqragtlsggeQQM------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 561 ggqkqrVAIARALIRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLSTVRA-ADTIIGFEHGTAV 635
Cdd:COG0410 145 ------LAIGRALMSRPKLLLLDEPSLGL---APLIVEEIFEIIRRlnreGVTILLVEQNARFALEiADRAYVLERGRIV 215
|
250
....*....|....
gi 21536378 636 ERGTHEELLERKGV 649
Cdd:COG0410 216 LEGTAAELLADPEV 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
423-615 |
5.62e-19 |
|
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: 86.54 E-value: 5.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 423 HNVTFHYpsRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlniQWLRDQIGIVE 502
Cdd:cd03226 3 ENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 503 QEP--VLFSTTIAENIRYGREDA--TMEDIVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkqRVAIAR 571
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELdaGNEQAETVLKDLDLYALKERHPlslsggqKQ------------------RLAIAA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536378 572 ALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAH 615
Cdd:cd03226 140 ALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITH 184
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
438-644 |
6.37e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.86 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRD----QIGIVEQEPVLFS-TTI 512
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 513 AENIRYGREDATM------EDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARALIRNPKILLLDMAT 586
Cdd:PRK10070 124 LDNTAFGMELAGInaeerrEKALDALRQVGLENYAHSYPDELS-----------GGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 587 SALDNESEAMVQEVLSKIQ--HGHTIISVAHRL-STVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1087-1275 |
6.66e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.83 E-value: 6.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1087 YPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkVNVQFLRSNIGIVSQ-EPVL 1165
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPGAERGVVFQnEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 FACSIMDNIKYGDNTKEIPMERVIAAAKQAQlhdfvmslpekyeTNVGSQGS------QLSRGEKQRIAIARAIVRDPKI 1239
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQML-------------KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAH 1275
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1086-1275 |
6.98e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.00 E-value: 6.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRPDSQ-VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSNIGIVSQEPV 1164
Cdd:COG4525 12 RYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRGVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFA-CSIMDNIKYGdntkeIPMERVIAAAKQAQLHDFVmslpekyeTNVGSQG------SQLSRGEKQRIAIARAIVRDP 1237
Cdd:COG4525 87 LLPwLNVLDNVAFG-----LRLRGVPKAERRARAEELL--------ALVGLADfarrriWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAH 1275
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1085-1307 |
8.39e-19 |
|
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: 88.37 E-value: 8.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrsnIGIVSQEPV 1164
Cdd:cd03291 42 FSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFACSIMDNIKYGDNTKEIPMERVIaaaKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:cd03291 109 IMPGTIKENIIFGVSYDEYRYKSVV---KACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1245 ATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:cd03291 186 PFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1094-1305 |
8.78e-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: 86.83 E-value: 8.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVqFLRSNIGI--VSQEPVLF-ACSI 1170
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIK-----YGDNTKEIpMERViaaakQAQLHDFvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:cd03218 93 EENILavleiRGLSKKER-EEKL-----EELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1246 TSALDTESEKTVQVALDKAREGRTCIVIA-HRLS-TIQNADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
420-646 |
8.96e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 90.01 E-value: 8.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRDQIG 499
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFS-TTIAENIRYG--REDATMEDIVQAAKEANAY----NFIMDLPQQFdtlvgegggqmSGGQKQRVAIARA 572
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEALRMvqleEFAQRKPHQL-----------SGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 573 LIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAH----RLSTvraADTIIGFEHGTAVERGTHEELLER 646
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
756-1050 |
9.95e-19 |
|
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: 88.26 E-value: 9.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 756 LVGSVGAAVNGTVTPLYAflfSQILGTFSipDKEEQRSQINGVCLLFVamgcVSLFTQFLQGYAFAKSGELLTKRLRKFG 835
Cdd:cd18551 5 LLLSLLGTAASLAQPLLV---KNLIDALS--AGGSSGGLLALLVALFL----LQAVLSALSSYLLGRTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 836 FRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSG 915
Cdd:cd18551 76 WRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 916 ATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIA 995
Cdd:cd18551 154 LPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 996 NSASYRYGGYLISNEGLHFS-------YVFRVISAVvlsaTALGRAFSytpSYAKAKISAAR 1050
Cdd:cd18551 234 LLVVLGVGGARVASGALTVGtlvafllYLFQLITPL----SQLSSFFT---QLQKALGALER 288
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1094-1311 |
1.76e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 90.53 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQGKVMIDGHDSKKVNVQFL---RSNIGIVSQEPV------ 1164
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNsslnpr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFACSIMDN---IKYGDNTKEIPMERVIAAAKQAQLHdfvmslPE---KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK15134 379 LNVLQIIEEglrVHQPTLSAAQREQQVIAVMEEVGLD------PEtrhRYP-------AEFSGGQRQRIAIARALILKPS 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1239 ILLLDEATSALDteseKTVQ---VALDKAREGR---TCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQKGAYY 1311
Cdd:PRK15134 446 LIILDEPTSSLD----KTVQaqiLALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
420-676 |
1.96e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 87.47 E-value: 1.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIG 499
Cdd:COG4152 2 LELKGLTKRFG---DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLF-STTIAENIRY-GR-EDATMEDIVQAAKE--------ANAYNFIMDLP---QQfdtlvgegggqmsggqkq 565
Cdd:COG4152 75 YLPEERGLYpKMKVGEQLVYlARlKGLSKAEAKRRADEwlerlglgDRANKKVEELSkgnQQ------------------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 566 RVAIARALIRNPKILLLDMATSALD--NeSEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 642
Cdd:COG4152 137 KVQLIAALLHDPELLILDEPFSGLDpvN-VELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDE 215
|
250 260 270
....*....|....*....|....*....|....
gi 21536378 643 LLERKGVYFTLVTLQSQGNQALNEEDIKDATEDD 676
Cdd:COG4152 216 IRRQFGRNTLRLEADGDAGWLRALPGVTVVEEDG 249
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1089-1319 |
2.02e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.13 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVL-FA 1167
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIKYG-----------DNTKEIPMERVIAAAKQAQLHDFVMSlpekyetnvgsqgsQLSRGEKQRIAIARAIVRD 1236
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrfdtwTETDRAAVERAMERTGVAQFADRPVT--------------SLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1237 PKILLLDEATSALDTESE-KTVQVALDKAREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKG------THEELMAQKG 1308
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGppadvlTADTLRAAFD 237
|
250
....*....|....
gi 21536378 1309 AYYKLVT---TGSP 1319
Cdd:PRK09536 238 ARTAVGTdpaTGAP 251
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
420-626 |
2.02e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.09 E-value: 2.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNiQWLRDQ 497
Cdd:COG3845 6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPR-DAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFST-TIAENIRYGREDATME--DIVQAAKE----ANAYNF-------IMDLP---QQfdtlvgegggqms 560
Cdd:COG3845 82 IGMVHQHFMLVPNlTVAENIVLGLEPTKGGrlDRKAARARirelSERYGLdvdpdakVEDLSvgeQQ------------- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 561 ggqkqRVAIARALIRNPKILLLDMATSAL-DNESE-------AMVQEvlskiqhGHTIISVAHRLSTVRA-ADTI 626
Cdd:COG3845 149 -----RVEILKALYRGARILILDEPTAVLtPQEADelfeilrRLAAE-------GKSIIFITHKLREVMAiADRV 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1078-1305 |
3.60e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 86.61 E-value: 3.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH----DSKKVNVQF 1151
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERvitaGKKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERviAAAKQAQLHDFVmSLPEKYETNvgsqgS--QLSRGEKQRI 1227
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEED--AKQKAREMIELV-GLPEELLAR-----SpfELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1228 AIARAIVRDPKILLLDEATSALDTESEKTVQ---VALDKaREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK13634 155 AIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
..
gi 21536378 1304 MA 1305
Cdd:PRK13634 234 FA 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
434-646 |
3.87e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 85.73 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLF 508
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 ST-TIAENIRYGREdatMEDIVQAAKEANA-YNFIMDLPQQFDTL---VGEGGGQMSGGQKQRVAIARALIRNPKILLLD 583
Cdd:PRK14247 95 PNlSIFENVALGLK---LNRLVKSKKELQErVRWALEKAQLWDEVkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 584 MATSALDNESEAMVQEVLSKIQHGHTIISVAH-RLSTVRAADTIIGFEHGTAVERGTHEELLER 646
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1100-1250 |
6.08e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.63 E-value: 6.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1100 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQflRSNIGIVSQEPVLFA-CSIMDNIKYG- 1177
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1178 ------DNTKEIPMERViaaAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALD 1250
Cdd:PRK10771 97 npglklNAAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
788-1050 |
6.10e-18 |
|
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: 85.95 E-value: 6.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 788 KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQ 867
Cdd:cd18542 31 GGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 868 VQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGatqTRMLTGFASRDKQALEMVGQITN---EAL 944
Cdd:cd18542 109 IRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFS---YVFFKKVRPAFEEIREQEGELNTvlqENL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 945 SNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGLHF-------SYV 1017
Cdd:cd18542 186 TGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLgelvafiSYL 265
|
250 260 270
....*....|....*....|....*....|...
gi 21536378 1018 FRVISAVvlsaTALGRAFSytpSYAKAKISAAR 1050
Cdd:cd18542 266 WMLIWPV----RQLGRLIN---DMSRASASAER 291
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1091-1292 |
7.74e-18 |
|
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: 83.92 E-value: 7.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV----MIDGHDSKKVNVQFLRSNIGIVSQEPVLF 1166
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 ACSIMDNIKYGDNTKEipmERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:cd03290 92 NATVEENITFGSPFNK---QRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536378 1247 SALDTE-SEKTVQVALDK--AREGRTCIVIAHRLSTIQNADIIAVMAQG 1292
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1095-1303 |
1.08e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFLRSNIGIVSQEPVLFA-CSIMD 1172
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGIYLVPQEPLLFPnLSVKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKYGDNTKEIPMERVIAAAKQAQLHdfvmslpekyeTNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALdTE 1252
Cdd:PRK15439 106 NILFGLPKRQASMQKMKQLLAALGCQ-----------LDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASL-TP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1253 SE-----KTVQVALDKareGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK15439 174 AEterlfSRIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
440-646 |
1.15e-17 |
|
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: 86.31 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 440 DLNMVIKPGEMTALVGPSGAGKSTALQLI---QRfydPCEGMVTVDGH---DIRSLniQWL---RDQIGIVEQEPVLFST 510
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEvlqDSARG--IFLpphRRRIGYVFQEARLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 511 -TIAENIRYGREdatmedivQAAKEANAYNF--IMDL----------P-------QQfdtlvgegggqmsggqkqRVAIA 570
Cdd:COG4148 92 lSVRGNLLYGRK--------RAPRAERRISFdeVVELlgighlldrrPatlsggeRQ------------------RVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 571 RALIRNPKILLLDMATSALDNESEamvQEVLSKIQ--HGHT---IISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 644
Cdd:COG4148 146 RALLSSPRLLLMDEPLAALDLARK---AEILPYLErlRDELdipILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222
|
..
gi 21536378 645 ER 646
Cdd:COG4148 223 SR 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
420-646 |
1.49e-17 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 85.55 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYP--------SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN- 490
Cdd:COG4608 8 LEVRDLKKHFPvrgglfgrTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSg 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 491 --IQWLRDQIGIVEQEPvlFS---------TTIAENIRY-------GREDATME--DIVQAAKE-ANAYnfimdlPQQFd 549
Cdd:COG4608 88 reLRPLRRRMQMVFQDP--YAslnprmtvgDIIAEPLRIhglaskaERRERVAEllELVGLRPEhADRY------PHEFs 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 550 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVR-AADTI 626
Cdd:COG4608 160 gg-----------qrqRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQdeLGLTYLFISHDLSVVRhISDRV 228
|
250 260
....*....|....*....|
gi 21536378 627 IGFEHGTAVERGTHEELLER 646
Cdd:COG4608 229 AVMYLGKIVEIAPRDELYAR 248
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1078-1307 |
1.59e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.65 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKvNVQFLRSNIG 1157
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVL-FACSIMDNI-----KYGDNTKEIpmERVIAAakqaqLHDFVmSLPEKYETNVgsqgSQLSRGEKQRIAIAR 1231
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLlvfgrYFGMSTREI--EAVIPS-----LLEFA-RLESKADARV----SDLSGGMKRRLTLAR 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1232 AIVRDPKILLLDEATSALDTESEKTVQVALDK--AReGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:PRK13536 186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
429-627 |
1.60e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.28 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 429 YPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlrdQIGIVEQEPVlf 508
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ----RSEVPDSLPL-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 stTIAENI------------RYGREDatmEDIVQAAKEANAynfIMDL-PQQFDTLvgegggqmSGGQKQRVAIARALIR 575
Cdd:NF040873 73 --TVRDLVamgrwarrglwrRLTRDD---RAAVDDALERVG---LADLaGRQLGEL--------SGGQRQRALLAQGLAQ 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 576 NPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVRAADTII 627
Cdd:NF040873 137 EADLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCV 189
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1071-1277 |
1.87e-17 |
|
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: 88.81 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1071 WDNfQGKIDFVDCKFTYPSRPDSqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDqGKVMIDGHDSKKVNVQ 1150
Cdd:TIGR01271 1212 WPS-GGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1151 FLRSNIGIVSQEPVLFACSIMDNIkygDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIA 1230
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLA 1365
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536378 1231 RAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRL 1277
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1077-1319 |
2.02e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.67 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1077 KIDFVDCKFTYPSrpDSQVLNGLSVSISPGQTLAFVGSSGCGKST---SIQLLERFYDpdqGKVMIDGhdsKKVN-VQFL 1152
Cdd:PRK11650 3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrMVAGLERITS---GEIWIGG---RVVNeLEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1153 RSNIGIVSQEPVLFA-CSIMDNIKYG-DNTK----EIpMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQR 1226
Cdd:PRK11650 75 DRDIAMVFQNYALYPhMSVRENMAYGlKIRGmpkaEI-EERVAEAARILELEPLLDRKP-----------RELSGGQRQR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1227 IAIARAIVRDPKILLLDEATSALDTESEktVQVALD----KAREGRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHE 1301
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKLR--VQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
250 260
....*....|....*....|....
gi 21536378 1302 ELmaqkgaYYKLVTT------GSP 1319
Cdd:PRK11650 221 EV------YEKPASTfvasfiGSP 238
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1078-1319 |
2.22e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 2.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTY-PSRP-DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV----MIDGHDSKKVNVQF 1151
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIVSQEP--VLFACSIMDNIKYGDNTKEIPMERVIA-AAKQAQLHDFVMSLPEKyetnvgsQGSQLSRGEKQRIA 1228
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFWEK-------SPFELSGGQMRRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1229 IARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMaQ 1306
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVF-Q 233
|
250
....*....|...
gi 21536378 1307 KGAYYKLVTTGSP 1319
Cdd:PRK13643 234 EVDFLKAHELGVP 246
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1089-1276 |
2.41e-17 |
|
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: 80.66 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVL-NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqflrSNIGIVSQEPVLFA 1167
Cdd:cd03223 9 ATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRPYLPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIKYgdntkeiPMERViaaakqaqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:cd03223 78 GTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATS 120
|
170 180
....*....|....*....|....*....
gi 21536378 1248 ALDTESEKTVQVALDKarEGRTCIVIAHR 1276
Cdd:cd03223 121 ALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1097-1320 |
2.88e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 84.76 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1097 NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN-VQFL--RSNIGIVSQEPVlfaCSIMDN 1173
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPL---ASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1174 IKYGDNTKEiPMERVIAAAKQAQLHDFVMSLPEKyetnVGSQGSQLSR-------GEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:PRK15079 115 MTIGEIIAE-PLRTYHPKLSRQEVKDRVKAMMLK----VGLLPNLINRyphefsgGQCQRIGIARALILEPKLIICDEPV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1247 SALDTESEKTVqVALDKA--RE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ-KGAYYKLVTTGSPI 1320
Cdd:PRK15079 190 SALDVSIQAQV-VNLLQQlqREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNpLHPYTKALMSAVPI 267
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
420-644 |
3.10e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.50 E-value: 3.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKST-ALQLiQRFYDPCEGMVTVDGHDIRSLN-IQWLRDQ 497
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTlALHL-NGLLRPQKGKVLVSGIDTGDFSkLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEP--VLFSTTIAENIRYGREDATMEDIV------QAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAI 569
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEirkrvdRALAEIGLEKYRHRSPKTLS-----------GGQGQCVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
418-616 |
3.48e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 86.78 E-value: 3.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYPS-RPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDiRSLniqwlrd 496
Cdd:COG4178 361 GALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-RVL------- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 qigIVEQEPVLFSTTIAENIRY--GREDATMEDIVQAAKEANaynfimdLP--------------------QQfdtlvge 554
Cdd:COG4178 430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGhlaerldeeadwdqvlslgeQQ------- 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 555 gggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR 616
Cdd:COG4178 493 -----------RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1093-1278 |
3.95e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.17 E-value: 3.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1093 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQF---LRSN-IGIVSQ-EPVLFA 1167
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIKygdntkeipMERVIAAAKQAQLHD--FVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:PRK11629 102 FTALENVA---------MPLLIGKKKPAEINSraLEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190
....*....|....*....|....*....|....*
gi 21536378 1246 TSALDTESEKTVQVALDK--AREGRTCIVIAHRLS 1278
Cdd:PRK11629 173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1099-1298 |
4.28e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1099 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH------DSKkvnVQFLRSNIGIVSQEPVlfaCSIMD 1172
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlsPGK---LQALRRDIQFIFQDPY---ASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKYGDNTKEiPMeRV-------IAAAKQAQLHDFVMSLPE---KYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK10261 417 RQTVGDSIME-PL-RVhgllpgkAAAARVAWLLERVGLLPEhawRYP-------HEFSGGQRQRICIARALALNPKVIIA 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1243 DEATSALDTE-SEKTVQVALDKARE-GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 1298
Cdd:PRK10261 488 DEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
440-647 |
4.39e-17 |
|
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: 84.39 E-value: 4.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 440 DLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS------LNIQwlRDQIGIVEQEPVLFS-TTI 512
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPE--KRRIGYVFQEARLFPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 513 AENIRYGREDATMEDiVQAAKEAnaynfIMDLpQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNE 592
Cdd:TIGR02142 93 RGNLRYGMKRARPSE-RRISFER-----VIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 593 SEAMVQEVLSKIqHGHT---IISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 647
Cdd:TIGR02142 166 RKYEILPYLERL-HAEFgipILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
420-617 |
5.56e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 81.55 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTF---HYPSRpevkilndLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlRD 496
Cdd:PRK10771 2 LKLTDITWlyhHLPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFS-TTIAENIRYG---------REDATMEDIvqaAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQR 566
Cdd:PRK10771 72 PVSMLFQENNLFShLTVAQNIGLGlnpglklnaAQREKLHAI---ARQMGIEDLLARLPGQL-----------SGGQRQR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 567 VAIARALIRNPKILLLDMATSALD----NESEAMVQEVLSKIQhgHTIISVAHRL 617
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQ--LTLLMVSHSL 190
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
419-639 |
6.72e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 6.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 419 EIEFHNVTFHYPSRPEVKilnDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQ- 492
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 493 -WLRDQIGIVEQEPVLFSTTIAENIRYGRE----DATMEDIVQAA-KEANAYNFIMD-LPQQFDTLvgegggqmSGGQKQ 565
Cdd:PRK14243 87 vEVRRRIGMVFQKPNPFPKSIYDNIAYGARingyKGDMDELVERSlRQAALWDEVKDkLKQSGLSL--------SGGQQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 566 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 639
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGG 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
420-590 |
7.00e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 83.98 E-value: 7.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTfhyPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRD-QI 498
Cdd:PRK10851 3 IEIANIK---KSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFS-TTIAENIRYG------REDATME----------DIVQAAKEANAYnfimdlPQQFDtlvgegggqmsG 561
Cdd:PRK10851 77 GFVFQHYALFRhMTVFDNIAFGltvlprRERPNAAaikakvtqllEMVQLAHLADRY------PAQLS-----------G 139
|
170 180
....*....|....*....|....*....
gi 21536378 562 GQKQRVAIARALIRNPKILLLDMATSALD 590
Cdd:PRK10851 140 GQKQRVALARALAVEPQILLLDEPFGALD 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1096-1306 |
7.69e-17 |
|
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: 85.24 E-value: 7.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-------MIDGHDSKKVNVQFLRSNIGIVSQEPVLFA- 1167
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIkygdnTKEIPMERVIAAAKQAQLHDFVMS-LPEKYETNVGSQ-GSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:TIGR03269 380 RTVLDNL-----TEAIGLELPDELARMKAVITLKMVgFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1246 TSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1099-1305 |
8.43e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 82.14 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1099 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPvlfACSIMDNIKYGD 1178
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP---STSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1179 --------NTKEIPMER---VIAAAKQAQLhdfvmsLPEkyetNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:PRK15112 109 ildfplrlNTDLEPEQRekqIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1248 ALD-TESEKTVQVALD-KAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PRK15112 179 SLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
790-995 |
8.82e-17 |
|
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: 82.53 E-value: 8.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 790 EQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQ 869
Cdd:cd18575 30 GNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 870 GAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPF----LALSGATQTRMltgfaSRDKQ-ALEMVGQITNEAL 944
Cdd:cd18575 108 TVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLvvlpIILFGRRVRRL-----SRASQdRLADLSAFAEETL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536378 945 SNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIA 995
Cdd:cd18575 183 SAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGA 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
420-643 |
9.78e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL--RDQ 497
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEP--VLFSTTIAENIRYG------REDATMEDIVQAAKEANAYNFIMDLPQQFdtlvgegggqmSGGQKQRVAI 569
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPHHL-----------SGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 643
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1096-1301 |
1.14e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVSQEPVLF-ACSI 1170
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIrsprDAIALGIGMVHQHFMLVpNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYGDNTKEIPMERVIAAAKQaqlhdfVMSLPEKY------ETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVE----DLSVGEQQRVEILKALYRGARILILDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1245 ATSALdTESE-KTVQVALDK-AREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIekGTHE 1301
Cdd:COG3845 168 PTAVL-TPQEaDELFEILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKVV--GTVD 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1085-1275 |
1.57e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHdskkvnvqfLRsnIGIVSQEPV 1164
Cdd:COG0488 6 KSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFA-CSIMDNIKYGDN---TKEIPMERVIAA--------AKQAQLHDFVMSL-------------------PEKYETNVG 1213
Cdd:COG0488 72 LDDdLTVLDTVLDGDAelrALEAELEELEAKlaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDLDRPVS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1214 SqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES----EKTVqvaldKAREGrTCIVIAH 1275
Cdd:COG0488 152 E----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSH 207
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1095-1275 |
1.69e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 80.21 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQ---FLRS-NIGIVSQE----PVLF 1166
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRAkHVGFVFQSfmliPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 AcsiMDNIKY-----GDNTKEiPMERVIAAAKQAQLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PRK10584 105 A---LENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 21536378 1242 LDEATSALDTES-EKTVQVALDKARE-GRTCIVIAH 1275
Cdd:PRK10584 170 ADEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTH 205
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
420-645 |
1.77e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.70 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHY-PSRP-EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQW 493
Cdd:PRK13643 2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 494 LRDQIGIVEQEP--VLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVAIAR 571
Cdd:PRK13643 82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPK-EKAEKIAAEKLEMVGLADEF---WEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 572 ALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 645
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1092-1301 |
1.82e-16 |
|
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: 79.11 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGKVMIDGHDSKKVNVQfLRSNIGI--VSQEPVlfa 1167
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 csimdnikygdntkEIPMERVIaaakqaqlhDFVMSLpekyetNVGsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:cd03217 88 --------------EIPGVKNA---------DFLRYV------NEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1248 ALDTESEKTVQVALDKAR-EGRTCIVIAH--RLSTIQNADIIAVMAQGVVIEKGTHE 1301
Cdd:cd03217 134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1094-1306 |
1.92e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKS-TSIQLLERFYDPD----QGKVMIDGHDSKKVNVQFLR----SNIGIVSQEP- 1163
Cdd:PRK15134 23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1164 ---------------VLfacSIMDNIKYGDNTKEI--PMERV-IAAAKQaQLHDFvmslPEkyetnvgsqgsQLSRGEKQ 1225
Cdd:PRK15134 103 vslnplhtlekqlyeVL---SLHRGMRREAARGEIlnCLDRVgIRQAAK-RLTDY----PH-----------QLSGGERQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1226 RIAIARAIVRDPKILLLDEATSALDTesekTVQVA-LDKARE-----GRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKG 1298
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDV----SVQAQiLQLLRElqqelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQN 239
|
....*...
gi 21536378 1299 THEELMAQ 1306
Cdd:PRK15134 240 RAATLFSA 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
421-627 |
2.18e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 79.45 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 421 EFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGHDIRSLNIQwlRDQ 497
Cdd:COG4136 3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFS-TTIAENIRYG---------REDAtmedIVQAAKEANAYNFIMDLPqqfDTLvgegggqmSGGQKQRV 567
Cdd:COG4136 78 IGILFQDDLLFPhLSVGENLAFAlpptigraqRRAR----VEQALEEAGLAGFADRDP---ATL--------SGGQRARV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 568 AIARALIRNPKILLLDMATSALDNESEAMVQE-VLSKI-QHGHTIISVAHRLSTVRAADTII 627
Cdd:COG4136 143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREfVFEQIrQRGIPALLVTHDEEDAPAAGRVL 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
415-644 |
2.28e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 80.80 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 415 RIKGEiefhNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL 494
Cdd:PRK10253 7 RLRGE----QLTLGYGKY---TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 495 RDQIGIVEQEPVL-FSTTIAENIRYGR------------EDatmEDIVQAAKEANAynfIMDLP-QQFDTLvgegggqmS 560
Cdd:PRK10253 80 ARRIGLLAQNATTpGDITVQELVARGRyphqplftrwrkED---EEAVTKAMQATG---ITHLAdQSVDTL--------S 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 561 GGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVER 637
Cdd:PRK10253 146 GGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQ 225
|
....*..
gi 21536378 638 GTHEELL 644
Cdd:PRK10253 226 GAPKEIV 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1092-1301 |
2.37e-16 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 80.11 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL---ERfYDPDQGKVMIDGHD---------SKK------------- 1146
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDilelspderARAgiflafqypveip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1147 -VNV-QFLRSNIGIVSQEPVlfacSIMDNIKygdntkeipmeRVIAAAKQaqlhdfvMSLPEKY---ETNVGsqgsqLSR 1221
Cdd:COG0396 91 gVSVsNFLRTALNARRGEEL----SAREFLK-----------LLKEKMKE-------LGLDEDFldrYVNEG-----FSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1222 GEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAH--RLSTIQNADIIAVMAQGVVIEKG 1298
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
...
gi 21536378 1299 THE 1301
Cdd:COG0396 224 GKE 226
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1095-1305 |
3.27e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.53 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDP-----DQGKVMIDGHDSKKV-NVQFLRSNIGIVSQEPVLFAC 1168
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNIKYGDNTKEIPMERVIAAAKQAQLHDfvMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSA 1248
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1249 LDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
436-644 |
3.36e-16 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.06 E-value: 3.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVL-FSTTIAE 514
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 515 NIRYGR------------EDatmEDIVQAAKEANaynfimdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLL 582
Cdd:PRK11231 96 LVAYGRspwlslwgrlsaED---NARVNQAMEQT----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 583 DMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
435-626 |
3.41e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 83.18 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 435 VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGI--VEQEPVLF-STT 511
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 512 IAENIRYG--REDATMEDIVQAAKEANAYnfiMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPKILLLDMATSAL 589
Cdd:PRK15439 103 VKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSL--------EVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 21536378 590 D-NESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTI 626
Cdd:PRK15439 172 TpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRI 210
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1110-1302 |
3.46e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.84 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1110 AFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH---DS-KKVNVQFLRSNIGIVSQEPVLFA-CSIMDNIKYGdntkeip 1184
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPhYKVRGNLRYG------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1185 mervIAAAKQAQLHDFVM-----SLPEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQV 1259
Cdd:PRK11144 101 ----MAKSMVAQFDKIVAllgiePLLDRYP-------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 1260 ALDK-AREGRTCIV-IAHRLSTI-QNADIIAVMAQGVVIEKGTHEE 1302
Cdd:PRK11144 170 YLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1094-1277 |
3.50e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 80.90 E-value: 3.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMI---DGHDSKKV---------------------NV 1149
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTkekekvleklviqktrfkkikKI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1150 QFLRSNIGIVSQ--EPVLFACSIMDNIKYGDNTKEIPMERviaAAKQAQLHDFVMSLPEKYetnvgSQGS--QLSRGEKQ 1225
Cdd:PRK13651 101 KEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEE---AKKRAAKYIELVGLDESY-----LQRSpfELSGGQKR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1226 RIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKA-REGRTCIVIAHRL 1277
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDL 225
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1092-1305 |
3.97e-16 |
|
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: 79.26 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFLRSN------IGIVSQEPVL 1165
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----ITGLPPHriarlgIGYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 FA-CSIMDNIkygdntkEIPMERVIAAAKQAQLHDFVMSL-PEKYEtNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:COG0410 90 FPsLTVEENL-------LLGAYARRDRAEVRADLERVYELfPRLKE-RRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1244 EATSALdteSEKTVQVALDK----AREGRTCIVI---AHRLSTIqnADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:COG0410 162 EPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1099-1299 |
4.16e-16 |
|
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: 84.68 E-value: 4.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1099 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKkVNVQFLRSNIGIVSQEPVLFA-CSIMDNIKYG 1177
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHhLTVAEHILFY 1027
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1178 DNTKEIPMErviaaakQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV 1257
Cdd:TIGR01257 1028 AQLKGRSWE-------EAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 1258 QVALDKAREGRTCIVIAHRLStiqNADI----IAVMAQGVVIEKGT 1299
Cdd:TIGR01257 1101 WDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-644 |
4.72e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 79.71 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQWLRDQIGIVEQEPVLFS- 509
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 510 TTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSAL 589
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 590 DNESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK14246 185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
168-364 |
4.87e-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: 80.07 E-value: 4.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 168 ARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTI--CGFLLGFfrGWKLTLVI 245
Cdd:cd18590 65 SRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLgmLGFMLSL--SWQLTLLT 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 246 ISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFF 325
Cdd:cd18590 143 LIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVY 222
|
170 180 190
....*....|....*....|....*....|....*....
gi 21536378 326 TGFVWCLIFLCYALAFWYGSTLvLDEGEYTPGTLVQIFL 364
Cdd:cd18590 223 LLVRRVLQLGVQVLMLYCGRQL-IQSGHLTTGSLVSFIL 260
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
778-1009 |
5.34e-16 |
|
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: 80.15 E-value: 5.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 778 QILGTF--SIPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPG 855
Cdd:cd18541 20 RIIGRAidALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQ--KNRTG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 856 ALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTgfaSRDKQALEM 935
Cdd:cd18541 98 DLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIH---KRFRKVQEA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 936 VGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISN 1009
Cdd:cd18541 175 FSDLSDrvqESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIR 251
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
420-641 |
7.19e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 78.52 E-value: 7.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH------DIRSLNIQW 493
Cdd:PRK11124 3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfskTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 494 LRDQIGIVEQEPVLFS-TTIAENIRygreDATME----DIVQAAKEAN-----------AYNFIMDLP---QQfdtlvge 554
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLI----EAPCRvlglSKDQALARAEkllerlrlkpyADRFPLHLSggqQQ------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 555 gggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH-GHTIISVAHRLSTVR-AADTIIGFEHG 632
Cdd:PRK11124 149 -----------RVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARkTASRVVYMENG 217
|
....*....
gi 21536378 633 TAVERGTHE 641
Cdd:PRK11124 218 HIVEQGDAS 226
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
138-360 |
7.92e-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: 7.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 138 MIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQM 217
Cdd:cd18544 40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 218 ALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIgaatiglSVSKFTDYELKAYAKA-GVVAD------EVISSMRT 290
Cdd:cd18544 120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL-------ATYLFRKKSRKAYREVrEKLSRlnaflqESISGMSV 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 291 VAAFGGEKREVERYEK---NLVFAQRWGIRkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18544 193 IQLFNREKREFEEFDEinqEYRKANLKSIK---LFALFRPLVELLSSLALALVLWYGGGQVLS-GAVTLGVLY 261
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
420-645 |
8.21e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.03 E-value: 8.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVkilNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRdQIG 499
Cdd:PRK11607 20 LEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQR-PIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFS-TTIAENIRYG-REDATMEDIVQAAKE-----ANAYNFIMDLPQQFDtlvgegggqmsGGQKQRVAIARA 572
Cdd:PRK11607 95 MMFQSYALFPhMTVEQNIAFGlKQDKLPKAEIASRVNemlglVHMQEFAKRKPHQLS-----------GGQRQRVALARS 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 573 LIRNPKILLLDMATSALDNE-SEAMVQEVLSKIQH-GHTIISVAH-RLSTVRAADTIIGFEHGTAVERGTHEELLE 645
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKlRDRMQLEVVDILERvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1085-1313 |
8.34e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 83.25 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPdqgkvMIDGHdskkvnvQFLRSNIGIVSQEPV 1164
Cdd:PLN03130 622 FSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP-----RSDAS-------VVIRGTVAYVPQVSW 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFACSIMDNIKYGDNTKEIPMERVIAAAkqAQLHDFVMsLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PLN03130 690 IFNATVRDNILFGSPFDPERYERAIDVT--ALQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1245 ATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:PLN03130 767 PLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
434-633 |
8.97e-16 |
|
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: 77.86 E-value: 8.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDgHDIRSLNI------QWL---RDQIGIVEQe 504
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR-HDGGWVDLaqasprEILalrRRTIGYVSQ- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 505 pvlFSTTI---------AENIRygrEDATMEDIVQA-AKEANAYnfiMDLP---------------QQfdtlvgegggqm 559
Cdd:COG4778 101 ---FLRVIprvsaldvvAEPLL---ERGVDREEARArARELLAR---LNLPerlwdlppatfsggeQQ------------ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 560 sggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGT 633
Cdd:COG4778 160 ------RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIeEAKARGTAIIGIFHDEEVREAvADRVVDVTPFS 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
420-643 |
9.16e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 9.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVK---ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW-LR 495
Cdd:PRK13633 5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 496 DQIGIVEQEP--VLFSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRV 567
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPEnlgippEEIRERVDESLKKVGMYEYRRHAPHLLS-----------GGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 568 AIARALIRNPKILLLDMATSALDNESEamvQEVLSKIQ-----HGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEE 642
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGR---REVVNTIKelnkkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKE 230
|
.
gi 21536378 643 L 643
Cdd:PRK13633 231 I 231
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
437-645 |
9.50e-16 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.06 E-value: 9.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKSTA----LQLIqrfydPCEGMVTVDGHDIRSLNIQWL---RDQIGIVEQEP---- 505
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTglalLRLI-----NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssl 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 506 -----VLfsTTIAENIRY--------GRED---ATMEDIVQAAKEANAYnfimdlPQQFDtlvgegggqmsGGQKQRVAI 569
Cdd:PRK15134 376 nprlnVL--QIIEEGLRVhqptlsaaQREQqviAVMEEVGLDPETRHRY------PAEFS-----------GGQRQRIAI 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTI--ISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 645
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-365 |
9.90e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 79.48 E-value: 9.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQM-ALFIQRM 224
Cdd:cd18563 50 AGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLpDFLTNIL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 225 TSTICGFLLgFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAK-AGVVADeVISSMRTVAAFGGEKREVER 303
Cdd:cd18563 130 MIIGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRlNSVLND-TLPGIRVVKAFGQEKREIKR 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 304 YEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVQiFLS 365
Cdd:cd18563 208 FDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLS-GTMTLGTLVA-FLS 267
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
420-647 |
1.17e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 499
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVL-FSTTIAENI----RYGREDA-TMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGgqkqRVAIARAL 573
Cdd:PRK13536 118 VVPQFDNLdLEFTVRENLlvfgRYFGMSTrEIEAVIPSLLE------FARLESKADARVSDLSGGMKR----RLTLARAL 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1103-1303 |
1.22e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.46 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1103 ISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVN-VQFLRSNIGIVSQEPVLFA-CSIMDNIKYG--- 1177
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNdVPPAERGVGMVFQSYALYPhLSVAENMSFGlkl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1178 --DNTKEIPmERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEK 1255
Cdd:PRK11000 103 agAKKEEIN-QRVNQVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1256 TVQVALDK--AREGRTCIVIAH-RLSTIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK11000 171 QMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
420-633 |
1.32e-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: 75.18 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdGHDIRslniqwlrdqIG 499
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQepvlFSttiaeniryGREDAtmedivqaakeanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIRNPKI 579
Cdd:cd03221 67 YFEQ----LS---------GGEKM------------------------------------------RLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQhgHTIISVAH-R--LSTVraADTIIGFEHGT 633
Cdd:cd03221 92 LLLDEPTNHLDLESIEALEEALKEYP--GTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
420-620 |
1.57e-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: 76.51 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQ-LIQRFYD-PCEGMVTVDGhdiRSLNIQWLRd 496
Cdd:cd03232 4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAgVITGEILING---RPLDKNFQR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFST-TIAENIRYgreDATMEDIVQAAKEanaynfimdlpqqfdtlvgegggqmsggqkqRVAIARALIR 575
Cdd:cd03232 80 STGYVEQQDVHSPNlTVREALRF---SALLRGLSVEQRK-------------------------------RLTIGVELAA 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 576 NPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV 620
Cdd:cd03232 126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQAILCTIHQPSAS 171
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
145-365 |
1.66e-15 |
|
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: 79.09 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 145 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQ-MALFIQr 223
Cdd:cd18564 60 LVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGvLPLLTN- 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 224 mTSTICGFL-LGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVE 302
Cdd:cd18564 139 -LLTLVGMLgVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEER 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 303 RYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLVqIFLS 365
Cdd:cd18564 218 RFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLA-GRLTPGDLL-VFLA 278
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
424-644 |
1.84e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.70 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL-------------N 490
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 491 IQWLRDQIGIVEQEPVLFS-TTIAENIrygredatMEDIVQA-------AKEANAynFIMDLPQQFDTLVGEGGGQMSGG 562
Cdd:PRK10619 87 LRLLRTRLTMVFQHFNLWShMTVLENV--------MEAPIQVlglskqeARERAV--KYLAKVGIDERAQGKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 563 QKQRVAIARALIRNPKILLLDMATSALDNEseaMVQEVLSKIQH----GHTIISVAHRLSTVRAADTIIGFEH-GTAVER 637
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPE---LVGEVLRIMQQlaeeGKTMVVVTHEMGFARHVSSHVIFLHqGKIEEE 233
|
....*..
gi 21536378 638 GTHEELL 644
Cdd:PRK10619 234 GAPEQLF 240
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
431-644 |
1.96e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.27 E-value: 1.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 431 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVL-FS 509
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 510 TTIAENIRYGR---------EDATMEDIVQAAKEANAYNFIMDLPqqFDTLvgegggqmSGGQKQRVAIARALIRNPKIL 580
Cdd:PRK09536 92 FDVRQVVEMGRtphrsrfdtWTETDRAAVERAMERTGVAQFADRP--VTSL--------SGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 581 LLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK09536 162 LLDEPTASLDiNHQVRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1095-1318 |
2.26e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.43 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvNVQFL-------------RSNIgivsq 1161
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALlelgagfhpeltgRENI----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1162 epvLFACSIMdnikyGDNTKEIP--MERVIAAAkqaQLHDFvMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIVRDPKI 1239
Cdd:COG1134 110 ---YLNGRLL-----GLSRKEIDekFDEIVEFA---ELGDF-IDQPVKT----------YSSGMRARLAFAVATAVDPDI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1240 LLLDEATSALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAqkgAYYKLVTTG 1317
Cdd:COG1134 168 LLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLAGR 244
|
.
gi 21536378 1318 S 1318
Cdd:COG1134 245 E 245
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
420-644 |
2.33e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST-TIAENIRYGR----------EDatmEDIVQaakEANAYNFIMDLPQQF-DTLvgegggqmsggqkqRV 567
Cdd:COG4604 79 ILRQENHINSRlTVRELVAFGRfpyskgrltaED---REIID---EAIAYLDLEDLADRYlDELsgg--------qrqRA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 568 AIARALIRNPKILLLDMATSALD-NESEAMVQeVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEEL 643
Cdd:COG4604 145 FIAMVLAQDTDYVLLDEPLNNLDmKHSVQMMK-LLRRLadELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPEEI 223
|
.
gi 21536378 644 L 644
Cdd:COG4604 224 I 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
434-638 |
2.76e-15 |
|
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: 76.10 E-value: 2.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLRdQIGIVEQEPVLF-STTI 512
Cdd:cd03268 12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALR-RIGALIEAPGFYpNLTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 513 AENIR-----YGREDATME---DIV----QAAKEANAYNFIMdlpQQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 580
Cdd:cd03268 90 RENLRllarlLGIRKKRIDevlDVVglkdSAKKKVKGFSLGM---KQ------------------RLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 581 LLDMATSALDNESEAMVQE-VLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 638
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRElILSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1096-1313 |
3.00e-15 |
|
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: 76.74 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVnvqflrsnigivsQEP-----VLFacsi 1170
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG---KQI-------------TEPgpdrmVVF---- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 mdnikygDNTKEIPMERV---IAAAKQAQLHDfvMSLPEKYETN------VGSQGS------QLSRGEKQRIAIARAIVR 1235
Cdd:TIGR01184 61 -------QNYSLLPWLTVrenIALAVDRVLPD--LSKSERRAIVeehialVGLTEAadkrpgQLSGGMKQRVAIARALSI 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1236 DPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRL-STIQNADIIAVMAQG----------VVIEKGTHEE 1302
Cdd:TIGR01184 132 RPKVLLLDEPFGALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGpaanigqileVPFPRPRDRL 211
|
250
....*....|.
gi 21536378 1303 LMAQKGAYYKL 1313
Cdd:TIGR01184 212 EVVEDPSYYDL 222
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
785-1012 |
3.25e-15 |
|
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: 77.81 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 785 IPDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATD 864
Cdd:cd18544 30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTND 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 865 ASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGAT-QTRMLTGF-ASRDKQAlEMVGQItNE 942
Cdd:cd18544 108 TEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLfRKKSRKAYrEVREKLS-RLNAFL-QE 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 943 ALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 1012
Cdd:cd18544 186 SISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAV 255
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1086-1318 |
3.27e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.54 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRPDS-QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVN----VQFLRSNIGIVS 1160
Cdd:PRK10535 13 SYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLRREHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1161 QEPVLFA-CSIMDNIkygdntkEIP-----MERviaAAKQAQLHDFVMSLpeKYETNVGSQGSQLSRGEKQRIAIARAIV 1234
Cdd:PRK10535 93 QRYHLLShLTAAQNV-------EVPavyagLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1235 RDPKILLLDEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGTEPV 240
|
....*
gi 21536378 1314 VTTGS 1318
Cdd:PRK10535 241 VNTAS 245
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
1093-1303 |
5.10e-15 |
|
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: 76.02 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1093 SQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CSI 1170
Cdd:TIGR03410 13 SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDiTKLPPHERARAGIAYVPQGREIFPrLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYG-----DNTKEIPmerviaaakqaqlhDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:TIGR03410 93 EENLLTGlaalpRRSRKIP--------------DEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1246 TSALDTESEKTVQVALDK--AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:TIGR03410 159 TEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
418-666 |
6.00e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 76.97 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYPSRP--EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI-----RSLN 490
Cdd:PRK13645 5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 491 IQWLRDQIGIVEQEP--VLFSTTIAENIRYGREDATmEDIVQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVA 568
Cdd:PRK13645 85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 569 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG------T 639
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnkEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfeifS 240
|
250 260 270
....*....|....*....|....*....|..
gi 21536378 640 HEELL-----ERKGVYFTLVTLQSQGNQALNE 666
Cdd:PRK13645 241 NQELLtkieiDPPKLYQLMYKLKNKGIDLLNK 272
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
424-647 |
6.96e-15 |
|
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: 75.64 E-value: 6.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-RDQIGIVE 502
Cdd:TIGR03410 5 NLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 503 QEPVLFST-TIAENIRYGREdatmediVQAAKEANAYNFIMDL-P-----------------QQfdtlvgegggqmsggq 563
Cdd:TIGR03410 82 QGREIFPRlTVEENLLTGLA-------ALPRRSRKIPDEIYELfPvlkemlgrrggdlsggqQQ---------------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 564 kqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTH 640
Cdd:TIGR03410 139 --QLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLraEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAG 216
|
....*..
gi 21536378 641 EELLERK 647
Cdd:TIGR03410 217 DELDEDK 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1095-1280 |
7.16e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.28 E-value: 7.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnVQFL----RSN-IGIVSQEPVLFAC- 1168
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKD-----VTKLpeykRAKyIGRVFQDPMMGTAp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 --SIMDN------------IKYGDNTKEIPMERviaaakqAQLHDFVMSLPEKYETNVGSqgsqLSRGEKQRIAIARAIV 1234
Cdd:COG1101 96 smTIEENlalayrrgkrrgLRRGLTKKRRELFR-------ELLATLGLGLENRLDTKVGL----LSGGQRQALSLLMATL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 1235 RDPKILLLDEATSALDTeseKTVQVALDKAREgrtcIVIAHRLSTI 1280
Cdd:COG1101 165 TKPKLLLLDEHTAALDP---KTAALVLELTEK----IVEENNLTTL 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
433-626 |
8.57e-15 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.82 E-value: 8.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 433 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDGHDIRSLNIqwlRDQ----IGIVEQEP 505
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNI---RDTeragIAIIHQEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 506 VLFST-TIAENIRYGRE--------DATM----EDIVQAAK-EANAYNFIMDLP---QQFdtlvgegggqmsggqkqrVA 568
Cdd:PRK13549 92 ALVKElSVLENIFLGNEitpggimdYDAMylraQKLLAQLKlDINPATPVGNLGlgqQQL------------------VE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 569 IARALIRNPKILLLDMATSALdNESEAmvqEVLSKI-----QHGHTIISVAHRLSTVRA-ADTI 626
Cdd:PRK13549 154 IAKALNKQARLLILDEPTASL-TESET---AVLLDIirdlkAHGIACIYISHKLNEVKAiSDTI 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1095-1299 |
8.97e-15 |
|
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: 75.45 E-value: 8.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRsNIGIV--SQEPVLFACSIMD 1172
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKYGDNTKEIPMERviAAAKQAQLHDfVMSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:cd03267 115 SFYLLAAIYDLPPAR--FKKRLDELSE-LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536378 1253 SEKTVQVALDKAREGRTCIVIahrLSTIQNADIIAVMAQGVVIEKGT 1299
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVL---LTSHYMKDIEALARRVLVIDKGR 231
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1094-1292 |
9.99e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 9.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSN-IGIVSQE-PVLFACSIM 1171
Cdd:PRK09700 19 HALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 DNIKYGDN-TKEIPMERVIAAAK---QAQLHDFVMSLPEKYETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATS 1247
Cdd:PRK09700 99 ENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 21536378 1248 AL-DTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQG 1292
Cdd:PRK09700 175 SLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
422-593 |
1.04e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 422 FHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhDIRslniqwlrdqIGIV 501
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 502 EQEPVLFST-TIAENIR----------------YGREDATMEDIVQAAK------EANAYNF------IM--------DL 544
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLdgdaelraleaeleelEAKLAEPDEDLERLAElqeefeALGGWEAearaeeILsglgfpeeDL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536378 545 PQQFDTL-----VgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNES 593
Cdd:COG0488 147 DRPVSELsggwrR-------------RVALARALLSEPDLLLLDEPTNHLDLES 187
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
789-1244 |
1.39e-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: 78.30 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 789 EEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDLRNSpgALTTRLATDASQV 868
Cdd:COG4615 41 NATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAA--RLLAALTEDVRTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 869 QGAAgSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFfpfLALSGATQTRMLtgfaSRDKQALEMVGQITNEALSNIR 948
Cdd:COG4615 119 SQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL---LGLGVAGYRLLV----RRARRHLRRAREAEDRLFKHFR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 949 TVAGIGKE------RRfiEALeteLEKPFKTAIQKA--------NIYGFCFAFAQCIMFIansasyryggyLIsneGL-- 1012
Cdd:COG4615 191 ALLEGFKElklnrrRR--RAF---FDEDLQPTAERYrdlriradTIFALANNWGNLLFFA-----------LI---GLil 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1013 ----HFSYVF-RVISAVVL----SATALGRAFSYTPSYAKAKISAARFFQL---LDRQPPISVYNTAGEKWDNFQgKIDF 1080
Cdd:COG4615 252 fllpALGWADpAVLSGFVLvllfLRGPLSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLEL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1081 VDCKFTYPSRPDSQ--VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGI 1158
Cdd:COG4615 331 RGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1159 VSQEPVLFacsimDNIkYGDNTKEIPmERVIAAAKQAQLHDFVmslpeKYETNVGSQgSQLSRGEKQRIAIARAIVRDPK 1238
Cdd:COG4615 411 VFSDFHLF-----DRL-LGLDGEADP-ARARELLERLELDHKV-----SVEDGRFST-TDLSQGQRKRLALLVALLEDRP 477
|
....*.
gi 21536378 1239 ILLLDE 1244
Cdd:COG4615 478 ILVFDE 483
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
774-1050 |
1.41e-14 |
|
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: 75.90 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 774 FLFSQILGTFSIPD----------KEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQD 843
Cdd:cd18548 7 FKLLEVLLELLLPTlmadiidegiANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 844 IAWFDDLrnSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLT 923
Cdd:cd18548 87 FAEIDKF--GTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 924 GFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYG 1003
Cdd:cd18548 165 PLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFG 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1004 GYLISNEGLHF-------SYVFRVISAVVLSATALGrafsytpSYAKAKISAAR 1050
Cdd:cd18548 245 GHLINAGSLQVgdlvafiNYLMQILMSLMMLSMVFV-------MLPRASASAKR 291
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
436-643 |
1.42e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 76.67 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN-IQWL--RDQIGIVEQEPvLFSTT- 511
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDP-LASLNp 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 512 -------IAENIRYGREDATMEDIVQAAKEANAY-----NFIMDLPQQFdtlvgegggqmSGGQKQRVAIARALIRNPKI 579
Cdd:PRK15079 114 rmtigeiIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEF-----------SGGQCQRIGIARALILEPKL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 580 LLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFEHGTAVERGTHEEL 643
Cdd:PRK15079 183 IICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
420-645 |
1.44e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYD-----PCEGMVTVDGHDIRSLNIQWL 494
Cdd:PRK14267 5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 495 --RDQIGIVEQEPVLFS-TTIAENIRYG-------REDATMEDIVQ-AAKEANAY----NFIMDLPQQFDtlvgegggqm 559
Cdd:PRK14267 82 evRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDERVEwALKKAALWdevkDRLNDYPSNLS---------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 560 sGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHR-LSTVRAADTIIGFEHGTAVERG 638
Cdd:PRK14267 152 -GGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
....*..
gi 21536378 639 THEELLE 645
Cdd:PRK14267 231 PTRKVFE 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
420-646 |
1.67e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.22 E-value: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYpsRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEP--VLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFImdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 577
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 578 KILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLER 646
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLpeTYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
420-627 |
1.69e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 78.23 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPE-VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---- 494
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 495 RDQIGIVEQEPVLFS-TTIAENIRYgreDATMEDIVQAAKEANAYNFIMDL---------PQQFDtlvgegggqmsGGQK 564
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRLgledrveyqPSQLS-----------GGQQ 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 565 QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRAADTII 627
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLrDRGHTVIIVTHDPQVAAQAERVI 214
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
131-531 |
1.75e-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: 77.92 E-value: 1.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 131 LLNIESEMIKFASYYAGIAVAVLITGYIQicfwVIAAARQIQ----KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDI 206
Cdd:COG4615 40 LNATGAALARLLLLFAGLLVLLLLSRLAS----QLLLTRLGQhavaRLRLRLSRRILAAPLERLERIGAARLLAALTEDV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 207 NKINDAIAdQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVsplIGIGAATIGLSVSKFtdyeLKAYAKAGVVADEVIS 286
Cdd:COG4615 116 RTISQAFV-RLPELLQSVALVLGCLAYLAWLSPPLFLLTLVL---LGLGVAGYRLLVRRA----RRHLRRAREAEDRLFK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 287 SMRTVaaFGG--------EKRE----------VERYEKNLVFAQRWgirkgivmgFFTGFVW--CLIFLCYALAFWYGST 346
Cdd:COG4615 188 HFRAL--LEGfkelklnrRRRRaffdedlqptAERYRDLRIRADTI---------FALANNWgnLLFFALIGLILFLLPA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 347 LVLDEGEYTPG-TLVQIF----LSVIVGALnlgnasPcleAFATGRAAATSIfETIDRKpiIDCMSEDGYKLDRIK---- 417
Cdd:COG4615 257 LGWADPAVLSGfVLVLLFlrgpLSQLVGAL------P---TLSRANVALRKI-EELELA--LAAAEPAAADAAAPPapad 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 -GEIEFHNVTFHYPSRPEVK--ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL 494
Cdd:COG4615 325 fQTLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAY 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 21536378 495 RDQIGIVEQEPVLFSTTiaenirYGREDATMEDIVQA 531
Cdd:COG4615 405 RQLFSAVFSDFHLFDRL------LGLDGEADPARARE 435
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1096-1292 |
1.80e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDGHDSKKVNVQFL-RSNIGIVSQEPVLFA-CSI 1170
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTeRAGIAIIHQELALVKeLSV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYGDNTKE---IPMERVIAAAKQ--AQLhdfvmslpeKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEA 1245
Cdd:PRK13549 100 LENIFLGNEITPggiMDYDAMYLRAQKllAQL---------KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536378 1246 TSALdTESEKTVQVAL--DKAREGRTCIVIAHRLSTIQN-ADIIAVMAQG 1292
Cdd:PRK13549 171 TASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
420-638 |
2.11e-14 |
|
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: 73.47 E-value: 2.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIG 499
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLF-STTIAENIRYGREDATMEdIVQAAKEANAYNFIMDLP----QQFDTLvgegggqmSGGQKQRVAIARALI 574
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYLAQLKGLK-KEEARRRIDEWLERLELSeyanKRVEEL--------SKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 575 RNPKILLLDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTV-RAADTIIGFEHGTAVERG 638
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
424-646 |
2.43e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 75.77 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPSR-----PE--VKILNDLNMVIKPGEMTALVGPSGAGKST---ALQLIQRfydPCEGMVTVDGHDIRSLN--- 490
Cdd:PRK11308 10 DLKKHYPVKrglfkPErlVKALDGVSFTLERGKTLAVVGESGCGKSTlarLLTMIET---PTGGELYYQGQDLLKADpea 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 491 IQWLRDQIGIVEQ-----------------EPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYnfimdlPQQFdtlvg 553
Cdd:PRK11308 87 QKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRY------PHMF----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 554 egggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFE 630
Cdd:PRK11308 156 ------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEhIADEVMVMY 229
|
250
....*....|....*.
gi 21536378 631 HGTAVERGTHEELLER 646
Cdd:PRK11308 230 LGRCVEKGTKEQIFNN 245
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
420-667 |
2.72e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 74.49 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHY------PSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--------- 484
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdyky 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 485 ---DIR--------SLNIqwlRDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQfdtlvg 553
Cdd:COG4167 85 rckHIRmifqdpntSLNP---RLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSSGQK------ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 554 egggqmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVR-AADTIIGFE 630
Cdd:COG4167 156 -----------QRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQekLGISYIYVSQHLGIVKhISDKVLVMH 224
|
250 260 270
....*....|....*....|....*....|....*..
gi 21536378 631 HGTAVERGTHEELLERKGVYFTLVTLQSQGNQALNEE 667
Cdd:COG4167 225 QGEVVEYGKTAEVFANPQHEVTKRLIESHFGEALTAD 261
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
432-611 |
2.86e-14 |
|
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: 73.46 E-value: 2.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 432 RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI---QRFYDPCEGMVTVDGhdiRSLNIQWLRDQIGIVEQEPVLF 508
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 ST-TIAENIRYGREDATMEDIVQAAKEANAYnfIMDLPQQFDTLVGEGGGQMSGG-QKQRVAIARALIRNPKILLLDMAT 586
Cdd:cd03234 94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVE--DVLLRDLALTRIGGNLVKGISGgERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180
....*....|....*....|....*
gi 21536378 587 SALDNESEAMVQEVLSKIQHGHTII 611
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIV 196
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1092-1250 |
4.16e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 73.94 E-value: 4.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMidghdSKKVNVQFLRSNIGIVSQEPVLFAC-SI 1170
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEAREDTRLMFQDARLLPWkKV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1171 MDNIKYGDNTKEIPmerviaAAKQA----QLHDFVMSLPekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:PRK11247 99 IDNVGLGLKGQWRD------AALQAlaavGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLLLLDEPL 161
|
....
gi 21536378 1247 SALD 1250
Cdd:PRK11247 162 GALD 165
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1099-1303 |
4.67e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 4.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1099 LSVSISPGQTLAFVGSSGCGKSTSIQLLERFYD-PdqGKVM-----IDGHD----SKKVNVQFLRSNIGIVSQEPV--LF 1166
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyP--GRVMaekleFNGQDlqriSEKERRNLVGAEVAMIFQDPMtsLN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 AC-----SIMDNIKY--GDNTKEiPMERVIAAAKQAQLHDFVMSLpEKYEtnvgsqgSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:PRK11022 104 PCytvgfQIMEAIKVhqGGNKKT-RRQRAIDLLNQVGIPDPASRL-DVYP-------HQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1240 LLLDEATSALD-TESEKTVQVALD-KAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK11022 175 LIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
438-620 |
4.74e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.99 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI---RSLNIQWLRDQIGIVEQE-PVLFSTTIA 513
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhHLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 514 ENIRYGR--EDATMEDI---VQAAKEA-----NAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKIL 580
Cdd:PRK10908 98 DNVAIPLiiAGASGDDIrrrVSAALDKvglldKAKNFPIQLSggeQQ------------------RVGIARAVVNKPAVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21536378 581 LLDMATSALDNE-SEAMVQ--EVLSKIqhGHTIISVAHRLSTV 620
Cdd:PRK10908 160 LADEPTGNLDDAlSEGILRlfEEFNRV--GVTVLMATHDIGLI 200
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1091-1306 |
4.84e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkVNVQF------LRSNIGIVSQE-- 1162
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG-----QEMRFasttaaLAAGVAIIYQElh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 --PVLfacSIMDNIKYGD--NTKEIPMERVIAAAKQAQLH----DFVMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIV 1234
Cdd:PRK11288 90 lvPEM---TVAENLYLGQlpHKGGIVNRRLLNYEAREQLEhlgvDIDPDTPLKY----------LSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1235 RDPKILLLDEATSALDT-ESEKTVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEkgTHEElMAQ 1306
Cdd:PRK11288 157 RNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDD-MAQ 227
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
420-616 |
4.84e-14 |
|
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: 71.42 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPS-RPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdpcegmvtvdghdirslniQWLRDQI 498
Cdd:cd03223 1 IELENLSLATPDgRV---LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-------------------PWGSGRI 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLF--------STTIAENIRYGREDATMEDivqaakEanaynfimdlpQQfdtlvgegggqmsggqkqRVAIA 570
Cdd:cd03223 59 GMPEGEDLLFlpqrpylpLGTLREQLIYPWDDVLSGG------E-----------QQ------------------RLAFA 103
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 571 RALIRNPKILLLDMATSALDNESEAMVQEVLSkiQHGHTIISVAHR 616
Cdd:cd03223 104 RLLLHKPKFVFLDEATSALDEESEDRLYQLLK--ELGITVISVGHR 147
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1089-1295 |
5.08e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNVQFLRSN----IGIVSQE-- 1162
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQEln 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 --PVLfacSIMDNIKYGDNTKE----IPMERVIAAAKQ--AQLhdfvmSLPEKYETNVGsqgsQLSRGEKQRIAIARAIV 1234
Cdd:PRK10762 90 liPQL---TIAENIFLGREFVNrfgrIDWKKMYAEADKllARL-----NLRFSSDKLVG----ELSIGEQQMVEIAKVLS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1235 RDPKILLLDEATSAL-DTESEKTVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVI 1295
Cdd:PRK10762 158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDGQFI 220
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
795-975 |
6.91e-14 |
|
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: 74.09 E-value: 6.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 795 INGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGS 874
Cdd:cd18564 53 LLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLVS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 875 QIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGfASRDKQALEmvGQIT---NEALSNIRTVA 951
Cdd:cd18564 131 GVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKE-ASREQRRRE--GALAsvaQESLSAIRVVQ 207
|
170 180
....*....|....*....|....
gi 21536378 952 GIGKERRFIEALETELEKPFKTAI 975
Cdd:cd18564 208 AFGREEHEERRFARENRKSLRAGL 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1086-1244 |
7.61e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 7.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPSRpdsQVLNGLSVSISPGQTLAFVGSSGCGKSTSiqllerFY------DPDQGKVMIDGHDSKKVNVqFLRSNIGI- 1158
Cdd:COG1137 12 SYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1159 -VSQEPVLFA-CSIMDNIK----YGDNTKEIPMERViaaakQAQLHDFvmSLpekyeTNV-GSQGSQLSRGEKQRIAIAR 1231
Cdd:COG1137 82 yLPQEASIFRkLTVEDNILavleLRKLSKKEREERL-----EELLEEF--GI-----THLrKSKAYSLSGGERRRVEIAR 149
|
170
....*....|...
gi 21536378 1232 AIVRDPKILLLDE 1244
Cdd:COG1137 150 ALATNPKFILLDE 162
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1078-1305 |
1.07e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPsrpDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhDSKKVNVQFLRSNIG 1157
Cdd:PRK13537 8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCG-EPVPSRARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQepvlfacsiMDNIKYGDNTKEipMERVIA---AAKQAQLHDFVMSLPE--KYETNVGSQGSQLSRGEKQRIAIARA 1232
Cdd:PRK13537 84 VVPQ---------FDNLDPDFTVRE--NLLVFGryfGLSAAAARALVPPLLEfaKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1233 IVRDPKILLLDEATSALDTESEKTVQVALDK--AReGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
436-583 |
1.20e-13 |
|
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: 71.81 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIVEQEPVLF-STTIA 513
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFrKLTVE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 514 ENIRYGREDATmEDIVQAAKEANAynFIMDLpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLD 583
Cdd:cd03218 94 ENILAVLEIRG-LSKKEREEKLEE--LLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1075-1305 |
1.37e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.49 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1075 QGKIDFVDCKFTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFL-- 1152
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLyt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1153 -RSNIGIVSQEPVLFA-CSIMDNIKYgdntkeiPMeRVIAAAKQAQLHDFVMSlpeKYETnVGSQG------SQLSRGEK 1224
Cdd:PRK11831 82 vRKRMSMLFQSGALFTdMNVFDNVAY-------PL-REHTQLPAPLLHSTVMM---KLEA-VGLRGaaklmpSELSGGMA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1225 QRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHE 1301
Cdd:PRK11831 150 RRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQ 229
|
....
gi 21536378 1302 ELMA 1305
Cdd:PRK11831 230 ALQA 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
438-615 |
1.96e-13 |
|
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: 71.34 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIGIVEQEPVLFSTTIAENIr 517
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----PDRMVVFQNYSLLPWLTVRENI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 518 YGREDATMEDIVQAAKEAnaynfIMDLPQQFDTLVGEGGGQMSGGQ---KQRVAIARALIRNPKILLLDMATSALDNESE 594
Cdd:TIGR01184 76 ALAVDRVLPDLSKSERRA-----IVEEHIALVGLTEAADKRPGQLSggmKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 21536378 595 AMVQEVLSKI--QHGHTIISVAH 615
Cdd:TIGR01184 151 GNLQEELMQIweEHRVTVLMVTH 173
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
178-360 |
2.05e-13 |
|
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: 72.48 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 178 YFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPLIGIga 256
Cdd:cd18570 81 YFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTiSLFLDLLMVIISGIIL-FFYNWKLFLITLLIIPLYIL-- 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 257 aTIGLSVSKFTDY---ELKAYAK--AGVVadEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKG---IVMGFFTGF 328
Cdd:cd18570 157 -IILLFNKPFKKKnreVMESNAElnSYLI--ESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGklsNLQSSIKGL 233
|
170 180 190
....*....|....*....|....*....|..
gi 21536378 329 VwCLIFLcyALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18570 234 I-SLIGS--LLILWIGSYLVIK-GQLSLGQLI 261
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
755-1012 |
2.11e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 72.52 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 755 MLVGSVGAAVNGTVTPlyaFLFSQILGTfSIPDKEEQRsqINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKF 834
Cdd:cd18550 4 VLLLILLSALLGLLPP---LLLREIIDD-ALPQGDLGL--LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 835 GFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALS 914
Cdd:cd18550 78 LYAHLQRMSLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 915 GATQTRMLTGFASRDKQALEMVGQITNEALSnirtVAGI------GKERRFIEALETELEKPFKTAIqKANIYG--FcFA 986
Cdd:cd18550 156 TRRVGRRRRKLTREQQEKLAELNSIMQETLS----VSGAllvklfGREDDEAARFARRSRELRDLGV-RQALAGrwF-FA 229
|
250 260
....*....|....*....|....*.
gi 21536378 987 FAQCIMFIANSASYRYGGYLISNEGL 1012
Cdd:cd18550 230 ALGLFTAIGPALVYWVGGLLVIGGGL 255
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1094-1298 |
2.96e-13 |
|
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: 70.64 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSkkvnvQFLRSNIGIvsqEPVLfacSIMDN 1173
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGGGF---NPEL---TGREN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1174 IK-----YGDNTKEIP--MERVIAAakqAQLHDFvMSLPEKyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:cd03220 105 IYlngrlLGLSRKEIDekIDEIIEF---SELGDF-IDLPVK----------TYSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1247 SALDTE-SEKTVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIEKG 1298
Cdd:cd03220 171 AVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
418-650 |
3.28e-13 |
|
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: 71.42 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYPSRPEVkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDpCEGMVTVDGHDIRSLNIQWLRDQ 497
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFSTTIAENIR-YGREDAtmEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRN 576
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNLDpYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 577 PKILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEELLERKGVY 650
Cdd:cd03289 157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
423-636 |
3.30e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 3.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 423 HNVTFHYPS------RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN------ 490
Cdd:PRK10419 7 SGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrka 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 491 ----IQWL-RDQIGIVE---------QEPVLFSTTIAENIRYGREDAtMEDIVQAAKEanaynfIMD-LPQQFdtlvgeg 555
Cdd:PRK10419 87 frrdIQMVfQDSISAVNprktvreiiREPLRHLLSLDKAERLARASE-MLRAVDLDDS------VLDkRPPQL------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 556 ggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTV-RAADTIIGFEHG 632
Cdd:PRK10419 153 ----SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVeRFCQRVMVMDNG 228
|
....
gi 21536378 633 TAVE 636
Cdd:PRK10419 229 QIVE 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
424-646 |
4.34e-13 |
|
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: 73.57 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPSRpEVKILNDLNMVIKPGEMTALVGPSGAGKS-TAL---QLIQRFYDPCEGMVTVDGHDIRSLNIQWLR---- 495
Cdd:COG4172 13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALsilRLLPDPAAHPSGSILFDGQDLLGLSERELRrirg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 496 DQIGIVEQEPV-----LFS--TTIAENIR----YGREDATME--------DIVQAAKEANAYnfimdlP-------QQfd 549
Cdd:COG4172 92 NRIAMIFQEPMtslnpLHTigKQIAEVLRlhrgLSGAAARARalellervGIPDPERRLDAY------PhqlsggqRQ-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 550 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTI 626
Cdd:COG4172 164 ----------------RVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQreLGMALLLITHDLGVVRRfADRV 227
|
250 260
....*....|....*....|
gi 21536378 627 IGFEHGTAVERGTHEELLER 646
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFAA 247
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
419-643 |
4.64e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 71.66 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 419 EIEFHNVTFHYPSRP--EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL------- 489
Cdd:PRK13651 2 QIKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkeke 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 490 -----------------NIQWLRDQIGIVEQ--EPVLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFdt 550
Cdd:PRK13651 82 kvleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESY-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 551 lVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV-RAADTIIG 628
Cdd:PRK13651 159 -LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVlEWTKRTIF 237
|
250
....*....|....*.
gi 21536378 629 FEHGTAVERG-THEEL 643
Cdd:PRK13651 238 FKDGKIIKDGdTYDIL 253
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1092-1305 |
4.76e-13 |
|
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: 73.30 E-value: 4.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGKVM-----------ID------------GHDSKK 1146
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyVErpskvgepcpvcGGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1147 VNVQF----------LRSNIGIVSQEPvlFAC----SIMDNIKYGDNTKEIPMERVIAAA----KQAQLHDFVMSLpeky 1208
Cdd:TIGR03269 92 EEVDFwnlsdklrrrIRKRIAIMLQRT--FALygddTVLDNVLEALEEIGYEGKEAVGRAvdliEMVQLSHRITHI---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1209 etnvgsqGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKA--REGRTCIVIAHRLSTIQN-ADI 1285
Cdd:TIGR03269 166 -------ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDK 238
|
250 260
....*....|....*....|
gi 21536378 1286 IAVMAQGVVIEKGTHEELMA 1305
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVA 258
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1094-1307 |
5.64e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 70.31 E-value: 5.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNV-QFLRSNIGIVSQEPVLFA-CSIM 1171
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRrLSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 DNIkygdntkeIPMERVIAAAKQAQLHDFVMSLPEKYETN--VGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PRK10895 97 DNL--------MAVLQIRDDLSAEQREDRANELMEEFHIEhlRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1250 DTESEKTVQVALDKARE-GRTCIVIAHRL-STIQNADIIAVMAQGVVIEKGTHEELMAQK 1307
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1092-1300 |
6.42e-13 |
|
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: 72.94 E-value: 6.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDGHDSKKVNVQFL-RSNIGIVSQEPVLFA 1167
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 -CSIMDNIKYGdNTKEIPMERVIAAAKQAQLHDFV--MSLPEkyeTNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:TIGR02633 92 eLSVAENIFLG-NEITLPGGRMAYNAMYLRAKNLLreLQLDA---DNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1245 ATSALdTESEKTVQVAL--DKAREGRTCIVIAHRLSTIQnadiiAVMAQGVVIEKGTH 1300
Cdd:TIGR02633 168 PSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQH 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
420-647 |
6.48e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.99 E-value: 6.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIG 499
Cdd:PRK13537 8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQ----EPvlfSTTIAENIR-----YGREDATMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGgqkqRVAIA 570
Cdd:PRK13537 84 VVPQfdnlDP---DFTVRENLLvfgryFGLSAAAARALVPPLLE------FAKLENKADAKVGELSGGMKR----RLTLA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 571 RALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERK 647
Cdd:PRK13537 151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLrSLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
420-638 |
7.47e-13 |
|
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: 69.48 E-value: 7.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPS-------------------RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT 480
Cdd:cd03220 1 IELENVSKSYPTykggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 481 VDGhdirslNIQWLRD-QIGIveqEPVLfstTIAENIR-----YGREDATMEDIvqaakeanaYNFIMD---LPQQFDTL 551
Cdd:cd03220 81 VRG------RVSSLLGlGGGF---NPEL---TGRENIYlngrlLGLSRKEIDEK---------IDEIIEfseLGDFIDLP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 552 VgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRA-ADTIIGF 629
Cdd:cd03220 140 V----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKRlCDRALVL 215
|
....*....
gi 21536378 630 EHGTAVERG 638
Cdd:cd03220 216 EKGKIRFDG 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
431-638 |
7.95e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 7.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 431 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDQ--IGIVEQE-PVL 507
Cdd:PRK09700 14 SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQElSVI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 508 FSTTIAENIRYGRE------DATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIARALIRNPKILL 581
Cdd:PRK09700 93 DELTVLENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM----LEIAKTLMLDAKVII 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 582 LDMATSALDNESEAMVQEVLSKIQ-HGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERG 638
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
148-308 |
8.27e-13 |
|
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: 70.58 E-value: 8.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 148 IAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTST 227
Cdd:cd18589 45 LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARG 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 228 ICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKN 307
Cdd:cd18589 125 LFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQR 204
|
.
gi 21536378 308 L 308
Cdd:cd18589 205 L 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
424-645 |
8.66e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.20 E-value: 8.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQ 503
Cdd:PRK10575 16 NVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 504 E-PVLFSTTIAENI------------RYGREDAtmedivQAAKEANAYNFIMDLPQQF-DTLvgegggqmSGGQKQRVAI 569
Cdd:PRK10575 93 QlPAAEGMTVRELVaigrypwhgalgRFGAADR------EKVEEAISLVGLKPLAHRLvDSL--------SGGERQRAWI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 570 ARALIRNPKILLLDMATSALD----NESEAMVQEvLSKiQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDiahqVDVLALVHR-LSQ-ERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236
|
.
gi 21536378 645 E 645
Cdd:PRK10575 237 R 237
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
803-1010 |
1.05e-12 |
|
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: 70.42 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 803 VAMGCVS-LFTqflqgYAFAKsgelLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVN 881
Cdd:cd18784 51 VAAGIRGgLFT-----LAMAR----LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVSLNLNIFLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 882 SFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFIE 961
Cdd:cd18784 120 SLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEAN 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536378 962 ALETELEKPFKTAIQKANIYG---FCFAFAQCIMFIansASYRYGGYLISNE 1010
Cdd:cd18784 200 RYSEKLKDTYKLKIKEALAYGgyvWSNELTELALTV---STLYYGGHLVITG 248
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
139-360 |
1.15e-12 |
|
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: 70.27 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 139 IKFASYYAgiAVAVLITGYIQicFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA 218
Cdd:cd18574 46 LKLLGLYL--LQSLLTFAYIS--LLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 219 LFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEK 298
Cdd:cd18574 122 QGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMED 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 299 REVERYEKNLVFAQRWGIRKGIVMGFFTG----FVWCLIFLCYalafWYGSTLVlDEGEYTPGTLV 360
Cdd:cd18574 202 RELELYEEEVEKAAKLNEKLGLGIGIFQGlsnlALNGIVLGVL----YYGGSLV-SRGELTAGDLM 262
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
432-645 |
1.17e-12 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 72.39 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 432 RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQrFYDP----CEGMVTVDGHDIrslNIQWLRDQIGIVEQEPVL 507
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 508 FST-TIAENI------RYGREDAT------MEDIVQAAKEANAYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALI 574
Cdd:TIGR00955 111 IPTlTVREHLmfqahlRMPRRVTKkekrerVDEVLQALGLRKCANTRIGVPGRVKGL--------SGGERKRLAFASELL 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 575 RNPKILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLST--VRAADTIIGFEHGTAVERGTHEELLE 645
Cdd:TIGR00955 183 TDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
433-636 |
1.31e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.74 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 433 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDG-----HDIRSlniqwlRDQIGIV--E 502
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRD------SEALGIViiH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 503 QE----PVLfstTIAENIRYGREDATM------EDIVQAAK-------EANAYNFIMDL---PQQFdtlvgegggqmsgg 562
Cdd:NF040905 85 QElaliPYL---SIAENIFLGNERAKRgvidwnETNRRAREllakvglDESPDTLVTDIgvgKQQL-------------- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 563 qkqrVAIARALIRNPKILLLDMATSAL-DNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVE 636
Cdd:NF040905 148 ----VEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
434-648 |
1.65e-12 |
|
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: 67.94 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRF--YDPCEGMVTVDGHDIRSLNIQwLRDQIGI--VEQEPVLFS 509
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 510 -TTIAENIRY------GREdatmedivqaakeanaynfimdlpqqfdtlvgegggqmsggqKQRVAIARALIRNPKILLL 582
Cdd:cd03217 91 gVKNADFLRYvnegfsGGE------------------------------------------KKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 583 DMATSALDNESEAMVQEVLSKIQH-GHTIISVAH--RLSTVRAADTIIGFEHGTAVERGTHE--ELLERKG 648
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKG 199
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
420-604 |
1.80e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.12 E-value: 1.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYP-SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI------Rslniq 492
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadR----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 493 wlrdqiGIVEQEPVLFS-TTIAENIRYG----------REDATMEDIVQAAKEANAYNFIMDLP---QQfdtlvgegggq 558
Cdd:COG4525 79 ------GVVFQKDALLPwLNVLDNVAFGlrlrgvpkaeRRARAEELLALVGLADFARRRIWQLSggmRQ----------- 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 559 msggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI 604
Cdd:COG4525 142 -------RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDV 180
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1100-1298 |
1.85e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.80 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1100 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQ---------FLRSNIGIVSQEP---VLFA 1167
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYalseaerrrLLRTEWGFVHQHPrdgLRMQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNI----------KYGD--NTKEIPMERV-IAAAKqaqLHDfvmsLPekyetnvgsqgSQLSRGEKQRIAIARAIV 1234
Cdd:PRK11701 106 VSAGGNIgerlmavgarHYGDirATAGDWLERVeIDAAR---IDD----LP-----------TTFSGGMQQRLQIARNLV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1235 RDPKILLLDEATSALDTesekTVQVA-LDKARE-----GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKG 1298
Cdd:PRK11701 168 THPRLVFMDEPTGGLDV----SVQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
420-644 |
2.13e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.05 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNV--TFHYPS----RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDI------- 486
Cdd:PRK15112 5 LEVRNLskTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 487 RSLNIQWL----------RDQIGIVEQEPVLFSTTIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQfdtlvgegg 556
Cdd:PRK15112 85 RSQRIRMIfqdpstslnpRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQK--------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 557 gqmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHTI--ISVAHRLSTVR-AADTIIGFEHGT 633
Cdd:PRK15112 156 --------QRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGIsyIYVTQHLGMMKhISDQVLVMHQGE 227
|
250
....*....|.
gi 21536378 634 AVERGTHEELL 644
Cdd:PRK15112 228 VVERGSTADVL 238
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
418-617 |
2.20e-12 |
|
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: 72.25 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEIEFHNVTFHYPSRPEvKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDpCEGMVTVDGHDIRSLNIQWLRDQ 497
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFSTTIAENIRyGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNP 577
Cdd:TIGR01271 1294 FGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21536378 578 KILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRL 617
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
406-620 |
3.20e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 71.68 E-value: 3.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 406 MSEDGYKLDRIKGEIEFH--NVTFHYPSRPEVK-ILNDLNMVIKPGEMTALVGPSGAGKSTALQ-LIQRFydpCEGMVT- 480
Cdd:TIGR00956 744 DVNDEKDMEKESGEDIFHwrNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERV---TTGVITg 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 481 ----VDGHDIRSLniqwLRDQIGIVEQEPV-LFSTTIAENIRYG---REDATMEDivqaaKEANAY-NFIMDL---PQQF 548
Cdd:TIGR00956 821 gdrlVNGRPLDSS----FQRSIGYVQQQDLhLPTSTVRESLRFSaylRQPKSVSK-----SEKMEYvEEVIKLlemESYA 891
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 549 DTLVGEGGGQMSGGQKQRVAIARALIRNPKILL-LDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTV 620
Cdd:TIGR00956 892 DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQPSAI 965
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
434-650 |
3.45e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 69.11 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVD----GHDIRSL------------NIQWLRDQ 497
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEP--VLFSTTIAENIRYGREDATMEDIvQAAKEANAYNFIMDLPQQFdtlVGEGGGQMSGGQKQRVAIARALIR 575
Cdd:PRK13631 118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKS-EAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 576 NPKILLLDMATSALDNESEA-MVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLERKGVY 650
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
420-646 |
3.51e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVdGHDIRslniqwlrdqIG 499
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLF--STTIAENIRYGREDATMEDIVQAAKeanAYNFImdlPQQFDTLVgegggqmsggqKQ-------RVAIA 570
Cdd:COG0488 382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLG---RFLFS---GDDAFKPV-----------GVlsggekaRLALA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 571 RALIRNPKILLLDMATSALDNESEAMVQEVLSKIQhGhTIISVAH-R--LSTVraADTIIGFEHGTAVER-GTHEELLER 646
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
147-370 |
3.94e-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: 68.58 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 147 GIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIndaiadQMALF-IQRMT 225
Cdd:cd18548 47 LLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGTSSLITRLTNDVTQV------QNFVMmLLRML 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 226 ST-----ICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKRE 300
Cdd:cd18548 121 VRapimlIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYE 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 301 VERYEK-NLVFAQRwGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVlDEGEYTPGTLV-------QIFLSVIVGA 370
Cdd:cd18548 201 EERFDKaNDDLTDT-SLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLI-NAGSLQVGDLVafinylmQILMSLMMLS 276
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
428-606 |
4.02e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.80 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 428 HYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWlrdqiGIVEQ-EPV 506
Cdd:PRK11248 10 DYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQnEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 507 LFSTTIAENIRYG----------REDATMEDIVQAAKEANAYNFIMDLpqqfdtlvgegggqmSGGQKQRVAIARALIRN 576
Cdd:PRK11248 82 LPWRNVQDNVAFGlqlagvekmqRLEIAHQMLKKVGLEGAEKRYIWQL---------------SGGQRQRVGIARALAAN 146
|
170 180 190
....*....|....*....|....*....|
gi 21536378 577 PKILLLDMATSALDNESEAMVQEVLSKIQH 606
Cdd:PRK11248 147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQ 176
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
793-996 |
4.06e-12 |
|
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: 68.58 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 793 SQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAA 872
Cdd:cd18547 42 SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQAL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 873 GSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSgatqTRMLTGFASR--DKQAlEMVGQIT---NEALSNI 947
Cdd:cd18547 120 SQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV----TKFIAKRSQKyfRKQQ-KALGELNgyiEEMISGQ 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536378 948 RTVAGIGKERRFIEALETELEKPFKTAIqKANIYGfcFAFAQCIMFIAN 996
Cdd:cd18547 195 KVVKAFNREEEAIEEFDEINEELYKASF-KAQFYS--GLLMPIMNFINN 240
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
424-632 |
4.36e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 67.78 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQrfydpceGMVTVDGHDIRSLN--IQWLRDQIGIV 501
Cdd:PRK11247 17 AVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLA-------GLETPSAGELLAGTapLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 502 EQEPVLFS-TTIAENIRYG-----REDATME-DIVQAAKEANAYNFIMDLPQQfdtlvgegggqmsggqkQRVAIARALI 574
Cdd:PRK11247 87 FQDARLLPwKKVIDNVGLGlkgqwRDAALQAlAAVGLADRANEWPAALSGGQK-----------------QRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 575 RNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLS-TVRAADTIIGFEHG 632
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1096-1301 |
4.45e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 4.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVnvqfLRSN-IGIVSQE-------PVLFA 1167
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNlVAYVPQSeevdwsfPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNiKYGD-----NTKEIPMERVIAAAKQAQLHDFVMSlpekyetnvgsQGSQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK15056 99 DVVMMG-RYGHmgwlrRAKKRDRQIVTAALARVDMVEFRHR-----------QIGELSGGQKKRVFLARAIAQQGQVILL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1243 DEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHE 1301
Cdd:PRK15056 167 DEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
424-617 |
4.87e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 67.80 E-value: 4.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiQWLRDQ-IGIVE 502
Cdd:COG1101 8 SKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRAKyIGRVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 503 QEPVL---FSTTIAEN------------IRYGREDATMEDIVQAAKEANaynfiMDLPQQFDTlvgegggqmsggqkqRV 567
Cdd:COG1101 87 QDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDT---------------KV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 568 ---------AIA--RALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRL 617
Cdd:COG1101 147 gllsggqrqALSllMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNM 209
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1078-1275 |
4.92e-12 |
|
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: 64.78 E-value: 4.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDghdsKKVNVQFLrsnig 1157
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 ivsqepvlfacsimdnikygdntkeipmerviaaakqaqlhdfvmslpekyetnvgsqgSQLSRGEKQRIAIARAIVRDP 1237
Cdd:cd03221 69 -----------------------------------------------------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190
....*....|....*....|....*....|....*...
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALdKAREGrTCIVIAH 1275
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-644 |
5.44e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 67.81 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGM-----VTVDGHDIRSL-NIQWLRDQIGIVEQEPVLFST 510
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 511 TIAENIRYGREDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALD 590
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 591 NESEAMVQEVLSKIQHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
427-660 |
5.68e-12 |
|
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: 70.81 E-value: 5.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 427 FHYPSRPEVkilNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSlNIQWLRDQIGIVEQEPV 506
Cdd:TIGR01257 938 FEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNI 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 507 LFS-TTIAENIRY-----GR--EDATMEdiVQAAKEANAYNFIMDLPQQfdtlvgegggQMSGGQKQRVAIARALIRNPK 578
Cdd:TIGR01257 1014 LFHhLTVAEHILFyaqlkGRswEEAQLE--MEAMLEDTGLHHKRNEEAQ----------DLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 579 ILLLDMATSALDNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE--RKGVYFTLV- 654
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLKNcfGTGFYLTLVr 1161
|
....*....
gi 21536378 655 ---TLQSQG 660
Cdd:TIGR01257 1162 kmkNIQSQR 1170
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
420-615 |
8.15e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHY-PSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW---LR 495
Cdd:PRK10584 7 VEVHHLKKSVgQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 496 DQ-IGIVEQEPVLFSTTIA-ENI------RYGREDATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqmsGGQKQRV 567
Cdd:PRK10584 87 AKhVGFVFQSFMLIPTLNAlENVelpallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLS-----------GGEQQRV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536378 568 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAH 615
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1095-1298 |
8.48e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 8.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFY--DPDQGKVMIDghdskkvNVQFlrsnigivSQEpvlfaCSIMD 1172
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-------DNQF--------GRE-----ASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1173 NIKYGDNTKEipmerVIAAAKQAQLHDFVMSLpEKYetnvgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTE 1252
Cdd:COG2401 105 AIGRKGDFKD-----AVELLNAVGLSDAVLWL-RRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536378 1253 SEKTVQVALDKA--REGRTCIVIAHRlstiqnADIIAVMAQGVVIEKG 1298
Cdd:COG2401 171 TAKRVARNLQKLarRAGITLVVATHH------YDVIDDLQPDLLIFVG 212
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1094-1292 |
1.04e-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: 65.34 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL-ERFYDPD-QGKVMIDGhdsKKVNVQFLRSnIGIVSQEPVLFACSim 1171
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING---RPLDKNFQRS-TGYVEQQDVHSPNL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 dnikygdnTKEIPMErvIAAAKQAqlhdfvmslpekyetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSALDT 1251
Cdd:cd03232 95 --------TVREALR--FSALLRG-----------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 21536378 1252 ESEKTVQVALDK-AREGRTCIVIAHRLS--TIQNADIIAVMAQG 1292
Cdd:cd03232 142 QAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1092-1298 |
1.04e-11 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 66.52 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ERFYDPDQGKVMIDGHDSKKVNVQfLRSNIGIV--SQEPV--- 1164
Cdd:TIGR01978 12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEPD-ERARAGLFlaFQYPEeip 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 -----LFACSIMDNIKYGDNTKEIPMERVIAAAKQA-QLHDFVMSLPEKYeTNVGsqgsqLSRGEKQRIAIARAIVRDPK 1238
Cdd:TIGR01978 91 gvsnlEFLRSALNARRSARGEEPLDLLDFEKLLKEKlALLDMDEEFLNRS-VNEG-----FSGGEKKRNEILQMALLEPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 1239 ILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAH--RLSTIQNADIIAVMAQGVVIEKG 1298
Cdd:TIGR01978 165 LAILDEIDSGLDIDALKIVAEGINRLRePDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1090-1303 |
1.05e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1090 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-------------MIDGHDSKKVNVQFLR-SN 1155
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRgAD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1156 IGIVSQEPV-----LFAC--SIMDNIKYGDNTKEipmERVIAAAKQaqLHDFVmSLPEKyETNVGSQGSQLSRGEKQRIA 1228
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQGASR---EEAMVEAKR--MLDQV-RIPEA-QTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1229 IARAIVRDPKILLLDEATSALD-TESEKTVQ-VALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDvTIQAQILQlIKVLQKEMSMGVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1096-1315 |
1.23e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRsNIGIV----SQepVLFACSIM 1171
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ--LWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 DNIK-----YgdntkEIPMERviAAAKQAQLHDfVMSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:COG4586 115 DSFRllkaiY-----RIPDAE--YKKRLDELVE-LLDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1247 SALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELmAQKGAYYKLVT 1315
Cdd:COG4586 183 IGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEEL-KERFGPYKTIV 253
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1090-1274 |
1.23e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 65.28 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1090 RPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGivSQEPVLFACS 1169
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYGDNTKEIPMERVIAAAKQAQLHDfVMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*
gi 21536378 1250 DTESEKTVQvALDKAREGRTCIVIA 1274
Cdd:PRK13539 159 DAAAVALFA-ELIRAHLAQGGIVIA 182
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
427-633 |
1.39e-11 |
|
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: 65.82 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 427 FHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRdQIGIV--EQE 504
Cdd:cd03267 26 LFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLR-RIGVVfgQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 505 PVLFSTTIAENIRYGREDATMEDiVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGgqkqRVAIARALIRNPKILLLDM 584
Cdd:cd03267 105 QLWWDLPVIDSFYLLAAIYDLPP-ARFKKRLDELSELLDLEELLDTPVRQLSLGQRM----RAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536378 585 ATSALDNESEAMVQEVLSKIQ--HGHTIISVAHRLSTVRA-ADTIIGFEHGT 633
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNreRGTTVLLTSHYMKDIEAlARRVLVIDKGR 231
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1099-1304 |
1.46e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1099 LSVSISPGQTLAFVGSSGCGKSTsiqLLERFYD--PDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFAcsiMDNIK 1175
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPlEAWSAAELARHRAYLSQQQTPPFA---MPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1176 Y-----GDNTKEipmerviaAAKQAQLHDFV--MSLPEKYETNVGsqgsQLSRGEKQRIAIARAIVR-------DPKILL 1241
Cdd:PRK03695 89 YltlhqPDKTRT--------EAVASALNEVAeaLGLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1242 LDEATSALDTesekTVQVALDK-----AREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 1304
Cdd:PRK03695 157 LDEPMNSLDV----AQQAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
145-360 |
1.70e-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: 66.72 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 145 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 224
Cdd:cd18545 46 FLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 225 TSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIG-LSVSKFTDYELKayaKAGVVAD--EVISSMRTVAAFGGEKREV 301
Cdd:cd18545 126 LTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRrRARKAWQRVRKK---ISNLNAYlhESISGIRVIQSFAREDENE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 302 ERYE---KNLVFAQRWGIRkgivmgfFTGFVWCLIFLCYALA----FWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18545 203 EIFDelnRENRKANMRAVR-------LNALFWPLVELISALGtalvYWYGGKLVLG-GAITVGVLV 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1078-1306 |
2.11e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIdGHdskkvNVQflrsnIG 1157
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVLFAC--SIMDNIK-YGDNTKEIpmerviaaakqaqlhdFVMSL-------PEKYETNVGSqgsqLSRGEKQRI 1227
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELRdGAPGGTEQ----------------EVRGYlgrflfsGDDAFKPVGV----LSGGEKARL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1228 AIARAIVRDPKILLLDEATSALDTESEKTVQVALDkAREGrTCIVIAH-R--LSTIQNaDIIAVMAQGVVIEKGTHEELM 1304
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRVAT-RILEFEDGGVREYPGGYDDYL 518
|
..
gi 21536378 1305 AQ 1306
Cdd:COG0488 519 EK 520
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1091-1304 |
2.27e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 2.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH-----DSKKvnvqFLRSNIGIVSQEPVL 1165
Cdd:PRK10575 22 PGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQpleswSSKA----FARKVAYLPQQLPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 FACSIMDNI------------KYGDNTKEipmeRVIAAAKQAQLHDFVMSLpekyetnVGSqgsqLSRGEKQRIAIARAI 1233
Cdd:PRK10575 98 EGMTVRELVaigrypwhgalgRFGAADRE----KVEEAISLVGLKPLAHRL-------VDS----LSGGERQRAWIAMLV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1234 VRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAhRLSTIQNA----DIIAVMAQGVVIEKGTHEELM 1304
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAELM 236
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1105-1287 |
2.28e-11 |
|
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: 63.16 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1105 PGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV-MIDGHDSKKVNVQFLRsnigivsqepvlfacsimdnikygdntkei 1183
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1184 pmerviaaakqaqlhdfvmslpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALD- 1262
Cdd:smart00382 51 -------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEEl 105
|
170 180 190
....*....|....*....|....*....|.
gi 21536378 1263 ------KAREGRTCIVIAHRLSTIQNADIIA 1287
Cdd:smart00382 106 rlllllKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
432-602 |
2.58e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 2.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 432 RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN----IQWL--RDQIgiveqEP 505
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvaeaCHYLghRNAM-----KP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 506 VLfstTIAENIR-----YGREDATmediVQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkQRVAIARAL 573
Cdd:PRK13539 87 AL---TVAENLEfwaafLGGEELD----IAAALEAVGLAPLAHLPfgylsagQK-----------------RRVALARLL 142
|
170 180
....*....|....*....|....*....
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVLS 602
Cdd:PRK13539 143 VSNRPIWILDEPTAALDAAAVALFAELIR 171
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
420-646 |
2.77e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.10 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYP-------------------SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT 480
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 481 VDGhdirslNIQWLrdqIGiveqepvlFST------TIAENIR-----YG---RE-DATMEDIVQAAkeanaynfimDLP 545
Cdd:COG1134 85 VNG------RVSAL---LE--------LGAgfhpelTGRENIYlngrlLGlsrKEiDEKFDEIVEFA----------ELG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 546 QQFDT---------LVgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNE----SEAMVQEvlsKIQHGHTIIS 612
Cdd:COG1134 138 DFIDQpvktyssgmRA-------------RLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRE---LRESGRTVIF 201
|
250 260 270
....*....|....*....|....*....|....*
gi 21536378 613 VAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLER 646
Cdd:COG1134 202 VSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
433-633 |
2.82e-11 |
|
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: 64.66 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 433 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV--------TVDGHDIRSLNiqwlRDQIGIVEQE 504
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRN----RYSVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 505 PVLFSTTIAENIRYGreDATMEDIVQAAKEANAYNFIMD-LPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLD 583
Cdd:cd03290 88 PWLLNATVEENITFG--SPFNKQRYKAVTDACSLQPDIDlLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 584 MATSALD-NESEAMVQEVLSKI--QHGHTIISVAHRLSTVRAADTIIGFEHGT 633
Cdd:cd03290 166 DPFSALDiHLSDHLMQEGILKFlqDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
136-306 |
3.50e-11 |
|
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: 65.89 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 136 SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAD 215
Cdd:cd18547 42 SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 216 QMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFG 295
Cdd:cd18547 122 SLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFN 201
|
170
....*....|.
gi 21536378 296 GEKREVERYEK 306
Cdd:cd18547 202 REEEAIEEFDE 212
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
424-632 |
3.89e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.59 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDghDIRSLNIQWLRDQIGIVEQ 503
Cdd:PRK11000 8 NVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIG--EKRMNDVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 504 EPVLFS-TTIAENIRYGREDATMEDIvQAAKEANAYNFIMdlpqQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLL 582
Cdd:PRK11000 83 SYALYPhLSVAENMSFGLKLAGAKKE-EINQRVNQVAEVL----QLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 583 DMATSALDNESEAMVQEVLSKIQH--GHTIISVAHrlSTVRA---ADTIIGFEHG 632
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTH--DQVEAmtlADKIVVLDAG 210
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
805-964 |
5.33e-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: 65.05 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 805 MGCVSLFTQF---LQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVN 881
Cdd:cd18590 42 MCLFSLGSSLsagLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTTLMSRSVALNANVLLR 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 882 SFTNVTVAMIIAFSFSWKLSLVILCFFPFLALsgaTQTRMLTGFASRDKQALEMV---GQITNEALSNIRTVAGIGKE-- 956
Cdd:cd18590 120 SLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAI---AQKVYNTYHQKLSQAVQDSIakaGELAREAVSSIRTVRSFKAEee 196
|
170
....*....|
gi 21536378 957 --RRFIEALE 964
Cdd:cd18590 197 eaCRYSEALE 206
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
437-643 |
5.60e-11 |
|
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: 64.88 E-value: 5.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLrdqigiveqepvlFSTTIAENI 516
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRISFSSQFSWI-------------MPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 517 RYG--REDATMEDIVQAAKEANAynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESE 594
Cdd:cd03291 119 IFGvsYDEYRYKSVVKACQLEED---ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536378 595 AMVQE-VLSKIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGTHEEL 643
Cdd:cd03291 196 KEIFEsCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
421-643 |
5.61e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 5.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 421 EFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRDQ--- 497
Cdd:PRK11288 6 SFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAST---TAAlaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 -IGIVEQE----PVLfstTIAENIRYGR--EDATMEDIVQAAKEANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIA 570
Cdd:PRK11288 80 gVAIIYQElhlvPEM---TVAENLYLGQlpHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQM----VEIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 571 RALIRNPKILLLDMATSALD-NESEAMVQEVLSKIQHGHTIISVAHRLSTV-RAADTIIGFEHGTAVErgTHEEL 643
Cdd:PRK11288 153 KALARNARVIAFDEPTSSLSaREIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
426-632 |
5.62e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.65 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 426 TFHypsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQ----LIQRFYDPcEGMVTVDGHDIR-----SLNIQWLRD 496
Cdd:PRK09984 13 TFN-----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIELLGRTVQregrlARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIG-IVEQEPVLFSTTIAENIRYGREDAT--------------MEDIVQAAKEANAYNFIMdlpQQFDTLvgegggqmSG 561
Cdd:PRK09984 87 NTGyIFQQFNLVNRLSVLENVLIGALGSTpfwrtcfswftreqKQRALQALTRVGMVHFAH---QRVSTL--------SG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 562 GQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLS-TVRAADTIIGFEHG 632
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQG 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
437-644 |
5.96e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 66.65 E-value: 5.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKS-TALQLIQRFYDP----CEGMVTVDGHDIRSLNIQWLR----DQIGIVEQEPVL 507
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 508 fSTTIAENI-----------RYGREDATMEDIV---------QAAKEANaynfimDLPQQFdtlvgegggqmSGGQKQRV 567
Cdd:PRK15134 104 -SLNPLHTLekqlyevlslhRGMRREAARGEILncldrvgirQAAKRLT------DYPHQL-----------SGGERQRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 568 AIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELL 644
Cdd:PRK15134 166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1095-1305 |
7.06e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 66.83 E-value: 7.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLE-RFYDPD-QGKVMIDGhdsKKVNVQFLRsNIGIVSQEPVLFA----- 1167
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhltvr 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 -----CSIMDNIK-YGDNTKEIPMERVIAAAKQAQLHDFVMSlpekyetNVGSQGsqLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PLN03211 159 etlvfCSLLRLPKsLTKQEKILVAESVISELGLTKCENTIIG-------NSFIRG--ISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1242 LDEATSALD-TESEKTVQVALDKAREGRTCIVIAHRLST--IQNADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PLN03211 230 LDEPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1094-1303 |
8.22e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 64.26 E-value: 8.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQ---GKVMIDGHDSKKV-----NVQFLRSNIGIVSQEPVL 1165
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 F-ACSIMDNIKYGdNTKEIPMERV-IAAAKQAQLHDFVMSLpekyeTNVG------SQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK09984 98 VnRLSVLENVLIG-ALGSTPFWRTcFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALD--KAREGRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
756-1033 |
8.24e-11 |
|
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: 64.43 E-value: 8.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 756 LVGSVGAAVNGTVTPLYAFLFSQILgtfsI--PDKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRK 833
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRA----IdgPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 834 FGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFPFLAL 913
Cdd:cd18543 77 DLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFLAFGPFLLGNLLT-LVVGLVVMLVLSPPLALVALASLPPLVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 914 SGATQTRMLTGfASRDKQalEMVGQIT---NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQC 990
Cdd:cd18543 154 VARRFRRRYFP-ASRRAQ--DQAGDLAtvvEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEA 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 991 IMFIANSASYRYGGYLISNEGL-------HFSYV------FRVISAVVLSA----TALGR 1033
Cdd:cd18543 231 LPELGLAAVLALGGWLVANGSLtlgtlvaFSAYLtmlvwpVRMLGWLLAMAqrarAAAER 290
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
423-583 |
8.31e-11 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 63.51 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 423 HNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTAlqliqrFY------DPCEGMVTVDGHDIRSLNIqWLRD 496
Cdd:COG1137 7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGI--VEQEPVLF-STTIAENIRygredATMEDIVQAAKEANAYnfIMDLPQQF----------DTLvgegggqmsggq 563
Cdd:COG1137 77 RLGIgyLPQEASIFrKLTVEDNIL-----AVLELRKLSKKEREER--LEELLEEFgithlrkskaYSLsgg--------e 141
|
170 180
....*....|....*....|
gi 21536378 564 kqRVAIARALIRNPKILLLD 583
Cdd:COG1137 142 rrRVEIARALATNPKFILLD 161
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
439-643 |
8.65e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 63.86 E-value: 8.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 439 NDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwlrdQI---GIVE--QEPVLF-STTI 512
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIarmGVVRtfQHVRLFrEMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 513 AENI--------------------RYGRedATMEDIVQAA---------KEAN------AYNfimdlpQQfdtlvgeggg 557
Cdd:PRK11300 98 IENLlvaqhqqlktglfsgllktpAFRR--AESEALDRAAtwlervgllEHANrqagnlAYG------QQ---------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 558 qmsggqkQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTA 634
Cdd:PRK11300 160 -------RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELrnEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTP 232
|
....*....
gi 21536378 635 VERGTHEEL 643
Cdd:PRK11300 233 LANGTPEEI 241
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1092-1277 |
9.74e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 9.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMidgHDSKkvnvqfLRsnIGIVSQ----EPVL-F 1166
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGK------LR--IGYVPQklylDTTLpL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 ACSIMDNIKYGDNTKEI--PMERVIAAakqaQLHDFVMSlpekyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK09544 85 TVNRFLRLRPGTKKEDIlpALKRVQAG----HLIDAPMQ--------------KLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 21536378 1245 ATSALDTESektvQVAL----DKAREGRTCIV--IAHRL 1277
Cdd:PRK09544 147 PTQGVDVNG----QVALydliDQLRRELDCAVlmVSHDL 181
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
420-649 |
1.02e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrslnIQW-----L 494
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 495 RDQIGIVEQEPVLFS-TTIAENIRYGREDATMEDIVQAAKEanaynfIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARAL 573
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKW------VYELFPRLHERRIQRAGTMSGGEQQMLAIGRAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 574 IRNPKILLLDMATSALdneSEAMVQEVLSKIQH----GHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELLERKG 648
Cdd:PRK11614 153 MSQPRLLLLDEPSLGL---APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEA 229
|
.
gi 21536378 649 V 649
Cdd:PRK11614 230 V 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1100-1309 |
1.08e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 66.30 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1100 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGH--DSKKVNVqflRSNIGIVSQepvlfACSImdnikYG 1177
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQpvDAGDIAT---RRRVGYMSQ-----AFSL-----YG 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1178 DNT----------------KEIPmERVIAAAKQAQLHDFVMSLPEkyetnvgsqgsQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:NF033858 353 ELTvrqnlelharlfhlpaAEIA-ARVAEMLERFDLADVADALPD-----------SLPLGIRQRLSLAVAVIHKPELLI 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1242 LDEATSALDTesektvqVA--------LDKAREGRTCIVIA-HRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGA 1309
Cdd:NF033858 421 LDEPTSGVDP-------VArdmfwrllIELSREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARGA 490
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
435-626 |
1.16e-10 |
|
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: 65.62 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 435 VKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPC---EGMVTVDGHDIRSLNIQWL-RDQIGIVEQEPVLF-S 509
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 510 TTIAENIRYGRE---------DATM----EDIVQAAK--EANAYNFIMDLPQQFDTLVgegggqmsggqkqrvAIARALI 574
Cdd:TIGR02633 93 LSVAENIFLGNEitlpggrmaYNAMylraKNLLRELQldADNVTRPVGDYGGGQQQLV---------------EIAKALN 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 21536378 575 RNPKILLLDMATSAL-DNESEAMVQEVLSKIQHGHTIISVAHRLSTVRA-ADTI 626
Cdd:TIGR02633 158 KQARLLILDEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTI 211
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
424-646 |
1.21e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.03 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYpSRPEVKILNDLNMVIKPGEMTALVGPSGAGKS-TALQLIqRFYDPCEGMVTVDGHDIRSLNIQW--LRDQ--- 497
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGLVQCDKMLLRRRSRQVieLSEQsaa 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 ---------IGIVEQEPV-----LFST--TIAENIR----YGREDATME--DIVQAAKEANAYNFIMDLPQQFDtlvgeg 555
Cdd:PRK10261 97 qmrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREEAMVEakRMLDQVRIPEAQTILSRYPHQLS------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 556 ggqmsGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGHT--IISVAHRLSTV-RAADTIIGFEHG 632
Cdd:PRK10261 171 -----GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQG 245
|
250
....*....|....
gi 21536378 633 TAVERGTHEELLER 646
Cdd:PRK10261 246 EAVETGSVEQIFHA 259
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
420-645 |
1.28e-10 |
|
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: 65.59 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPS--RPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVT-------VDGHDIRSLN 490
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 491 IQWLRDQIGIVEQEPVLFS-TTIAENI----------RYGREDATMEDIVQAAKEANAYNFIMDLPQQFDtlvgegggqm 559
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLteaiglelpdELARMKAVITLKMVGFDEEKAEEILDKYPDELS---------- 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 560 sGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVL--SKIQHGHTIISVAHRLSTVR-AADTIIGFEHGTAVE 636
Cdd:TIGR03269 430 -EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLdVCDRAALMRDGKIVK 508
|
....*....
gi 21536378 637 RGTHEELLE 645
Cdd:TIGR03269 509 IGDPEEIVE 517
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
798-1012 |
1.85e-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: 350007 [Multi-domain] Cd Length: 296 Bit Score: 63.68 E-value: 1.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 798 VCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQG--AAGSQ 875
Cdd:cd18563 45 LVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDflSDGLP 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 876 iGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGK 955
Cdd:cd18563 123 -DFLTNILMIIGIG-VVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQ 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 956 ERRFIEALETELEKPFKTAIQKANIYGFCFAFaqcIMFIANSASY---RYGGYLISNEGL 1012
Cdd:cd18563 201 EKREIKRFDEANQELLDANIRAEKLWATFFPL---LTFLTSLGTLivwYFGGRQVLSGTM 257
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
420-622 |
1.99e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHdirslniqwLRdqIG 499
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFST---TIAENIRYgREDATMEDIVQAAKEANAYNFImDLPQQfdtlvgegggQMSGGQKQRVAIARALIRN 576
Cdd:PRK09544 71 YVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536378 577 PKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA 622
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMA 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
437-618 |
2.25e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 62.14 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQW---LRDQ-IGIVEQ-EPVLFSTT 511
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 512 IAENIrygredaTMEDIVQAAK--EANAYNFIMDLPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSAL 589
Cdd:PRK11629 104 ALENV-------AMPLLIGKKKpaEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 21536378 590 DNESEAMVQEVLSKI--QHGHTIISVAHRLS 618
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1095-1304 |
2.29e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.70 E-value: 2.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQepvlfacsimDNI 1174
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ----------NAT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1175 KYGDntkeIPMERVIAAAKQAQLHDFVMSLPEKYE-----------TNVGSQG-SQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:PRK10253 92 TPGD----ITVQELVARGRYPHQPLFTRWRKEDEEavtkamqatgiTHLADQSvDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1243 DEATSALDTESE-KTVQVALDKARE-GRTCIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 1304
Cdd:PRK10253 168 DEPTTWLDISHQiDLLELLSELNREkGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
146-360 |
2.53e-10 |
|
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: 62.99 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQIC---FWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDdINKINDAIADQMALFIQ 222
Cdd:cd18566 46 IGVVIAILLESLLRLLrsyILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIREFLTGQALLALL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 223 RMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGlsvskftdYELKAYAKAGVVAD--------EVISSMRTVAAF 294
Cdd:cd18566 125 DLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLG--------PILRRALKERSRADerrqnfliETLTGIHTIKAM 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 295 GGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18566 197 AMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVIN-GDLTVGALI 261
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
795-1012 |
2.57e-10 |
|
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: 62.87 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 795 INGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGS 874
Cdd:cd18545 39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 875 QIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGAT-QTRMLTGF-ASRDKQAlEMVGQItNEALSNIRTVAG 952
Cdd:cd18545 117 GLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLlRRRARKAWqRVRKKIS-NLNAYL-HESISGIRVIQS 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 953 IGKE----RRFIEaLETELEKPFKTAIQKANIYG----FCFAFAQCIMFIansasyrYGGYLISNEGL 1012
Cdd:cd18545 195 FAREdeneEIFDE-LNRENRKANMRAVRLNALFWplveLISALGTALVYW-------YGGKLVLGGAI 254
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1092-1301 |
3.05e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERF--YDPDQGKVMIDGHDSKKVNVQfLRSNIGI--VSQEPVLFA 1167
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflAFQYPIEIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 -CSIMDNIKYGDNTKEipmerviaaaKQAQLHD-----FVMSLPEKYETnVGSQGSQLSR--------GEKQRIAIARAI 1233
Cdd:CHL00131 98 gVSNADFLRLAYNSKR----------KFQGLPEldpleFLEIINEKLKL-VGMDPSFLSRnvnegfsgGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1234 VRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIV-IAH--RLSTIQNADIIAVMAQGVVIEKGTHE 1301
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
431-615 |
4.88e-10 |
|
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: 60.58 E-value: 4.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 431 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLFST 510
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 511 TIAENIRYGREDATMEDIVQAAKEANAYNFiMDLPqqFDTLvgegggqmSGGQKQRVAIARALIRNPKILLLDMATSALD 590
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEALARVGLNGF-EDRP--VAQL--------SAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*.
gi 21536378 591 NESEAMVQEVL-SKIQHGHTIISVAH 615
Cdd:cd03231 158 KAGVARFAEAMaGHCARGGMVVLTTH 183
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
792-999 |
5.20e-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: 62.12 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 792 RSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQG- 870
Cdd:cd18546 35 LGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSEl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 871 AAGSQIGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALsgAT-QTRMLTGFASRdkQALEMVGQIT---NEALSN 946
Cdd:cd18546 113 LQTGLVQLVVSLLTLVGIA-VVLLVLDPRLALVALAALPPLAL--ATrWFRRRSSRAYR--RARERIAAVNadlQETLAG 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 947 IRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFaqcIMFIANSAS 999
Cdd:cd18546 188 IRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPG---VELLGNLAT 237
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
427-659 |
5.71e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 61.56 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 427 FHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH--DIRSLNIQWLRDQIGIVEQE 504
Cdd:PRK13638 9 FRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 505 P--VLFSTTIAENIRYGREDATM--EDIVQAAKEA----NAYNFiMDLPQQfdtlvgegggQMSGGQKQRVAIARALIRN 576
Cdd:PRK13638 86 PeqQIFYTDIDSDIAFSLRNLGVpeAEITRRVDEAltlvDAQHF-RHQPIQ----------CLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 577 PKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISvAHRLSTV-RAADTIIGFEHGTAVERG------THEELLERK 647
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIvaQGNHVIIS-SHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAMEQA 233
|
250
....*....|...
gi 21536378 648 GVYFT-LVTLQSQ 659
Cdd:PRK13638 234 GLTQPwLVKLHTQ 246
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1091-1301 |
5.99e-10 |
|
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: 61.23 E-value: 5.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVLNGLSVsISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKV------------------------MIDGHDSKK 1146
Cdd:cd03236 12 PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildefrgselqnyftkLLEGDVKVI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1147 VNVQFlrsnigiVSQEPVLFACSIMDNIKYGD--NTKEIPMERviaaakqaqlhdfvMSLPEKYETNVgsqgSQLSRGEK 1224
Cdd:cd03236 91 VKPQY-------VDLIPKAVKGKVGELLKKKDerGKLDELVDQ--------------LELRHVLDRNI----DQLSGGEL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1225 QRIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVM-----AQGVV-IE 1296
Cdd:cd03236 146 QRVAIAAALARDADFYFFDEPSSYLDIKQRLNAaRLIRELAEDDNYVLVVEHDLAVLDYlSDYIHCLygepgAYGVVtLP 225
|
....*
gi 21536378 1297 KGTHE 1301
Cdd:cd03236 226 KSVRE 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1089-1292 |
6.00e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 63.21 E-value: 6.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVSQE-P 1163
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFksskEALENGISMVHQElN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1164 VLFACSIMDNIKYGdntkEIPMERVIaaAKQAQLHDFVMSLPEKYETNVG--SQGSQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PRK10982 84 LVLQRSVMDNMWLG----RYPTKGMF--VDQDKMYRDTKAIFDELDIDIDprAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1242 LDEATSALdteSEKTVQ---VALDKAREgRTC--IVIAHRLSTI-QNADIIAVMAQG 1292
Cdd:PRK10982 158 MDEPTSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDG 210
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
436-606 |
6.01e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 61.06 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIVEQEPVLFST-TIA 513
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 514 ENIRYG---REDATMEdivQAAKEANaynfimDLPQQFDT--LVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSA 588
Cdd:PRK10895 97 DNLMAVlqiRDDLSAE---QREDRAN------ELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170
....*....|....*...
gi 21536378 589 LDNESeamVQEVLSKIQH 606
Cdd:PRK10895 168 VDPIS---VIDIKRIIEH 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1096-1296 |
7.88e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.88 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD---QGKVMIDG--------HDSKKVNvqflrsnIGIVSQE-- 1162
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfkdiRDSEALG-------IVIIHQEla 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 --PVLfacSIMDNIKYGDntkEIPMERVI----AAAKQAQLHDFVmSLPEKYETNVGSQGSqlsrGEKQRIAIARAIVRD 1236
Cdd:NF040905 89 liPYL---SIAENIFLGN---ERAKRGVIdwneTNRRARELLAKV-GLDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 1237 PKILLLDEATSAL-DTESEKTVQVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQGVVIE 1296
Cdd:NF040905 158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
174-366 |
8.37e-10 |
|
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: 61.70 E-value: 8.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 174 MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDaiadqMA------LFIQrmTSTICG-FLLGFFRGWKLTLVII 246
Cdd:cd18549 77 MRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISE-----LAhhgpedLFIS--IITIIGsFIILLTINVPLTLIVF 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 247 SVSPLIGIGAATIGLsvsKFTDYELKAYAKAGVVADEV---ISSMRTVAAFGGEKREVERYEK-NLVF--AQRWGIRkgi 320
Cdd:cd18549 150 ALLPLMIIFTIYFNK---KMKKAFRRVREKIGEINAQLedsLSGIRVVKAFANEEYEIEKFDEgNDRFleSKKKAYK--- 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 321 VMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVQIFLSV 366
Cdd:cd18549 224 AMAYFFSGMNFFTNLLNLVVLVAGGYFII-KGEITLGDLVAFLLYV 268
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1097-1303 |
9.88e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.77 E-value: 9.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1097 NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-----SKKV----------NVQFLRS-----NI 1156
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHieglpGHQIarmgvvrtfqHVRLFREmtvieNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1157 gIVSQ----EPVLFAcSIMDNIKYGDNTKEiPMERVIAAAKQAQLHDFVmslpekyetnvGSQGSQLSRGEKQRIAIARA 1232
Cdd:PRK11300 102 -LVAQhqqlKTGLFS-GLLKTPAFRRAESE-ALDRAATWLERVGLLEHA-----------NRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 1233 IVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEEL 1303
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
760-966 |
1.45e-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: 350009 [Multi-domain] Cd Length: 313 Bit Score: 61.04 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 760 VGAAVNGTV--TPLYAFLFSQILGTfsipdkEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFR 837
Cdd:cd18565 22 IGVAIDAVFngEASFLPLVPASLGP------ADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 838 AMLGQDIAWFDDlrNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLAL-SGA 916
Cdd:cd18565 96 HVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAgTYW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21536378 917 TQTRMLTGFASRDKQALEMVGQITNeALSNIRTVAGIGKERRFIEALETE 966
Cdd:cd18565 174 FQRRIEPRYRAVREAVGDLNARLEN-NLSGIAVIKAFTAEDFERERVADA 222
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
757-1010 |
1.94e-09 |
|
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: 60.25 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 757 VGSVGAAVNGTVTPLyafLFSQILGTFSIPDKEEQRSQINGV-------CLLFVAMgcvSLFTqFLQGYAFAKSGELLTK 829
Cdd:cd18574 3 LSALAAALVNIQIPL---LLGDLVNVISRSLKETNGDFIEDLkkpalklLGLYLLQ---SLLT-FAYISLLSVVGERVAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 830 RLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 909
Cdd:cd18574 76 RLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 910 FLALSGATQTRMLTGFAsrdKQALEMVGQITN---EALSNIRTVAGIGKERRFIEALETELEKPFKTAIQkaniYGFCFA 986
Cdd:cd18574 154 VVVLVGTLYGSFLRKLS---RRAQAQVAKATGvadEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK----LGLGIG 226
|
250 260
....*....|....*....|....*...
gi 21536378 987 FAQCIMFIA-NS---ASYRYGGYLISNE 1010
Cdd:cd18574 227 IFQGLSNLAlNGivlGVLYYGGSLVSRG 254
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1089-1254 |
1.96e-09 |
|
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: 59.04 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFAC 1168
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNIKY--GDNTKeipmERVIAAAKQAQLHDFvmslpEKYETNvgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEAT 1246
Cdd:cd03231 89 SVLENLRFwhADHSD----EQVEEALARVGLNGF-----EDRPVA------QLSAGQQRRVALARLLLSGRPLWILDEPT 153
|
....*...
gi 21536378 1247 SALDTESE 1254
Cdd:cd03231 154 TALDKAGV 161
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
420-636 |
2.92e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.82 E-value: 2.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRP--------------------EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFY--DPCEG 477
Cdd:COG2401 8 FVLMRVTKVYSSVLdlservaivleafgvelrvvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 478 MVTVDghdirslNIQWLRDqigiveqepvlfsTTIAENI-RYGREDATMEdIVQAAKEANAYNFI-----MDLPQQFdtl 551
Cdd:COG2401 88 CVDVP-------DNQFGRE-------------ASLIDAIgRKGDFKDAVE-LLNAVGLSDAVLWLrrfkeLSTGQKF--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 552 vgegggqmsggqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA--ADTII 627
Cdd:COG2401 144 --------------RFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLarRAGITLVVATHHYDVIDDlqPDLLI 209
|
....*....
gi 21536378 628 GFEHGTAVE 636
Cdd:COG2401 210 FVGYGGVPE 218
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
166-390 |
3.13e-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: 350051 [Multi-domain] Cd Length: 293 Bit Score: 59.86 E-value: 3.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 166 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIqrmTST-----ICGFLlgFFRGWK 240
Cdd:cd18778 67 AEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI---TNVltlvgVAIIL--FSINPK 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 241 LTLVIISVSPLIGIGAAtiglsvsKFTDYELKAYAKA--------GVVADEvISSMRTVAAFGGEKREVERYEK------ 306
Cdd:cd18778 142 LALLTLIPIPFLALGAW-------LYSKKVRPRYRKVrealgelnALLQDN-LSGIREIQAFGREEEEAKRFEAlsrryr 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 307 --NLVFAQRWGIrKGIVMGFFTGfvwclifLCYALAFWYGSTLVLDeGEYTPGTLVQIFLSVI-----VGALNLGNaspc 379
Cdd:cd18778 214 kaQLRAMKLWAI-FHPLMEFLTS-------LGTVLVLGFGGRLVLA-GELTIGDLVAFLLYLGlfyepITSLHGLN---- 280
|
250
....*....|.
gi 21536378 380 lEAFATGRAAA 390
Cdd:cd18778 281 -EMLQRALAGA 290
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1089-1300 |
3.39e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKST-SIQLLERF-YDPDQGKVMIDGHDSKKVNVQfLRSNIGI--VSQEPV 1164
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 --------LFACSIMDNI-KYGDNTkeiPMERViaaakqaQLHDFV------MSLPEKYET---NVGSQGsqlsrGEKQR 1226
Cdd:PRK09580 89 eipgvsnqFFLQTALNAVrSYRGQE---PLDRF-------DFQDLMeekialLKMPEDLLTrsvNVGFSG-----GEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1227 IAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREG-RTCIVIAH--RLSTIQNADIIAVMAQGVVIEKGTH 1300
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1085-1252 |
4.08e-09 |
|
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: 58.57 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRpdSQVLNGLSVSISPG-----QTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDskkvnvqflrsnigiV 1159
Cdd:cd03237 1 YTYPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------V 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1160 SQEPVLFacsimdNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSlPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPKI 1239
Cdd:cd03237 64 SYKPQYI------KADYEGTVRDLLSSITKDFYTHPYFKTEIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADI 136
|
170
....*....|...
gi 21536378 1240 LLLDEATSALDTE 1252
Cdd:cd03237 137 YLLDEPSAYLDVE 149
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1094-1249 |
4.20e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.74 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD-SKKVNVQFLRSNIGIVSQEPVLFA-CSIM 1171
Cdd:PRK11614 19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDiTDWQTAKIMREAVAIVPEGRRVFSrMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 DNIKYGD--NTKEIPMERViaaakqAQLHDFvmsLPEKYETNVGSQGSqLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PRK11614 99 ENLAMGGffAERDQFQERI------KWVYEL---FPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1089-1306 |
5.73e-09 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.35 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQV--LNGLSVSISPGQTLAFVGSSGCGKS-TSIQLLERFYDPDQ--GKVMIDGHD-----SKKVNVqfLRS-NIG 1157
Cdd:PRK09473 23 STPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANGRigGSATFNGREilnlpEKELNK--LRAeQIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1158 IVSQEPVlfaCSIMDNIKYGDNTKEIPMerviaaakqaqLHDFvMSLPEKYETNV---------------GSQGSQLSRG 1222
Cdd:PRK09473 101 MIFQDPM---TSLNPYMRVGEQLMEVLM-----------LHKG-MSKAEAFEESVrmldavkmpearkrmKMYPHEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1223 EKQRIAIARAIVRDPKILLLDEATSALDTesekTVQVAL-----DKAREGRTCIV-IAHRLSTIQN-ADIIAVMAQGVVI 1295
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDV----TVQAQImtllnELKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTM 241
|
250
....*....|.
gi 21536378 1296 EKGTHEELMAQ 1306
Cdd:PRK09473 242 EYGNARDVFYQ 252
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
423-615 |
5.82e-09 |
|
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: 60.33 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 423 HNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLiqrfydpcegMVTVD----GHDIRSLNIQwlrdqI 498
Cdd:TIGR03719 8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI----------MAGVDkdfnGEARPQPGIK-----V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFST-TIAENI-------------------RYGREDATM----------EDIVQAAkeaNAYNFIMDLPQQF 548
Cdd:TIGR03719 71 GYLPQEPQLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFdklaaeqaelQEIIDAA---DAWDLDSQLEIAM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 549 DTLVGEGGGQMSGGQK----QRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLskIQHGHTIISVAH 615
Cdd:TIGR03719 148 DALRCPPWDADVTKLSggerRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL--QEYPGTVVAVTH 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1089-1304 |
6.07e-09 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLE-RFYDPD-------QGKVMIDGHDSKKVNVQFLRSNIGIVS 1160
Cdd:PRK13547 10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1161 Q--EPVlFACSIMDNIKYGdntkEIPMERVIAAAKQA--QLHDFVMSLPEKyETNVGSQGSQLSRGEKQRIAIARAI--- 1233
Cdd:PRK13547 90 QaaQPA-FAFSAREIVLLG----RYPHARRAGALTHRdgEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLaql 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1234 ------VRDPKILLLDEATSALD-TESEKTVQVALDKAREGRT-CIVIAHRLS-TIQNADIIAVMAQGVVIEKGTHEELM 1304
Cdd:PRK13547 164 wpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1092-1306 |
6.74e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 60.03 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHD---------SKKVNVQFLRSNIGIVSQe 1162
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHitrlsfeqlQKLVSDEWQRNNTDMLSP- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 pvlfacsimDNIKYGDNTKEIPMERVIAAAKQAQLH-----DFVMSLPEKYetnvgsqgsqLSRGEKQRIAIARAIVRDP 1237
Cdd:PRK10938 94 ---------GEDDTGRTTAEIIQDEVKDPARCEQLAqqfgiTALLDRRFKY----------LSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQ 1306
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
431-617 |
6.82e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.02 E-value: 6.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 431 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdiRSLNIQWLRDQ----IGIVEQEPV 506
Cdd:PRK10762 13 AFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqeagIGIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 507 LFST-TIAENIRYGREDATMEDIVQAAK---EANAYNFIMDLPQQFDTLVGEGGGQMSGGqkqrVAIARALIRNPKILLL 582
Cdd:PRK10762 90 LIPQlTIAENIFLGREFVNRFGRIDWKKmyaEADKLLARLNLRFSSDKLVGELSIGEQQM----VEIAKVLSFESKVIIM 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 21536378 583 DMATSAL-DNESEAMVQeVLSKIQ-HGHTIISVAHRL 617
Cdd:PRK10762 166 DEPTDALtDTETESLFR-VIRELKsQGRGIVYISHRL 201
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1091-1278 |
7.35e-09 |
|
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: 60.15 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVL-NGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvnvqflRSNIGIVSQEPVLFACS 1169
Cdd:TIGR00954 462 PNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1170 IMDNIKYGDNTKEIPMERV-----IAAAKQAQLHDFVmslpekyETNVGSQGSQ-----LSRGEKQRIAIARAIVRDPKI 1239
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLsdkdlEQILDNVQLTHIL-------EREGGWSAVQdwmdvLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190
....*....|....*....|....*....|....*....
gi 21536378 1240 LLLDEATSALDTESEKTVQVALDKAreGRTCIVIAHRLS 1278
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
144-348 |
7.52e-09 |
|
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: 58.67 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 144 YYAGIAVAVLITGYIQICFWVIA---AARQI-QKMrkfyFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMAL 219
Cdd:cd18580 44 YAALLVLASVLLVLLRWLLFVLAglrASRRLhDKL----LRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 220 FIQRMTSTICGFllgffrgwkltLVIISVSPLIGIGAATIGLSVSKFTDY------ELK---AYAKAGVVA--DEVISSM 288
Cdd:cd18580 120 FLQSLFSVLGSL-----------IVIAIVSPYFLIVLPPLLVVYYLLQRYylrtsrQLRrleSESRSPLYShfSETLSGL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 289 RTVAAFGGEKREVERYEKNL----------VFAQRWgirKGIVMGFF-TGFVWCLIFLCYALAFWYGSTLV 348
Cdd:cd18580 189 STIRAFGWQERFIEENLRLLdasqrafyllLAVQRW---LGLRLDLLgALLALVVALLAVLLRSSISAGLV 256
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
430-613 |
1.52e-08 |
|
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: 56.12 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 430 PSRPEVKILNDLNMVIKPGEMTALVGPSGAGKST---ALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQIgIVEQEPV 506
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEII-YVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 507 LFSTTiaenirygredaTMEDIVQAAKEANAYNFIMDLP--QQfdtlvgegggqmsggqkQRVAIARALIRNPKILLLDM 584
Cdd:cd03233 94 HFPTL------------TVRETLDFALRCKGNEFVRGISggER-----------------KRVSIAEALVSRASVLCWDN 144
|
170 180 190
....*....|....*....|....*....|..
gi 21536378 585 ATSALDNESE---AMVQEVLSKIQHGHTIISV 613
Cdd:cd03233 145 STRGLDSSTAleiLKCIRTMADVLKTTTFVSL 176
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
447-639 |
1.66e-08 |
|
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: 55.07 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 447 PGEMTALVGPSGAGKSTALQLIQRFYDP-CEGMVTVDGHDIRSLNIQWLRdqigiveqepvlfsttiaenirygredatm 525
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPpGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 526 edivqaakeanaynfimdlpqqfDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLS--- 602
Cdd:smart00382 51 -----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21536378 603 ----KIQHGHTIISVAHRLSTVRAADTIIGFEHGTAVERGT 639
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
431-615 |
1.84e-08 |
|
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: 55.83 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 431 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDG------HDIRSLNIQWLRDQIGIveqE 504
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplaeqRDEPHENILYLGHLPGL---K 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 505 PVLfstTIAENIRYGREDATMEDI-VQAAKEANAYNFIMDLP-------QQfdtlvgegggqmsggqkQRVAIARALIRN 576
Cdd:TIGR01189 86 PEL---SALENLHFWAAIHGGAQRtIEDALAAVGLTGFEDLPaaqlsagQQ-----------------RRLALARLWLSR 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21536378 577 PKILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAH 615
Cdd:TIGR01189 146 RPLWILDEPTTALDKAGVALLAGLLrAHLARGGIVLLTTH 185
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
145-328 |
2.01e-08 |
|
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: 57.10 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 145 YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRM 224
Cdd:cd18606 41 YAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 225 TSTICGFLLgffrgwkltlvIISVSPLIGIGAATIGLSVSKFTDY------ELK---AYAKAGVVA--DEVISSMRTVAA 293
Cdd:cd18606 121 SSIIGTFIL-----------IIIYLPWFAIALPPLLVLYYFIANYyrassrELKrleSILRSFVYAnfSESLSGLSTIRA 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536378 294 FGGEKREVERYEKN---------LVFA-QRW-GIR---KGIVMGFFTGF 328
Cdd:cd18606 190 YGAQDRFIKKNEKLidnmnrayfLTIAnQRWlAIRldlLGSLLVLIVAL 238
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1076-1252 |
2.04e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.81 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1076 GKIDFVDCKFTYpSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidgHDSKKVNVQFLRSN 1155
Cdd:PRK11147 316 GKIVFEMENVNY-QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1156 IGIVSQEPvlfacSIMDNIkyGDNTKEIPM---ERVIAaakqAQLHDFVMSlPEKYETNVgsqgSQLSRGEKQRIAIARA 1232
Cdd:PRK11147 391 RAELDPEK-----TVMDNL--AEGKQEVMVngrPRHVL----GYLQDFLFH-PKRAMTPV----KALSGGERNRLLLARL 454
|
170 180
....*....|....*....|
gi 21536378 1233 IVRDPKILLLDEATSALDTE 1252
Cdd:PRK11147 455 FLKPSNLLILDEPTNDLDVE 474
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1089-1253 |
2.24e-08 |
|
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: 55.83 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFAC 1168
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNIKYgdntkeipmerviaaakQAQLHDFVMSLPEKYETNVGSQG------SQLSRGEKQRIAIARAIVRDPKILLL 1242
Cdd:TIGR01189 89 SALENLHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWIL 151
|
170
....*....|.
gi 21536378 1243 DEATSALDTES 1253
Cdd:TIGR01189 152 DEPTTALDKAG 162
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
146-360 |
2.54e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 57.11 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMT 225
Cdd:cd18550 46 VAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 226 STICGFLLGFFRGWKLTLVIISVSPLIGIGAATIGLSVSKFTDYELKAYAKAGVVADEV--ISSMRTVAAFGGEKREVER 303
Cdd:cd18550 126 TLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAAR 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 304 YEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18550 206 FARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIG-GGLTIGTLV 261
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
179-364 |
2.58e-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: 57.19 E-value: 2.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 179 FRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIGaat 258
Cdd:cd18565 94 YDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAG--- 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 259 iglsVSKFTDYELKAYA----KAGVVA---DEVISSMRTVAAFGGEKREVERYEK--NLVFAQRWG-IRKGIVmgfFTGF 328
Cdd:cd18565 171 ----TYWFQRRIEPRYRavreAVGDLNarlENNLSGIAVIKAFTAEDFERERVADasEEYRDANWRaIRLRAA---FFPV 243
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21536378 329 VWCLIFLCYALAFWYGSTLVLD-----EGEYTPGTLVqIFL 364
Cdd:cd18565 244 IRLVAGAGFVATFVVGGYWVLDgpplfTGTLTVGTLV-TFL 283
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
431-615 |
3.22e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 431 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSL------NIQWLRDQIGIveqE 504
Cdd:PRK13538 10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 505 PVLfstTIAENIRY---GREDATMEDIVQAAKEANAYNFiMDLP-------QQfdtlvgegggqmsggqkQRVAIARALI 574
Cdd:PRK13538 87 TEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVPvrqlsagQQ-----------------RRVALARLWL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536378 575 RNPKILLLDMATSALDNESEAMVQEVLSK-IQHGHTIISVAH 615
Cdd:PRK13538 146 TRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1078-1284 |
3.22e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1078 IDFVDCKFTYPSRPdsqVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKK------VNVQF 1151
Cdd:PRK13540 2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlctyqKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1152 LRSNIGIvsqEPVLfacSIMDNIKYGDNTKEIPME--RVIAAAKQAQLHDFVMSLpekyetnvgsqgsqLSRGEKQRIAI 1229
Cdd:PRK13540 79 VGHRSGI---NPYL---TLRENCLYDIHFSPGAVGitELCRLFSLEHLIDYPCGL--------------LSSGQKRQVAL 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 1230 ARAIVRDPKILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQNAD 1284
Cdd:PRK13540 139 LRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
148-360 |
3.49e-08 |
|
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: 56.41 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 148 IAVAVLITGYIQIcfwVIAAARQI---QKMRKF-------YFRRIMRMEIGWFDCNSVGELNTRFSDDiNKINDAIADQ- 216
Cdd:cd18568 44 ILIGLLIVGIFQI---LLSAVRQYlldYFANRIdlsllsdFYKHLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSa 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 217 MALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPLIgigaATIGLSVSKFTDYELKAYAKAGVVAD----EVISSMRTVA 292
Cdd:cd18568 120 LTTILDLLMVFIYLGLM-FYYNLQLTLIVLAFIPLY----VLLTLLSSPKLKRNSREIFQANAEQQsflvEALTGIATIK 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 293 AFGGEKREVERYEK---NLVFAQRWGIRKGIVMGFFTGFvwcLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18568 195 ALAAERPIRWRWENkfaKALNTRFRGQKLSIVLQLISSL---INHLGTIAVLWYGAYLVIS-GQLTIGQLV 261
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
437-644 |
3.56e-08 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 56.37 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRfyDPCE----------GMVTVDGHDIRSLNIQWLRDQIGIVEQ--E 504
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG--DLTGggaprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 505 PVlFSTTIAENIRYGR----------EDATMEDIVQAAKEANAynfimdlpqqfDTLVGEGGGQMSGGQKQRVAIARAL- 573
Cdd:PRK13547 94 PA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELARVQFARVLa 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 574 --------IRNPKILLLDMATSALDNESE----AMVQEVLSKIQHGhtIISVAHRLS-TVRAADTIIGFEHGTAVERGTH 640
Cdd:PRK13547 162 qlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLG--VLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239
|
....
gi 21536378 641 EELL 644
Cdd:PRK13547 240 ADVL 243
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1092-1309 |
5.23e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.21 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidgHDSKKvnvqflrSNIGIVSQEPVL-FAC-- 1168
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSEN-------ANIGYYAQDHAYdFENdl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNI----KYGDNtkeipmERVIAAAkqaqLHDFVMSlpekyETNVGSQGSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK15064 400 TLFDWMsqwrQEGDD------EQAVRGT----LGRLLFS-----QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1245 ATSALDTESEKTVQVALDKArEGrTCIVIAH------RLSTiqnaDIIAVMAQGVVIEKGTHEELMAQKGA 1309
Cdd:PRK15064 465 PTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
420-643 |
5.55e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 55.54 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFhypSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL---RD 496
Cdd:PRK11831 8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEPVLFS-TTIAENIRYG-RE-----DATMEDIVQAAKEANAYNFIMDL-PQQFDtlvgegggqmsGGQKQRVA 568
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAYPlREhtqlpAPLLHSTVMMKLEAVGLRGAAKLmPSELS-----------GGMARRAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 569 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADT--IIGFEHgtAVERGTHEEL 643
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHayIVADKK--IVAHGSAQAL 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1089-1252 |
6.21e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 6.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1089 SRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNvqflRSN-IGIVSQEPVLFA 1167
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 -CSIMDNIKY-----GDNTKEIPMERVIaaakqaqlhdfVMSLPEKYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILL 1241
Cdd:PRK13543 96 dLSTLENLHFlcglhGRRAKQMPGSALA-----------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWL 160
|
170
....*....|.
gi 21536378 1242 LDEATSALDTE 1252
Cdd:PRK13543 161 LDEPYANLDLE 171
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
434-654 |
7.27e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.86 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQ----LIQrfydPCEGMVTVDGHDIRSLNIQWLRdQIGIV----EQ-- 503
Cdd:COG4586 34 EVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKmltgILV----PTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 504 --EPVLFSTTIAENIrYGREDA----TMEDIVQaakeanaynfIMDLPQQFDTLVgegggqmsggqkqR---------VA 568
Cdd:COG4586 109 wdLPAIDSFRLLKAI-YRIPDAeykkRLDELVE----------LLDLGELLDTPV-------------RqlslgqrmrCE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 569 IARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTVRA-ADTIIGFEHGTAVERGTHEELLE 645
Cdd:COG4586 165 LAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244
|
....*....
gi 21536378 646 RKGVYFTLV 654
Cdd:COG4586 245 RFGPYKTIV 253
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1029-1313 |
8.13e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1029 TALGRAFSYTPSYAKAKISAARF--FQLLDRQPPISVYNtAGEKWDnfqgKIDFVDCKFTYPSRPDSqvLNGLSVSISPG 1106
Cdd:PRK10522 277 TPLLSAVGALPTLLSAQVAFNKLnkLALAPYKAEFPRPQ-AFPDWQ----TLELRNVTFAYQDNGFS--VGPINLTIKRG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1107 QTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGHDSKKVNVQFLRSNIGIVSQEPVLFACSImdnikyGDNTKEIPME 1186
Cdd:PRK10522 350 ELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEGKPANPA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1187 RVIAAAKQAQLHDFVmSLPEKYETNVgsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAR 1265
Cdd:PRK10522 424 LVEKWLERLKMAHKL-ELEDGRISNL-----KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQ 497
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 21536378 1266 E-GRTCIVIAHRLSTIQNADIIAVMAQGVVIEKGTHEELMAQKGAYYKL 1313
Cdd:PRK10522 498 EmGKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASRDAVART 546
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
434-619 |
8.61e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQ-RFYDPC-EGMVTVDGhdiRSLNIQWLRdQIGIVEQEPVLFS-T 510
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 511 TIAENIRYGREDATMEDIVQAAKEANAYNFI--MDLPQQFDTLV-GEGGGQMSGGQKQRVAIARALIRNPKILLLDMATS 587
Cdd:PLN03211 156 TVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIgNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190
....*....|....*....|....*....|...
gi 21536378 588 ALDNESE-AMVQEVLSKIQHGHTIISVAHRLST 619
Cdd:PLN03211 236 GLDATAAyRLVLTLGSLAQKGKTIVTSMHQPSS 268
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
424-643 |
9.41e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.50 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 424 NVTFHYPSrPEVKILNDLNMVIKPGEMTALVGPSGAGKS-TALQLIQRFYDP--CEGMVTVDGHDIRSLN---IQWLR-D 496
Cdd:PRK09473 19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPekeLNKLRaE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 497 QIGIVEQEP----------------VLF-------STTIAENIRygredatMEDIV---QAAKEANAYnfimdlPQQFdt 550
Cdd:PRK09473 98 QISMIFQDPmtslnpymrvgeqlmeVLMlhkgmskAEAFEESVR-------MLDAVkmpEARKRMKMY------PHEF-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 551 lvgegggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVRA-ADTII 627
Cdd:PRK09473 163 ---------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVL 233
|
250
....*....|....*.
gi 21536378 628 GFEHGTAVERGTHEEL 643
Cdd:PRK09473 234 VMYAGRTMEYGNARDV 249
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
146-360 |
1.79e-07 |
|
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: 54.41 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQIcFWVIAAARQIQ-KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIAdqMALFIQRM 224
Cdd:cd18543 46 LALGVAEAVLSFLRR-YLAGRLSLGVEhDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA--FGPFLLGN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 225 TSTIC-GFLLGFFRGWKLTLVIISVSPLIGIGAAtigLSVSKFTDYELKAYAKAGVVA---DEVISSMRTVAAFGGEKRE 300
Cdd:cd18543 123 LLTLVvGLVVMLVLSPPLALVALASLPPLVLVAR---RFRRRYFPASRRAQDQAGDLAtvvEESVTGIRVVKAFGRERRE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 301 VERYEK--NLVFAQRwgIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18543 200 LDRFEAaaRRLRATR--LRAARLRARFWPLLEALPELGLAAVLALGGWLVAN-GSLTLGTLV 258
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
145-329 |
1.98e-07 |
|
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: 54.40 E-value: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 145 YAGIAVAVLITGYIQICFWVIA---AARQI-QKMrkfyFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALF 220
Cdd:cd18604 49 YALISLLSVLLGTLRYLLFFFGslrASRKLhERL----LHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 221 IQRMTSTICGFllgffrgwkltLVIISVSP---LIGIGAATIGLSVSKFtdY-----ELK---AYAKAGVVA--DEVISS 287
Cdd:cd18604 125 LESTLSLLVIL-----------IAIVVVSPaflLPAVVLAALYVYIGRL--YlrasrELKrleSVARSPILShfGETLAG 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 21536378 288 MRTVAAFGGEKREVER-YEK---------NLVFAQRW-GIRKGIVMGFFTGFV 329
Cdd:cd18604 192 LVTIRAFGAEERFIEEmLRRidrysrafrYLWNLNRWlSVRIDLLGALFSFAT 244
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1086-1253 |
2.17e-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: 55.33 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTsiqLLerfydpdqgKVM--IDghdsKKVNVQFLRS---NIGIVS 1160
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RIMagVD----KDFNGEARPQpgiKVGYLP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1161 QEP-----------VLFACS----IMD-----NIKYGDNTKEipMERViaAAKQAQLHDFV------------------M 1202
Cdd:TIGR03719 75 QEPqldptktvrenVEEGVAeikdALDrfneiSAKYAEPDAD--FDKL--AAEQAELQEIIdaadawdldsqleiamdaL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1203 SLPEKyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1253
Cdd:TIGR03719 151 RCPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
434-645 |
2.41e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.25 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLN---IQWLRDQIGIVEQEPV---- 506
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPYasld 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 507 ---LFSTTIAENIRY-----GREDAT-----MEDIVQAAKEANAYnfimdlPQQFDtlvgegggqmsGGQKQRVAIARAL 573
Cdd:PRK10261 416 prqTVGDSIMEPLRVhgllpGKAAAArvawlLERVGLLPEHAWRY------PHEFS-----------GGQRQRICIARAL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 574 IRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEELLE 645
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIGPRRAVFE 553
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
386-620 |
2.50e-07 |
|
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: 54.83 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 386 GRAAATSIFETIDRKPIIDCMSedGYKLD--------RIKGEI-EFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGP 456
Cdd:TIGR02633 217 GQHVATKDMSTMSEDDIITMMV--GREITslyphephEIGDVIlEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 457 SGAGKSTALQLIQRFYD-PCEGMVTVDGH--DIRSLnIQWLRDQI----------GIVEQEPVLFSTTIAENIRY---GR 520
Cdd:TIGR02633 295 VGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNP-AQAIRAGIamvpedrkrhGIVPILGVGKNITLSVLKSFcfkMR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 521 EDATMED--IVQAAKEANAYNFIMDLP--------QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALD 590
Cdd:TIGR02633 374 IDAAAELqiIGSAIQRLKVKTASPFLPigrlsggnQQ------------------KAVLAKMLLTNPRVLILDEPTRGVD 435
|
250 260 270
....*....|....*....|....*....|.
gi 21536378 591 NESEAMVQEVLSKI-QHGHTIISVAHRLSTV 620
Cdd:TIGR02633 436 VGAKYEIYKLINQLaQEGVAIIVVSSELAEV 466
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
438-644 |
2.63e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 53.31 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdPCEGMVTVDGHDIRSLNIQ-------WLRDQigiveQEPVLF-- 508
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQ-----QSPPFAmp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 -----STTIAENIRYGREDATMEDIVQAAKeanaynfIMD-LPQQFDTLvgegggqmSGGQKQRVAIARALIR-----NP 577
Cdd:COG4138 86 vfqylALHQPAGASSEAVEQLLAQLAEALG-------LEDkLSRPLTQL--------SGGEWQRVRLAAVLLQvwptiNP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 578 --KILLLDMATSALDNESEAMVQEVLSKI-QHGHTIISVAHRLS-TVRAADTIIGFEHGTAVERGTHEELL 644
Cdd:COG4138 151 egQLLLLDEPMNSLDVAQQAALDRLLRELcQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
166-360 |
2.94e-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: 53.75 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 166 AAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLV 244
Cdd:cd18782 69 TANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTAlTTLLDVLFSVIYIAVL-FSYSPLLTLV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 245 IISVSPLIGIgaatIGLSVSKFTDYELKAYAKAGVVAD----EVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGI 320
Cdd:cd18782 147 VLATVPLQLL----LTFLFGPILRRQIRRRAEASAKTQsylvESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTV 222
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 21536378 321 VMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLV 360
Cdd:cd18782 223 LGTTSGSLSQFLNKLSSLLVLWVGAYLVL-RGELTLGQLI 261
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1092-1286 |
3.43e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.18 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIdgHDSKKVNVQ-----FLRSNIGIVSQEPVLf 1166
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAkpyctYIGHNLGLKLEMTVF- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 acsimDNIKYgdnTKEI--PMERVIAAAKQAQLHDFvmsLPEKYETnvgsqgsqLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:PRK13541 89 -----ENLKF---WSEIynSAETLYAAIHYFKLHDL---LDEKCYS--------LSSGMQKIVAIARLIACQSDLWLLDE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 21536378 1245 ATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQNADII 1286
Cdd:PRK13541 150 VETNLSKENRDLLnNLIVMKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
830-964 |
3.60e-07 |
|
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: 53.24 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 830 RLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIGMIVNSFTNVTVAMIIAFSFSWKLSLVILCFFP 909
Cdd:cd18589 70 RLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLP 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 910 FLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKE----RRFIEALE 964
Cdd:cd18589 148 LLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEegeaQRYRQRLQ 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1088-1305 |
4.49e-07 |
|
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: 54.06 E-value: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1088 PSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPDQ--GKVMIDGHDSKKVN-VQFLRSNIGIVSQE-- 1162
Cdd:TIGR02633 268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFINGKPVDIRNpAQAIRAGIAMVPEDrk 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1163 -----PVLfacSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSqLSRGEKQRIAIARAIVRDP 1237
Cdd:TIGR02633 347 rhgivPIL---GVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGR-LSGGNQQKAVLAKMLLTNP 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1238 KILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQN-ADIIAVMAQG-----VVIEKGTHEELMA 1305
Cdd:TIGR02633 423 RVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGklkgdFVNHALTQEQVLA 497
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1096-1287 |
4.71e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQ-----TLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidghdSKKVNV----QFLRSNI-GIVSQepvl 1165
Cdd:PRK13409 350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------DPELKIsykpQYIKPDYdGTVED---- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1166 FACSIMDNikYGDN--TKEIpmerviaaAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLD 1243
Cdd:PRK13409 420 LLRSITDD--LGSSyyKSEI--------IKPLQLERL-------LDKNV----KDLSGGELQRVAIAACLSRDADLYLLD 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 21536378 1244 EATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIqnaDIIA 1287
Cdd:PRK13409 479 EPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI---DYIS 521
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
433-590 |
4.79e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 4.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 433 PEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI----QRFYDPCEGMVTVDGHDIRSLNIQWLRDQIGIVEQEPVLF 508
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 STTIAENIRYG--------REDATMEDiVQAAKEANAYNFIMDLPQQFDTLV-GEGGGQMSGGQKQRVAIARALIRNPKI 579
Cdd:TIGR00956 152 HLTVGETLDFAarcktpqnRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVgNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170
....*....|.
gi 21536378 580 LLLDMATSALD 590
Cdd:TIGR00956 231 QCWDNATRGLD 241
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
420-468 |
7.59e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 7.59e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLI 468
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI 306
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1091-1305 |
8.26e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.01 E-value: 8.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1091 PDSQVLNGLSVSISPGQTLAFVGSSGCGKSTS----IQLLERFYDPDQGKVMIDGhdsKKVNVQFLRsniGIVsqepvlf 1166
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDG---KPVAPCALR---GRK------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 ACSIMDNIK--------YGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARAIVRDPK 1238
Cdd:PRK10418 81 IATIMQNPRsafnplhtMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALLCEAP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1239 ILLLDEATSALDTESEKTVQVALDK--AREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMA 1305
Cdd:PRK10418 161 FIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
146-360 |
8.99e-07 |
|
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: 52.11 E-value: 8.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVLITGYIQICFWVIAAARQIQKM----RKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMA-LF 220
Cdd:cd18546 42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLlydlRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVqLV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 221 IQRMTSTICGFLLGFFRgWKLTLVIISVSPLIGIgaATIglsvsKFTDYELKAYAK-----AGVVAD--EVISSMRTVAA 293
Cdd:cd18546 122 VSLLTLVGIAVVLLVLD-PRLALVALAALPPLAL--ATR-----WFRRRSSRAYRRareriAAVNADlqETLAGIRVVQA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 294 FGGEKREVERY-EKNLVF--AQRWGIRkgiVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18546 194 FRRERRNAERFaELSDDYrdARLRAQR---LVAIYFPGVELLGNLATAAVLLVGAWRVAA-GTLTVGVLV 259
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
419-501 |
1.02e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 53.05 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 419 EIEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWLRDQI 498
Cdd:PRK10522 322 TLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
...
gi 21536378 499 GIV 501
Cdd:PRK10522 400 SAV 402
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
147-360 |
2.28e-06 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain] Cd Length: 294 Bit Score: 51.01 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 147 GIAVAVLITGYIQICF---WVIAAAR---QIQKMRKFyFRRIMRMEIGWFDCNSVGELNTRFSDdinkiNDAIADqmaLF 220
Cdd:cd18779 45 GLGLAALVLTQLLAGLlrsHLLLRLRtrlDTQLTLGF-LEHLLRLPYRFFQQRSTGDLLMRLSS-----NATIRE---LL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 221 IQRMTSTIC--GFLLGFFrgwkltLVIISVSPL-----IGIGAATIGL------SVSKFTDYELKAYAKAGVVADEVISS 287
Cdd:cd18779 116 TSQTLSALLdgTLVLGYL------ALLFAQSPLlglvvLGLAALQVALllatrrRVRELMARELAAQAEAQSYLVEALSG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 288 MRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18779 190 IETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLD-GQLSLGTML 261
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1217-1294 |
2.46e-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: 51.71 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1217 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALD-TESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVM----- 1289
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAILDYlADYVHILygepg 290
|
....*
gi 21536378 1290 AQGVV 1294
Cdd:COG1245 291 VYGVV 295
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
420-669 |
2.46e-06 |
|
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: 51.73 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPsrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRF--YDPCEGMVTVdgHDIRSLNIQWLRDQ 497
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIY--HVALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 498 IGIVEQEPVLFST-------------TIAENIR-------------YGrEDATMEDIVQAAKEA-----NAYNFIMDLPQ 546
Cdd:TIGR03269 76 SKVGEPCPVCGGTlepeevdfwnlsdKLRRRIRkriaimlqrtfalYG-DDTVLDNVLEALEEIgyegkEAVGRAVDLIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 547 --QFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSK--IQHGHTIISVAHRLSTV-R 621
Cdd:TIGR03269 155 mvQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIeD 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 21536378 622 AADTIIGFEHGTAVERGTHEELLErkgVYFTLVTLQSQGNQALNEEDI 669
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGEPI 279
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
420-590 |
3.98e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.61 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPEVkiLNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQwLRDqIG 499
Cdd:PRK11650 4 LKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRD-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFS-TTIAENIRYGREDATM------EDIVQAAKeanaynfIMDL-------PQQFdtlvgegggqmSGGQKQ 565
Cdd:PRK11650 80 MVFQNYALYPhMSVRENMAYGLKIRGMpkaeieERVAEAAR-------ILELeplldrkPREL-----------SGGQRQ 141
|
170 180
....*....|....*....|....*
gi 21536378 566 RVAIARALIRNPKILLLDMATSALD 590
Cdd:PRK11650 142 RVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
423-638 |
4.25e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 4.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 423 HNVTFHYPSRpevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIQWL-------- 494
Cdd:PRK11701 10 RGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 495 -RDQIGIVEQEP-------VLFSTTIAENI------RYGREDATMEDIVQAAKEANAYnfIMDLPQQFdtlvgegggqmS 560
Cdd:PRK11701 87 lRTEWGFVHQHPrdglrmqVSAGGNIGERLmavgarHYGDIRATAGDWLERVEIDAAR--IDDLPTTF-----------S 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 561 GGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQH--GHTIISVAHRLSTVR-AADTIIGFEHGTAVER 637
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARlLAHRLLVMKQGRVVES 233
|
.
gi 21536378 638 G 638
Cdd:PRK11701 234 G 234
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
1096-1286 |
4.61e-06 |
|
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: 49.54 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQ------LLERFY----DPDQGKvMIDGHD--SKKVNV------QFLRSN-- 1155
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLHlkkeQPGNHD-RIEGLEhiDKVIVIdqspigRTPRSNpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1156 --IGIVSQEPVLFaCSIMDNIKYGDNTKEIPME-RVIA-----AAKQAqlHDFVMSLP---EKYET---------NVGSQ 1215
Cdd:cd03271 90 tyTGVFDEIRELF-CEVCKGKRYNRETLEVRYKgKSIAdvldmTVEEA--LEFFENIPkiaRKLQTlcdvglgyiKLGQP 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1216 GSQLSRGEKQRIAIARAIVR---DPKILLLDEATSALDTESEKTVQVALDKARE-GRTCIVIAHRLSTIQNADII 1286
Cdd:cd03271 167 ATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
114-261 |
4.80e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), 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: 350045 [Multi-domain] Cd Length: 314 Bit Score: 50.01 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 114 WTNSSLNQNMT----NGTRCGLLNIESEMIKFASY-YAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIG 188
Cdd:cd18601 29 WANLEEKLNDTtdrvQGENSTNVDIEDLDRDFNLGiYAGLTAATFVFGFLRSLLFFHVAVSASKNLHNKMFASVLRAPIR 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 189 WFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTsTICGFLlgffrgwkltLVIISVSPLIGIGAATIGL 261
Cdd:cd18601 109 FFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLL-QVVGVV----------LLAVVVNPWVLIPVIPLVI 170
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1086-1253 |
4.91e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 4.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1086 TYPsrPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTsiqLLerfydpdqgKVM--IDghdsKKVNVQFLRS---NIGIVS 1160
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKST---LL---------RIMagVD----KEFEGEARPApgiKVGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1161 QEPVLfacsimdnikygDNTK---EIPMERV------------IAA-------------AKQAQLHDFV----------- 1201
Cdd:PRK11819 77 QEPQL------------DPEKtvrENVEEGVaevkaaldrfneIYAayaepdadfdalaAEQGELQEIIdaadawdldsq 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1202 -------MSLPEKyETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTES 1253
Cdd:PRK11819 145 leiamdaLRCPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1217-1294 |
8.11e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1217 SQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAREGRTCIVIAHRLSTIQN-ADIIAVM-----A 1290
Cdd:PRK13409 211 SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLDYlADNVHIAygepgA 290
|
....
gi 21536378 1291 QGVV 1294
Cdd:PRK13409 291 YGVV 294
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1092-1280 |
8.82e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL-ERFYDP--DQGKVMIDGHdskKVNVQFLRSnIGIVSQEPV-LFA 1167
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTGviTGGDRLVNGR---PLDSSFQRS-IGYVQQQDLhLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1168 CSIMDNIKYG---DNTKEIP----MERViaaakqaqlhDFVMSLPE--KY-ETNVGSQGSQLSRGEKQRIAIARAIVRDP 1237
Cdd:TIGR00956 851 STVRESLRFSaylRQPKSVSksekMEYV----------EEVIKLLEmeSYaDAVVGVPGEGLNVEQRKRLTIGVELVAKP 920
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536378 1238 KILL-LDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTI 1280
Cdd:TIGR00956 921 KLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
436-590 |
9.31e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 9.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 436 KILNDLNMVIK---PGE-MTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGH---DIRS-LNIQWLRDQIGIVEQEPVL 507
Cdd:PRK11144 8 QQLGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgICLPPEKRRIGYVFQDARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 508 FS-TTIAENIRYGReDATMedivqaakeanaynfimdlPQQFDTLVGEGGGQMSGG---------QKQRVAIARALIRNP 577
Cdd:PRK11144 88 FPhYKVRGNLRYGM-AKSM-------------------VAQFDKIVALLGIEPLLDrypgslsggEKQRVAIGRALLTAP 147
|
170
....*....|...
gi 21536378 578 KILLLDMATSALD 590
Cdd:PRK11144 148 ELLLMDEPLASLD 160
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
423-615 |
1.13e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.73 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 423 HNVTFHYPsrPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLiqrfydpcegMVTVD----GHDIRSLNIQwlrdqI 498
Cdd:PRK11819 10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRI----------MAGVDkefeGEARPAPGIK-----V 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 499 GIVEQEPVLFST-TIAENI-------------------RYGREDATM----------EDIVQAAkeaNAYNF------IM 542
Cdd:PRK11819 73 GYLPQEPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDADFdalaaeqgelQEIIDAA---DAWDLdsqleiAM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 543 D---LPQQfDTLVGEGGGQMSGgqkqRVAIARALIRNPKILLLDMATSALDNESEAMVQevlskiQHGH----TIISVAH 615
Cdd:PRK11819 150 DalrCPPW-DAKVTKLSGGERR----RVALCRLLLEKPDMLLLDEPTNHLDAESVAWLE------QFLHdypgTVVAVTH 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1085-1250 |
1.24e-05 |
|
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: 47.64 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1085 FTYPSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL----ERFYDPDqGKVMIDGHDSKKVNVQFlRSNIGIVS 1160
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtEGNVSVE-GDIHYNGIPYKEFAEKY-PGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1161 QEPVLFAcsimdnikygdntkEIPMERVIAAAKQAQLHDFVmslpekyetnvgsqgSQLSRGEKQRIAIARAIVRDPKIL 1240
Cdd:cd03233 90 EEDVHFP--------------TLTVRETLDFALRCKGNEFV---------------RGISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 21536378 1241 LLDEATSALD 1250
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1218-1305 |
1.27e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1218 QLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTI-QNADIIAVMAQGVV 1294
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 21536378 1295 IEKGTHEELMA 1305
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1095-1305 |
1.37e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 49.25 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL--ERfyDPDQGKVMIDGHDSKKVNV-QFLRSNIGIVSQEPVLFAC--- 1168
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGVAYIPEDRLGRGLvpd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 -SIMDNI---KYGDNtkeiPMER--VI---AAAKQAQlhdfvmSLPEKYE---TNVGSQGSQLSRGEKQRIAIARAIVRD 1236
Cdd:COG3845 351 mSVAENLilgRYRRP----PFSRggFLdrkAIRAFAE------ELIEEFDvrtPGPDTPARSLSGGNQQKVILARELSRD 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1237 PKILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQN-ADIIAVMAQG-----VVIEKGTHEEL---MA 1305
Cdd:COG3845 421 PKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGrivgeVPAAEATREEIgllMA 499
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1095-1305 |
1.38e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 49.25 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1095 VLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLerF--YDPDQGKVMIDGhdsKKVNV----QFLRSNIGIVS----QEPV 1164
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgaDPADSGEIRLDG---KPVRIrsprDAIRAGIAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1165 LFACSIMDNI------KYGDNtkeipmeRVIAAAKQAQL-HDFVMSLPEKY---ETNVGSqgsqLSRGEKQRIAIARAIV 1234
Cdd:COG1129 342 VLDLSIRENItlasldRLSRG-------GLLDRRRERALaEEYIKRLRIKTpspEQPVGN----LSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1235 RDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIahrlST-----IQNADIIAVMAQGVVI-----EKGTHEEL 1303
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVI----SSelpelLGLSDRILVMREGRIVgeldrEEATEEAI 486
|
..
gi 21536378 1304 MA 1305
Cdd:COG1129 487 MA 488
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1096-1287 |
1.84e-05 |
|
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: 49.01 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQ-----TLAFVGSSGCGKSTSIQLLERFYDPDQGKVmidghdSKKVNV----QFLRSNIGIVSQEpVLF 1166
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLKIsykpQYISPDYDGTVEE-FLR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 AC--SIMDNIKYgdNTkEIpmerviaaAKQAQLHDFvmslpekYETNVgsqgSQLSRGEKQRIAIARAIVRDPKILLLDE 1244
Cdd:COG1245 424 SAntDDFGSSYY--KT-EI--------IKPLGLEKL-------LDKNV----KDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 21536378 1245 ATSALDTESEKTVQVALDKAREGR--TCIVIAHRLSTIqnaDIIA 1287
Cdd:COG1245 482 PSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIS 523
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
148-360 |
1.94e-05 |
|
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: 47.89 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 148 IAVAVLITGYIQICFwVIAAARQIQKMRKF--------YFRRIMRMEIGWFDCNSVGELNTRFSdDINKINDAIADQMAL 219
Cdd:cd18555 44 LGIGILILFLLYGLF-SFLRGYIIIKLQTKldkslmsdFFEHLLKLPYSFFENRSSGDLLFRAN-SNVYIRQILSNQVIS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 220 FIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIGIgaaTIGLS---VSKFTDYELKAYAKAGVVADEVISSMRTVAAFGG 296
Cdd:cd18555 122 LIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVL---LLLLTrkkIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGS 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 297 EKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18555 199 EKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVIN-GELTLGELI 261
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
798-1012 |
2.39e-05 |
|
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: 47.83 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 798 VCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVQGAAGSQIG 877
Cdd:cd18549 44 IGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAHHGPE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 878 MIVNSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQT-RMLTGF-ASRDKQAlEMVGQITNeALSNIRTVAGIGK 955
Cdd:cd18549 122 DLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNkKMKKAFrRVREKIG-EINAQLED-SLSGIRVVKAFAN 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 956 ERRFIEALETELEKpFKTAIQKANIY-GFCFAFAQCIMFIANSASYRYGGYLISNEGL 1012
Cdd:cd18549 200 EEYEIEKFDEGNDR-FLESKKKAYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEI 256
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
420-646 |
2.43e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 47.39 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFhYPSRPEVKilnDLNMVIKPGEMTALVGPSGAGKSTAlqliqrfydpCEGMVTVDGHDIRSLNIQWLRDQIG 499
Cdd:PRK10418 5 IELRNIAL-QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSLT----------CAAALGILPAGVRQTAGRVLLDGKP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQE-PVLFSTTIAENIR-----------YGRE----------DATMEDIVQAAKEANA------YNFIMdlpqqfdtl 551
Cdd:PRK10418 71 VAPCAlRGRKIATIMQNPRsafnplhtmhtHAREtclalgkpadDATLTAALEAVGLENAarvlklYPFEM--------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 552 vgegggqmSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKI--QHGHTIISVAHRLSTV-RAADTIIG 628
Cdd:PRK10418 142 --------SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIvqKRALGMLLVTHDMGVVaRLADDVAV 213
|
250
....*....|....*...
gi 21536378 629 FEHGTAVERGTHEELLER 646
Cdd:PRK10418 214 MSHGRIVEQGDVETLFNA 231
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
434-500 |
2.46e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 2.46e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 434 EVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI--QRFYDPCEGMVTVDGHDIRSLNIQwLRDQIGI 500
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGI 86
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
431-617 |
3.31e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 431 SRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR-SLNIQWLRDQIGIVEQE-PVLF 508
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 509 STTIAENIRYGR---------EDATMEDIVQAAKEanaYNFIMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPKI 579
Cdd:PRK10982 87 QRSVMDNMWLGRyptkgmfvdQDKMYRDTKAIFDE---LDIDIDPRAKVATL--------SVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 21536378 580 LLLDMATSALdneSEAMVQEVLSKI----QHGHTIISVAHRL 617
Cdd:PRK10982 156 VIMDEPTSSL---TEKEVNHLFTIIrklkERGCGIVYISHKM 194
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
438-632 |
3.63e-05 |
|
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: 45.89 E-value: 3.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNI-QWLRDQIGIV-E---QEPVLFSTTI 512
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVpEdrkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 513 AENIRygredatmedivqaakeanaynfimdLP-------QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLDMA 585
Cdd:cd03215 96 AENIA--------------------------LSsllsggnQQ------------------KVVLARWLARDPRVLILDEP 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536378 586 TSALDNESEAMVQEVLSKI-QHGHTIISVAHRLSTVRA-ADTIIGFEHG 632
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELaDAGKAVLLISSELDELLGlCDRILVMYEG 180
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
752-1012 |
4.18e-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: 47.09 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 752 WPYMLVGSVGAAVNGTVTPLYAFLFSQILGTFSIPDKEEQrsqINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRL 831
Cdd:cd18540 1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDG---LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 832 RKFGFRAMLGQDIAWFDdlRNSPGALTTRLATDASQVqgaagSQI---GMI--VNSFTNVTVAMIIAFSFSWKLSLVILC 906
Cdd:cd18540 78 RKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRL-----GEIiswGLVdlVWGITYMIGILIVMLILNWKLALIVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 907 FFPFLAL-SGATQTRMLtgFASRdkQALEMVGQIT---NEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYG 982
Cdd:cd18540 151 VVPVLAVvSIYFQKKIL--KAYR--KVRKINSRITgafNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSA 226
|
250 260 270
....*....|....*....|....*....|
gi 21536378 983 FCFAFAQCIMFIANSASYRYGGYLISNEGL 1012
Cdd:cd18540 227 LFLPIVLFLGSIATALVLWYGGILVLAGAI 256
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1103-1253 |
4.53e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.64 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1103 ISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDghdsKKVNVQFLRsnigivsQEP---VlfACSIMDNIKYGdn 1179
Cdd:PRK11147 26 IEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLQ-------QDPprnV--EGTVYDFVAEG-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1180 TKEI-----------------PMERVIA--AAKQA--------QLHDFVMSLPEKYETNVGSQGSQLSRGEKQRIAIARA 1232
Cdd:PRK11147 91 IEEQaeylkryhdishlvetdPSEKNLNelAKLQEqldhhnlwQLENRINEVLAQLGLDPDAALSSLSGGWLRKAALGRA 170
|
170 180
....*....|....*....|.
gi 21536378 1233 IVRDPKILLLDEATSALDTES 1253
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIET 191
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1094-1298 |
4.98e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1094 QVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLL----ERFYDPDQGKVMIDGHDSKKVnVQFLRSNIGIVSQEPVLFA-C 1168
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFPhL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1169 SIMDNIKYGDNTKEiPMERVIAAAKQ---AQLHDFVMS---LPEKYETNVGS---QGsqLSRGEKQRIAIARAIVRDPKI 1239
Cdd:TIGR00956 154 TVGETLDFAARCKT-PQNRPDGVSREeyaKHIADVYMAtygLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1240 LLLDEATSALDTESektvqvALDKAREGRTCIVIAHRLSTI------QNA----DIIAVMAQGVVIEKG 1298
Cdd:TIGR00956 231 QCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFG 293
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1219-1305 |
6.21e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 47.31 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1219 LSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQN-ADIIAVMAQGVV-- 1294
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsg 475
|
90
....*....|....
gi 21536378 1295 ---IEKGTHEELMA 1305
Cdd:PRK10762 476 eftREQATQEKLMA 489
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1088-1305 |
7.29e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 7.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1088 PSRPDSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYdPD--QGKVMIDGhdsKKVNV----QFLRSNIGIVSQ 1161
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGrwEGEIFIDG---KPVKIrnpqQAIAQGIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1162 E-------PVLfacSIMDNIKYGDNTKEIPMERVIAAAKQAQLHDFVMSLPEKYETNVGSQGSqLSRGEKQRIAIARAIV 1234
Cdd:PRK13549 346 DrkrdgivPVM---GVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASPELAIAR-LSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1235 RDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQG-----VVIEKGTHEELMA 1305
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIyKLINQLVQQGVAIIVISSELPEVLGlSDRVLVMHEGklkgdLINHNLTQEQVME 499
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
429-615 |
7.44e-05 |
|
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: 45.86 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 429 YPSRpeVKILNDLNMVIKPG-----EMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIrSLNIQWLR-DQIGIVe 502
Cdd:cd03237 3 YPTM--KKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKaDYEGTV- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 503 qepvlfsttiaenirygreDATMEDIVQAAKEANAYNF-IMDlPQQFDTLVGEGGGQMSGGQKQRVAIARALIRNPKILL 581
Cdd:cd03237 79 -------------------RDLLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYL 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 21536378 582 LDMATSALDNESEAMVQEVLSKI--QHGHTIISVAH 615
Cdd:cd03237 139 LDEPSAYLDVEQRLMASKVIRRFaeNNEKTAFVVEH 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1208-1304 |
7.48e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 7.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1208 YETNVGSqgsqLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADI 1285
Cdd:PRK10982 385 HRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTDR 460
|
90 100
....*....|....*....|....
gi 21536378 1286 IAVMAQGVV-----IEKGTHEELM 1304
Cdd:PRK10982 461 ILVMSNGLVagivdTKTTTQNEIL 484
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1099-1292 |
7.86e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.97 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1099 LSVSISPGQTLAFVGSSGCGKStsiQLLERFY---DPDQGKVMIDGHDSKKVNVQfLRSNIGIV-----SQEPVLF---- 1166
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYldap 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1167 ----ACSIMDNIK--YGDNTKEipmerviaaakQAQLhdfvmslpEKYETNVG---SQGSQ----LSRGEKQRIAIARAI 1233
Cdd:PRK15439 358 lawnVCALTHNRRgfWIKPARE-----------NAVL--------ERYRRALNikfNHAEQaartLSGGNQQKVLIAKCL 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 1234 VRDPKILLLDEATSALDTESEKTV-QVALDKAREGRTCIVIAHRLSTI-QNADIIAVMAQG 1292
Cdd:PRK15439 419 EASPQLLIVDEPTRGVDVSARNDIyQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQG 479
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
801-1012 |
8.08e-05 |
|
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: 46.04 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 801 LFVAMGCVSLFtQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDIAWFDdlRNSPGALTTRLAtDASQVQGAAGSQIGMIV 880
Cdd:cd18566 48 VVIAILLESLL-RLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLTGQALLAL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 881 NSFTNVTVAMIIAFSFSWKLSLVILCFFPFLALSGATQTRMLTGFASRDKQALEMVGQITNEALSNIRTVAGIGKERRFI 960
Cdd:cd18566 124 LDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQML 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 21536378 961 EALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 1012
Cdd:cd18566 204 RRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDL 255
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1100-1302 |
9.33e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 46.83 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1100 SVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdsKKVNVQFLRSNI--GIV------SQEPVLFACSIM 1171
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIraGIMlcpedrKAEGIIPVHSVA 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 DNIKYGDNTKEIPMERVIAAAKQAQLHD-FVMSLpeKYETNVGSQG-SQLSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PRK11288 350 DNINISARRHHLRAGCLINNRWEAENADrFIRSL--NIKTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGI 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 1250 DTESEKTV-QVALDKAREGRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEE 1302
Cdd:PRK11288 428 DVGAKHEIyNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1064-1305 |
1.15e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 46.32 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1064 YNTAGEKWDNFQGKIDFVDCKFTypsRPDSQVLNGLSVSISPGQTLAFVGSSGCGKStsiQLLERFYDPDQ---GKVMID 1140
Cdd:PRK09700 250 FNAMKENVSNLAHETVFEVRNVT---SRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFGVDKragGEIRLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1141 GHD-SKKVNVQFLRSNIGIVSQ---EPVLFA-CSIMDNIKYGDNTK-----------EIPMERVIAAAKQAQLHDFVMSL 1204
Cdd:PRK09700 324 GKDiSPRSPLDAVKKGMAYITEsrrDNGFFPnFSIAQNMAISRSLKdggykgamglfHEVDEQRTAENQRELLALKCHSV 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1205 pekyETNVGsqgsQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDK-AREGRTCIVIAHRLSTIQNA 1283
Cdd:PRK09700 404 ----NQNIT----ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITV 475
|
250 260
....*....|....*....|....*....
gi 21536378 1284 -DIIAVMAQGVV------IEKGTHEELMA 1305
Cdd:PRK09700 476 cDRIAVFCEGRLtqiltnRDDMSEEEIMA 504
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
566-643 |
1.21e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 45.89 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 566 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 642
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHD 240
|
.
gi 21536378 643 L 643
Cdd:PRK11022 241 I 241
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
116-249 |
1.66e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging 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: 350043 [Multi-domain] Cd Length: 313 Bit Score: 45.25 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 116 NSSLNQNMTNGTRCGLLNIE--SEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCN 193
Cdd:cd18599 33 GSGNTTNNVDNSTVDSGNISdnPDLNFYQLVYGGSILVILLLSLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTT 112
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 194 SVGELNTRFSDDINKINDAIADQMALFIQRMtsticgfLLGFFrgwklTLVIISVS 249
Cdd:cd18599 113 PTGRILNRFSKDLDEVDVRLPFTLENFLQNV-------LLVVF-----SLIIIAIV 156
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
1219-1303 |
1.73e-04 |
|
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: 46.16 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1219 LSRGEKQRIAIARAIVRD---PKILLLDEATSALDTES-EKTVQVALDKAREGRTCIVIAHRLSTIQNAD-IIAV----- 1288
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDiKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADyIIDLgpegg 909
|
90
....*....|....*
gi 21536378 1289 MAQGVVIEKGTHEEL 1303
Cdd:TIGR00630 910 DGGGTVVASGTPEEV 924
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
408-479 |
1.78e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.65 E-value: 1.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 408 EDGYKLDRIKGEIEfhNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV 479
Cdd:PRK15064 310 EQDKKLHRNALEVE--NLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1217-1292 |
1.82e-04 |
|
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: 43.85 E-value: 1.82e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21536378 1217 SQLSRGEKQRIAIARAIVRDPK--ILLLDEATSALDTESEKTVQVALDKAR-EGRTCIVIAHRLSTIQNADIIAVMAQG 1292
Cdd:cd03238 86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDFGPG 164
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1215-1288 |
2.13e-04 |
|
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: 43.71 E-value: 2.13e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1215 QGSQLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKARE--GRTCIVIAHRLSTIQN-ADIIAV 1288
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHV 144
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
114-313 |
3.25e-04 |
|
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: 44.44 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 114 WTNSSLNQNmtngtrcgLLNIESEMIKFASYYAGIAVAVLITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCN 193
Cdd:cd18605 25 WVSHSNNSF--------FNFINDSFNFFLTVYGFLAGLNSLFTLLRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 194 SVGELNTRFSDDINKINDAIADQMALFIqRMTSTICGFLLGFFRGwkLTLVIISVSPLIGIGAatiglSVSKF---TDYE 270
Cdd:cd18605 97 PVGRILNRFSSDVYTIDDSLPFILNILL-AQLFGLLGYLVVICYQ--LPWLLLLLLPLAFIYY-----RIQRYyraTSRE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 21536378 271 LK---AYAKAGVVA--DEVISSMRTVAAFGGEKREVERYEKNLVFAQR 313
Cdd:cd18605 169 LKrlnSVNLSPLYThfSETLKGLVTIRAFRKQERFLKEYLEKLENNQR 216
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
114-317 |
3.41e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 44.13 E-value: 3.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 114 WTNSSLNQNMTNGTRCGLLNIESEMIKFASYYAGIAVAVLITGYIQ---ICFWVIAAARQI-QKMrkfyFRRIMRMEIGW 189
Cdd:cd18602 25 WTEANHDVASVVFNITSSSLEDDEVSYYISVYAGLSLGAVILSLVTnlaGELAGLRAARRLhDRM----LRNIVRAPMRF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 190 FDCNSVGELNTRFSDDINKIndaiaDQ-MALFIQRMTSTICgFLLGFFrgwkltLVIISVSPLIGIGAATIGLS---VSK 265
Cdd:cd18602 101 FDTTPIGRILNRFSSDTNVI-----DQkLPTTLERLLRFLL-LCLSAI------IVNAIVTPYFLIALIPIIIVyyfLQK 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 266 F---TDYELK---AYAKAGVVA--DEVISSMRTVAAFGGEKREVERYEK-----NLVF-----AQRW-GIR 317
Cdd:cd18602 169 FyraSSRELQrldNITKSPVFShfSETLGGLTTIRAFRQQARFTQQMLElidrnNTAFlflntANRWlGIR 239
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
420-488 |
3.65e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.12 E-value: 3.65e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 420 IEFHNVTFHYPSrpeVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLI------QrfydpcEGMVTVDGHDIRS 488
Cdd:NF033858 2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkiQ------QGRVEVLGGDMAD 67
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
138-369 |
3.67e-04 |
|
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: 44.01 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 138 MIKFASYYAG-IAVAVLITgyiqicFWVIAAARQIQK-----MRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKIND 211
Cdd:cd18540 41 LTGFILLYLGlILIQALSV------FLFIRLAGKIEMgvsydLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 212 AIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLIgigaatIGLSVsKFTDYELKAYAKA-----GVVAD--EV 284
Cdd:cd18540 115 IISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVL------AVVSI-YFQKKILKAYRKVrkinsRITGAfnEG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 285 ISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLdEGEYTPGTLVqIFL 364
Cdd:cd18540 188 ITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVL-AGAITIGTLV-AFI 265
|
....*
gi 21536378 365 SVIVG 369
Cdd:cd18540 266 SYATQ 270
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
437-489 |
3.68e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 43.63 E-value: 3.68e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 437 ILNDLNMVIKPGEMTALVGPSGAGKST--ALQLIQRFYDPCEGMVTVDGHDIRSL 489
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTlsATLAGREDYEVTGGTVEFKGKDLLEL 70
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
399-720 |
4.45e-04 |
|
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: 45.00 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 399 RKPIIDCMSEDGYKLDRI-----KGEI-EFHNVTFHYP--SRPEVkilNDLNMVIKPGEMTALVGPSGAGKSTALQLIQR 470
Cdd:TIGR01257 1911 KEPIFDEDDDVAEERQRIisggnKTDIlRLNELTKVYSgtSSPAV---DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTG 1987
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 471 FYDPCEGMVTVDGHDIRSlNIQWLRDQIGIVEQEPVLfsttiaENIRYGREDATMEDIVQA--AKE----ANAYNFIMDL 544
Cdd:TIGR01257 1988 DTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGREHLYLYARLRGvpAEEiekvANWSIQSLGL 2060
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 545 PQQFDTLVgeggGQMSGGQKQRVAIARALIRNPKILLLDMATSALDNESEAMV-QEVLSKIQHGHTIISVAHRLSTVRAA 623
Cdd:TIGR01257 2061 SLYADRLA----GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSMEECEAL 2136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 624 DTIIGFE-HGTAVERGTHEELLERKGVYFtLVTLQsqgnqalneedIKdATEDDML-----ARTFSRGSYQDSLRasiRQ 697
Cdd:TIGR01257 2137 CTRLAIMvKGAFQCLGTIQHLKSKFGDGY-IVTMK-----------IK-SPKDDLLpdlnpVEQFFQGNFPGSVQ---RE 2200
|
330 340
....*....|....*....|....*...
gi 21536378 698 RSKSQLSYLVHEPPLA-----VVDHKST 720
Cdd:TIGR01257 2201 RHYNMLQFQVSSSSLArifqlLISHKDS 2228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
444-618 |
4.74e-04 |
|
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: 43.51 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 444 VIKPGEMTALVGPSGAGKSTALQLIQ--------RFYDPCEGMVTVD---GHDIRSLNIQWLRDQIGI------VEQEPV 506
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpqyVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 507 LFSTTIAENIRYGREDATMEDIVQAakeanaynfiMDLpqqfDTLVGEGGGQMSGGQKQRVAIARALIRNPKILLLDMAT 586
Cdd:cd03236 102 AVKGKVGELLKKKDERGKLDELVDQ----------LEL----RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|...
gi 21536378 587 SALD-NESEAMVQEVLSKIQHGHTIISVAHRLS 618
Cdd:cd03236 168 SYLDiKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
438-633 |
5.05e-04 |
|
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: 42.31 E-value: 5.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 438 LNDLNMVIKPGEMTALVGPSGAGKSTALQliqrfydpcEGMVTVDGHDIRSLNIQWLRDQIGIVEQepvlFSTTIAENIR 517
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRNKLIFIDQ----LQFLIDVGLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 518 YgredatmedivqaakeanaynfiMDLPQQFDTLvgegggqmSGGQKQRVAIARALIRNPK--ILLLDMATSALDNESEA 595
Cdd:cd03238 78 Y-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 21536378 596 MVQEVLSK-IQHGHTIISVAHRLSTVRAADTIIGFEHGT 633
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1096-1312 |
5.99e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1096 LNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERFYDPDQGKVMIDGhdskkvNVQFLRSNIGIVSQ----EPVLFACSIM 1171
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQltgiENIEFKMLCM 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1172 dnikyGDNTKEIP--MERVIaaaKQAQLHDFVMSLPEKYetnvgsqgsqlSRGEKQRIAIARAIVRDPKILLLDEATSAL 1249
Cdd:PRK13546 114 -----GFKRKEIKamTPKII---EFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVG 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 1250 DtesEKTVQVALDKARE----GRTCIVIAHRLSTIQN-ADIIAVMAQGVVIEKGTHEELMAQKGAYYK 1312
Cdd:PRK13546 175 D---QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLN 239
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
179-360 |
7.17e-04 |
|
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: 43.22 E-value: 7.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 179 FRRIMRMEIGWFDCNSVGELNTRFsDDINKINDAIADQM-ALFIQRMTSTICGFLLgFFRGWKLTLVIISVSPL-IGIGA 256
Cdd:cd18567 82 FRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFvEALLDGLMAILTLVMM-FLYSPKLALIVLAAVALyALLRL 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 257 ATIGlSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLC 336
Cdd:cd18567 160 ALYP-PLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLE 238
|
170 180
....*....|....*....|....
gi 21536378 337 YALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18567 239 NILVIYLGALLVLD-GEFTVGMLF 261
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1218-1301 |
7.21e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1218 QLSRGEKQRIAIARAIVRDPKILLLDEATSALDTESEKTVQVALDKARegRTCIVIAHR---LSTIQnADIIAVMAQGVV 1294
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHArefLNTVV-TDILHLHGQKLV 420
|
....*..
gi 21536378 1295 IEKGTHE 1301
Cdd:PLN03073 421 TYKGDYD 427
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1184-1292 |
7.24e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1184 PMERVIAAAKQAQLHDFVMSLPekyetnVGSQGSQLSRGEKQRIAIARAIVRDPK---ILLLDEATSALDTESEKTVQVA 1260
Cdd:PRK00635 1671 PFLKKIQKPLQALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQ 1744
|
90 100 110
....*....|....*....|....*....|...
gi 21536378 1261 LDK-AREGRTCIVIAHRLSTIQNADIIAVMAQG 1292
Cdd:PRK00635 1745 LRTlVSLGHSVIYIDHDPALLKQADYLIEMGPG 1777
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
146-360 |
8.17e-04 |
|
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: 350056 [Multi-domain] Cd Length: 294 Bit Score: 42.89 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 146 AGIAVAVL---ITGYIQICFWVIAAARQIQKMRKFYFRRIMRMEIGWFDCNSVGELnTRFSDDINKINDAIADQMaLFIQ 222
Cdd:cd18783 46 IGVVIALLfegILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVL-TKHMQQIERIRQFLTGQL-FGTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 223 RMTSTICGFL-LGFFRGWKLTLVIISVSPLIgigAATIGLSVSKFTDYELKAY---AKAGVVADEVISSMRTVAAFGGEK 298
Cdd:cd18783 124 LDATSLLVFLpVLFFYSPTLALVVLAFSALI---ALIILAFLPPFRRRLQALYraeGERQAFLVETVHGIRTVKSLALEP 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21536378 299 REVERYEKNLVFAQRWGIRKGIVMGFFTGFVWCLIFLCYALAFWYGSTLVLDeGEYTPGTLV 360
Cdd:cd18783 201 RQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFA-GSLTVGALI 261
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
423-488 |
9.35e-04 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.14 E-value: 9.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21536378 423 HNVTFhypSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRS 488
Cdd:PRK13543 15 HALAF---SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR 77
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
420-479 |
1.39e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 1.39e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSRPevKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMV 479
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
418-590 |
1.71e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.61 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 418 GEI--EFHNVTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYdP--CEGMVTVDGH--DIRS--- 488
Cdd:PRK13549 256 GEVilEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDGKpvKIRNpqq 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 489 ---LNIQWL---RDQIGIVEQEPVLFSTTIAENIRY--------GREDATMEDIVQ--AAKEANAYNFIMDLP---QQfd 549
Cdd:PRK13549 335 aiaQGIAMVpedRKRDGIVPVMGVGKNITLAALDRFtggsriddAAELKTILESIQrlKVKTASPELAIARLSggnQQ-- 412
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 21536378 550 tlvgegggqmsggqkqRVAIARALIRNPKILLLDMATSALD 590
Cdd:PRK13549 413 ----------------KAVLAKCLLLNPKILILDEPTRGID 437
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
434-537 |
2.19e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 434 EVKILN-----DLNMVIKPGeMTALVGPSGAGKSTALQLIQRFYDPcEGMVTVDGHDI-RSLNIQWLRDQIGIVeqepvl 507
Cdd:COG3593 5 KIKIKNfrsikDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGP-SSSRKFDEEDFyLGDDPDLPEIEIELT------ 76
|
90 100 110
....*....|....*....|....*....|
gi 21536378 508 FSTTIAENIRYGREDATMEDIVQAAKEANA 537
Cdd:COG3593 77 FGSLLSRLLRLLLKEEDKEELEEALEELNE 106
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
425-484 |
2.22e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 2.22e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 425 VTFHYPSRPEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDP---CEGMVTVDGH 484
Cdd:PLN03140 168 LGINLAKKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPslkVSGEITYNGY 230
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1092-1285 |
2.35e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKSTSIQLLERfyDPDQG---KVMIDGH---------DSKKvnvqflrsNIGIV 1159
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGysnDLTLFGRrrgsgetiwDIKK--------HIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1160 SQEPVL---FACSIMDNIKYG--DNtkeIPMERVIAAAKQaQLHDFVMSLPEKYETNVGSQGSQLSRGEkQRIA-IARAI 1233
Cdd:PRK10938 342 SSSLHLdyrVSTSVRNVILSGffDS---IGIYQAVSDRQQ-KLAQQWLDILGIDKRTADAPFHSLSWGQ-QRLAlIVRAL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21536378 1234 VRDPKILLLDEATSALDTESEKTVQVALDK-AREGRT--------------CivIAHRLSTIQNADI 1285
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEFVPDGDI 481
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
775-1012 |
2.58e-03 |
|
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: 41.34 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 775 LFSQILgTFSIP----------DKEEQRSQINGVCLLFVAMGCVSLFTQFLQGYAFAKSGELLTKRLRKFGFRAMLGQDI 844
Cdd:cd18555 12 LLLQLL-TLLIPiltqyvidnvIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 845 AWFDdlRNSPGALTTRlATDASQVQGAAGSQ-IGMIVNSFTNVTVAmIIAFSFSWKLSLVILCFFPFLALsgatqTRMLT 923
Cdd:cd18555 91 SFFE--NRSSGDLLFR-ANSNVYIRQILSNQvISLIIDLLLLVIYL-IYMLYYSPLLTLIVLLLGLLIVL-----LLLLT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 924 GFASRDKQALEMVGQ-----ITNEALSNIRTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSA 998
Cdd:cd18555 162 RKKIKKLNQEEIVAQtkvqsYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLL 241
|
250
....*....|....
gi 21536378 999 SYRYGGYLISNEGL 1012
Cdd:cd18555 242 ILWIGAYLVINGEL 255
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
1092-1121 |
2.83e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.46 E-value: 2.83e-03
10 20 30
....*....|....*....|....*....|
gi 21536378 1092 DSQVLNGLSVSISPGQTLAFVGSSGCGKST 1121
Cdd:PRK01889 181 DGEGLDVLAAWLSGGKTVALLGSSGVGKST 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
420-468 |
2.88e-03 |
|
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: 41.84 E-value: 2.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 21536378 420 IEFHNVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLI 468
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI 368
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
453-543 |
2.98e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 40.42 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 453 LVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNiqwlRDQIGIVEQEPvlfsttiAENIRYGREDAT--MEDIVQ 530
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELH----PHYRELQAADP-------KTASEYTQPDASrwVEKLLQ 84
|
90
....*....|...
gi 21536378 531 AAKEaNAYNFIMD 543
Cdd:pfam06414 85 HAIE-NGYNIILE 96
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
873-1012 |
3.14e-03 |
|
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: 41.01 E-value: 3.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 873 GSQIGMIVNSFTnVTVAMIIAFSFSWKLSLVILCFFP-FLALSGATQTRMLTG----FASRDKQALEMVgqitnEALSNI 947
Cdd:cd18568 117 RSALTTILDLLM-VFIYLGLMFYYNLQLTLIVLAFIPlYVLLTLLSSPKLKRNsreiFQANAEQQSFLV-----EALTGI 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 948 RTVAGIGKERRFIEALETELEKPFKTAIQKANIYGFCFAFAQCIMFIANSASYRYGGYLISNEGL 1012
Cdd:cd18568 191 ATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQL 255
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
848-1050 |
3.23e-03 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) 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: 350040 [Multi-domain] Cd Length: 309 Bit Score: 41.33 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 848 DDLRNSPGALTTRLATDASQVQGAAgSQIGMIVNSFTNVTVAMIIAFSFSWKLSLV----ILCFFP---FLA-LSGATQT 919
Cdd:cd18596 108 EKSSASVGKINNLMSVDANRISEFA-AFLHLLVSAPLQIVIAIVFLYRLLGWSALVglavMVLLLPlngYLAkRYSRAQK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 920 RMLtgfASRDKQAlemvgQITNEALSNIRTVagigK----ERRFIEAL----ETELekpfkTAIQKANIYGFCFAFAQ-- 989
Cdd:cd18596 187 ELM---KARDARV-----QLVTEVLQGIRMI----KffawERKWEERIlearEEEL-----KWLRKRFLLDLLLSLLWfl 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 990 ---CIMFIAnsasyrYGGY-LISNEGLHFSYVFrviSAVVLSAT---ALGRAFSYTPSYAKAKISAAR 1050
Cdd:cd18596 250 ipiLVTVVT------FATYtLVMGQELTASVAF---TSLALFNMlrgPLNVLPELITQLLQAKVSLDR 308
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
173-385 |
3.33e-03 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). 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. 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: 349998 [Multi-domain] Cd Length: 299 Bit Score: 41.25 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 173 KMRKFYFRRIMRMEIGWFDCNSVGELNTRFSDDINKINDAIADQMALFIQRMTSTICGFLLGFFRGWKLTLVIISVSPLI 252
Cdd:cd18554 80 DIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFY 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 253 GIGAATIGLSVSKFTDYELKAYAKAGVVADEVISSMRTVAAFGGEKREVERYEK-NLVFAQRWGIRKGIVMGFFTGfVWC 331
Cdd:cd18554 160 ILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKrNGHFLTRALKHTRWNAKTFSA-VNT 238
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 21536378 332 LIFLCYALAFWYGSTLVLdEGEYTPGTLVQIF--LSVIVGAL-NLGNASPCL-EAFAT 385
Cdd:cd18554 239 ITDLAPLLVIGFAAYLVI-EGNLTVGTLVAFVgyMERMYSPLrRLVNSFTTLtQSFAS 295
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
386-583 |
3.79e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 41.54 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 386 GRAAATSIFETIDRKPIIDCM-----SEDGYKLDRIKGEI--EFHNVtfhypSRPEVkiLNDLNMVIKPGEMTALVGPSG 458
Cdd:COG1129 216 GRLVGTGPVAELTEDELVRLMvgrelEDLFPKRAAAPGEVvlEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVG 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 459 AGKSTALQLIQRFYDPCEGMVTVDGHDIRSLNIqwlRDQI--------------GIVEQEPVLFSTTIAeN--------- 515
Cdd:COG1129 289 AGRTELARALFGADPADSGEIRLDGKPVRIRSP---RDAIragiayvpedrkgeGLVLDLSIRENITLA-Sldrlsrggl 364
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21536378 516 IRYGREDATMEDIVQA--AKEANAYNFIMDLP---QQfdtlvgegggqmsggqkqRVAIARALIRNPKILLLD 583
Cdd:COG1129 365 LDRRRERALAEEYIKRlrIKTPSPEQPVGNLSggnQQ------------------KVVLAKWLATDPKVLILD 419
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
420-618 |
4.30e-03 |
|
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: 41.27 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 420 IEFHNVTFHYPSrpEVKILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGhdirslniqwlRDQIG 499
Cdd:TIGR00954 452 IKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLF 518
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 500 IVEQEPVLFSTTIAENIRY--GREDATMEDIVQAAKEAnaynfIMDLPQQFDTL--------VGEGGGQMSGGQKQRVAI 569
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIYpdSSEDMKRRGLSDKDLEQ-----ILDNVQLTHILereggwsaVQDWMDVLSGGEKQRIAM 593
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 21536378 570 ARALIRNPKILLLDMATSALDNESEAMVQEVLSKIqhGHTIISVAHRLS 618
Cdd:TIGR00954 594 ARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
567-633 |
4.63e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 4.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21536378 567 VAIARALIRNPK---ILLLDMATSALDNESEAMVQEVL-SKIQHGHTIISVAHRLSTVRAADTIIGFEHGT 633
Cdd:PRK00635 1708 IKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLrTLVSLGHSVIYIDHDPALLKQADYLIEMGPGS 1778
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1218-1300 |
6.25e-03 |
|
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: 38.88 E-value: 6.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 1218 QLSRGEKQRIAIA-----RAIVRDPkILLLDEATSALDTES-EKTVQVALDKAREGRTCIVIAHRLSTIQNADIIAVMaq 1291
Cdd:cd03227 77 QLSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI-- 153
|
....*....
gi 21536378 1292 GVVIEKGTH 1300
Cdd:cd03227 154 KKVITGVYK 162
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
566-644 |
6.40e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.17 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 566 RVAIARALIRNPKILLLDMATSALDNESEAMVQEVLSKIQHGH--TIISVAHRLSTV-RAADTIIGFEHGTAVERGTHEE 642
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLsQWADKINVLYCGQTVETAPSKE 245
|
..
gi 21536378 643 LL 644
Cdd:PRK15093 246 LV 247
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
424-487 |
7.04e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 39.55 E-value: 7.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 21536378 424 NVTFHYPSRPevkILNDLNMVIKPGEMTALVGPSGAGKSTALQLIQRFYDPCEGMVTVDGHDIR 487
Cdd:PRK13540 6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK 66
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
890-1022 |
8.71e-03 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 39.92 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21536378 890 MIIAFSFSW-KLSLVILCFFPFLALSGATQTRMLTGFAS-RDKQAL---EMVGqITNEALSNIRTVAGIGKERRF---IE 961
Cdd:cd18594 126 VIVLTGLLWrEIGPSSLAGLGVLLLLLPLQAYLGKLFAKyRRKTAGltdERVK-IMNEIISGMRVIKMYTWEESFaklIE 204
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21536378 962 AL-ETELEKPFKTA-IQKAN--IYGFCFAFAQCIMFIansasyrygGYLISNEGLHFSYVFRVIS 1022
Cdd:cd18594 205 NIrKKELKLIRKAAyIRAFNmaFFFFSPTLVSFATFV---------PYVLTGNTLTARKVFTVIS 260
|
|
| |
