|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
58-2398 |
0e+00 |
|
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: 1538.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 58 EIFIPLVLFFILLGLRQKKPTISVKEVSFYTAApLTSAGILPVMQSL-C----PDGQRDEFG-----FLQYANStvtqLL 127
Cdd:TIGR01257 28 ELVWPLSLFLVLIWLRNANPLYSQHECHFPNKA-MPSAGMLPWLQGIfCnvnnPCFQSPTPGespgiVSNYNNS----IL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 128 ERLDRVVEEGNLFDPARPSLG---SELEALRQHLEALSagpgtsgSHLDRSTVSSFSLDSVARNPQELWRFLTQNLSLPN 204
Cdd:TIGR01257 103 ARVYRDFQELLMDAPESQHLGqvwAELRTLSQFMDTLR-------THPERIAGRGIRIRDILKDEEALTLFLMKNIGLSD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 205 STAQALLAARVDPPEVYHLLfgPSSALDSqsglhkgqepwsrlggnplfrmeelllapalleqLTCTpgSGELGRILTVP 284
Cdd:TIGR01257 176 SVVYLLVNSQVRPEQFAYGV--PDLELKD----------------------------------IACS--EALLERFIIFS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 285 esQKGALQGYRDAVCSGQAAArarrFSGLSAELRNQLDVAKVSQQLgldaPNGSDSSPQAPPPRRLQALLGDLLD-AQKV 363
Cdd:TIGR01257 218 --QRRGAQTVRDALCSLSQGT----LQWIEDTLYANVDFFKLFHVL----PTLLDSRSQGINLRSWGGILSDMSPrIQEF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 364 LQDVDVLSALALLLPqgactgrtpgppasgaggaangtgagavmgpnaTAEEGAPSAaalatpdtlqgqcsaFVQLWAGL 443
Cdd:TIGR01257 288 IHRPSVQDLLWVTRP---------------------------------LLQNGGPET---------------FTQLMGIL 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 444 QPILCGnnrtiEPEAlrrGNMSSLGFTSKEQRN----LGL---------------------LVHLMTSNP---------- 488
Cdd:TIGR01257 320 SDLLCG-----YPEG---GGSRVFSFNWYEDNNykafLGIdstrkdpiysydkrttsfcnaLIQSLESNPltkiawraak 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 489 -----KILYAPAGSEVDRVILKANETFAFVGNVTHYAQVWLNISAEIRSFLEQGRLQQHLR----------WLQQYVAEL 553
Cdd:TIGR01257 392 pllmgKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRdtlqnptvkdFINRQLGEE 471
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 554 RLHPEALNLSLDELPPALRQD---NFSLPSGMALLQQLDTIDNaacgwiQFMSKVSVDIFKGFPDEESIVNYTLNQAYQD 630
Cdd:TIGR01257 472 GITAEAVLNFLYNGPREKQADdmtNFDWRDIFNITDRFLRLAN------QYLECLVLDKFESYDDEVQLTQRALSLLEEN 545
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 631 NVtvFASVIFQTRK--DGSLPPHVHYKIRQNSSFTEKTNEIRRAYWRPGPNTGGRFYFLY---GFVWIQDMMERAIIDTF 705
Cdd:TIGR01257 546 RF--WAGVVFPDMYpwTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYiwgGFAYLQDMVEQGITRSQ 623
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 706 VGHDVvEPGSYVQMFPYPCYTRDDFLFVIEHMMPLCMVISWVYSVAMTIQHIVAEKEHRLKEVMKTMGLNNAVHWVAWFI 785
Cdd:TIGR01257 624 MQAEP-PVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFL 702
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 786 TGFVQLSISVTALTAILKYGQVLMHSHVVIIWLFLAVYAVATIMFCFLVSVLYSKAKLASACGGIIYFLSYVPYMYVAIR 865
Cdd:TIGR01257 703 DSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAW 782
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 866 EevahDKITAFEKCIASLMSTTAFGLGSKYFALYEVAGVGIQWHTFSQSPVEGDDFNLLLAVTMLMVDAVVYGILTWYIE 945
Cdd:TIGR01257 783 Q----DRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLD 858
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 946 AVHPGMYGLPRPWYFPLQKSYWLG----SGRTEawewswpwartprlSVMEEDQACAMESRRFEETRGMEE---EPTHLP 1018
Cdd:TIGR01257 859 QVFPGDYGTPLPWYFLLQESYWLGgegcSTREE--------------RALEKTEPLTEEMEDPEHPEGINDsffERELPG 924
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1019 LV--VCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKN 1096
Cdd:TIGR01257 925 LVpgVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS 1004
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1097 LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAII 1176
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1177 LDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGTYGDGYRLTLVKR-- 1254
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRKmk 1164
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1255 --PAEPGGPQ------EPGLASSPPGRAPLSSCSEL------QVSQFIRKHVASCLLVSDTSTELSYILPSEAAKKGAFE 1320
Cdd:TIGR01257 1165 niQSQRGGCEgtcsctSKGFSTRCPARVDEITPEQVldgdvnELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYA 1244
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1321 RLFQHLERSLDALHLSSFGLMDTTLEEVFLKVSEEDQSLENSEADVKESRKDVlpGAEGPASGEghagnlarcseltqsq 1400
Cdd:TIGR01257 1245 SLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKRENA--NLRHPCSGP---------------- 1306
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1401 aslqsassvgsargDEGAGYTdvygdyrplfdnPQDPDNVSLQEVEAE-----ALSRVGQGSRKLDGGWLKVRQFHGLLV 1475
Cdd:TIGR01257 1307 --------------TEKAGQT------------PQASHTCSPGQPAAHpegqpPPEPEDPGVPLNTGARLILQHVQALLV 1360
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1476 KRFHCARRNSKALFSQILLPAFFVCVAMTVALSVPEIGDLPPLVLSPSQY-HNYTqprgnfipyaneerreyrlRLSPDA 1554
Cdd:TIGR01257 1361 KRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYgQQYT-------------------FFSMDE 1421
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1555 SPQQLVSTFrlpsgvgATCVLKSPAngslgptlnlssgesrllaarfFDSMCL-ESFTQGLPLSNfvppppspapsdspa 1633
Cdd:TIGR01257 1422 PNSEHLEVL-------ADVLLNKPG----------------------FGNRCLkEEWLPEYPCGN--------------- 1457
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1634 spdedLQAWNVslpPTAGPEM--------WTSAPSLPRlvrepVRCTCSAQGTGF-SCPSSVGGHPPQMRVV-TGDILTD 1703
Cdd:TIGR01257 1458 -----STPWKT---PSVSPNIthlfqkqkWTAAHPSPS-----CRCSTREKLTMLpECPEGAGGLPPPQRTQrSTEILQD 1524
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1704 ITGHNVSEYLLFT---------SDRFRLH--RYGAITFGNVLKSIPAS--------------FGTRAPPMVRKIAVRRAA 1758
Cdd:TIGR01257 1525 LTDRNISDFLVKTypalirsslKSKFWVNeqRYGGISIGGKLPAIPITgealvgflsdlgqmMNVSGGPVTREASKEMPD 1604
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1759 -----------QVFYNNKGYHSMPTYLNSLNNAILRANLPKSKgNPAAYGITVTNHPMNKTSASLS-LDYLLQGTDVVIA 1826
Cdd:TIGR01257 1605 flkhletedniKVWFNNKGWHALVSFLNVAHNAILRASLPKDR-DPEEYGITVISQPLNLTKEQLSeITVLTTSVDAVVA 1683
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1827 IFIIVAMSFVPASFVVFLVAEKSTKAKHLQFVSGCNPIIYWLANYVWDMLNYLVPATCCVIILFVFDLPAYTSPTNFPAV 1906
Cdd:TIGR01257 1684 ICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPAL 1763
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1907 LSLFLLYGWSITPIMYPASFWFEVPSSAYVFLIVINLFIGITATVATFLLQLFEHDKDLKVVNSYLKSCFLIFPNYNLGH 1986
Cdd:TIGR01257 1764 VALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELFENNRTLLRFNAMLRKLLIVFPHFCLGR 1843
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1987 GLMEMAYNEYINEYYAKIGQfDKMKSPFEWDIVTRGLVAMAVEGVVGFLLTIMCQYNF-----LRRPQRMPVstkpVEDD 2061
Cdd:TIGR01257 1844 GLIDLALSQAVTDVYAQFGE-EHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQHHFflsrwIAEPAKEPI----FDED 1918
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2062 VDVASERQRVLRGDADNDMVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2141
Cdd:TIGR01257 1919 DDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP---AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGD 1995
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2142 AFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGN 2221
Cdd:TIGR01257 1996 ATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGN 2075
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2301
Cdd:TIGR01257 2076 KRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2302 HLKNRFGDGYMITVRTKSSQ-----SVKDVVRFFNRNFPEAMLKERHHTKVQYQLKSEhiSLAQVFSKMEQVSGVLGIED 2376
Cdd:TIGR01257 2156 HLKSKFGDGYIVTMKIKSPKddllpDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSS--SLARIFQLLISHKDSLLIEE 2233
|
2490 2500
....*....|....*....|..
gi 47078218 2377 YSVSQTTLDNVFVNFAKKQSDN 2398
Cdd:TIGR01257 2234 YSVTQTTLDQVFVNFAKQQTET 2255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2081-2304 |
5.52e-117 |
|
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: 369.53 E-value: 5.52e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2160
Cdd:cd03263 1 LQIRNLTKTYKK---GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDlIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2304
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1021-1240 |
1.52e-113 |
|
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: 359.51 E-value: 1.52e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1021 VCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC 1100
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1181 TAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLK 1240
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1023-1236 |
5.11e-85 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 278.49 E-value: 5.11e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1102
Cdd:COG1131 3 VRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1183 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:COG1131 161 GLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2081-2307 |
7.88e-84 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 275.02 E-value: 7.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2160
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRF 2307
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
2088-2391 |
5.85e-68 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 232.28 E-value: 5.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2088 KVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCD 2167
Cdd:TIGR01188 1 KVY-----GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2168 ALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2247
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2248 DPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYmITVRTKSSQSVKDVV 2327
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEV 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2328 RFFNRNFPEAMLkERHHTKVQYQLKSEHISLAQvfskmEQVSGVLG--------IEDYSVSQTTLDNVFVNF 2391
Cdd:TIGR01188 235 SMLIAELGETGL-GLLAVTVDSDRIKILVPDGD-----ETVPEIVEaairngirIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2081-2304 |
3.18e-67 |
|
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: 226.87 E-value: 3.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2160
Cdd:cd03265 1 IEVENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2304
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1023-1231 |
2.58e-66 |
|
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: 225.12 E-value: 2.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1102
Cdd:COG4555 4 VENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1183 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLK 1231
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1028-1352 |
5.52e-66 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 226.50 E-value: 5.52e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1028 KVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLF 1107
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1187
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1188 ARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGTYGDGyrlTLVKRPAEPggpqepgl 1266
Cdd:TIGR01188 159 TRRAIWDYIRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKD---TLESRPRDI-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1267 ASSPPGRAPLSscSELQVSQFIRKhvasCLLVSDTSTELSYILPSEAAKKgAFERLfqhlerSLDALHLSSFGLMDTTLE 1346
Cdd:TIGR01188 228 QSLKVEVSMLI--AELGETGLGLL----AVTVDSDRIKILVPDGDETVPE-IVEAA------IRNGIRIRSISTERPSLD 294
|
....*.
gi 47078218 1347 EVFLKV 1352
Cdd:TIGR01188 295 DVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1023-1240 |
8.92e-66 |
|
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: 222.63 E-value: 8.92e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDkkLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1102
Cdd:cd03265 3 VENLVKKYGDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1183 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLK 1240
Cdd:cd03265 161 GLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1023-1230 |
1.37e-65 |
|
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: 219.96 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1102
Cdd:cd03230 3 VRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLwfysrlksmaqeeirremdkmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 47078218 1183 GVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03230 125 GLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2081-2294 |
3.26e-63 |
|
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: 213.41 E-value: 3.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2160
Cdd:cd03230 1 IEVRNLSKRYGKKT-----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQlytrlrgiswkdearvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2080-2309 |
8.94e-61 |
|
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: 209.33 E-value: 8.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2159
Cdd:COG4555 1 MIEVENLSKKYGKVP-----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2239
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2240 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGD 2309
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1023-1234 |
1.78e-54 |
|
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: 189.71 E-value: 1.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKddKKLALNKLSLNLyENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1102
Cdd:cd03264 3 LENLTKRYG--KKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1183 GVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1234
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2080-2397 |
2.19e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 184.16 E-value: 2.19e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKEllqVQQS 2159
Cdd:COG4152 1 MLELKGLTKRFGDKT-----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGISWKD-EARVVKWaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2238
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEaKRRADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2239 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGdGYMITVRTK 2318
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEAD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2319 SSQSvkdvvrfFNRNFPEAMLKERHHTKVQYQLKSEHiSLAQVFSkmeQVSGVLGIEDYSVSQTTLDNVFVNFAKKQSD 2397
Cdd:COG4152 231 GDAG-------WLRALPGVTVVEEDGDGAELKLEDGA-DAQELLR---ALLARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1023-1356 |
2.70e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 184.16 E-value: 2.70e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemDEIRKNLGMCPQ 1102
Cdd:COG4152 4 LKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1183 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGTYGdGYRLTLVKRPAEPGGP 1261
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEADGDAGWLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1262 QEPGLASsppgraplsscselqvsqfirkhvascllVSDTSTELSYILPSEAAKkgafERLFQHLersLDALHLSSFGLM 1341
Cdd:COG4152 238 ALPGVTV-----------------------------VEEDGDGAELKLEDGADA----QELLRAL---LARGPVREFEEV 281
|
330
....*....|....*
gi 47078218 1342 DTTLEEVFLKVSEED 1356
Cdd:COG4152 282 RPSLNEIFIEVVGEK 296
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2080-2298 |
5.53e-51 |
|
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: 180.26 E-value: 5.53e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2159
Cdd:cd03266 1 MITADALTKRFRDVK-KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2239
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2240 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2298
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2081-2295 |
5.72e-49 |
|
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: 173.94 E-value: 5.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQsL 2160
Cdd:cd03268 1 LKTNDLTKTYGKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDearvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2295
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1023-1229 |
1.49e-48 |
|
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: 173.04 E-value: 1.49e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGMCP 1101
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1181 TAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1023-1236 |
6.34e-48 |
|
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: 171.75 E-value: 6.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCP 1101
Cdd:COG1122 3 LENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QH--NVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:COG1122 82 QNpdDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1180 PTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2081-2295 |
1.00e-47 |
|
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: 170.45 E-value: 1.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKigrilAVDRLCLGVRPGeCFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2160
Cdd:cd03264 1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2241 DEPTTGMDPKAR-RFLwNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2295
Cdd:cd03264 155 DEPTAGLDPEERiRFR-NLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2081-2298 |
1.01e-46 |
|
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: 167.46 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKEllqVQQSL 2160
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2298
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2081-2293 |
5.10e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 169.22 E-value: 5.10e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2160
Cdd:PRK13537 8 IDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1026-1230 |
5.14e-46 |
|
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: 165.47 E-value: 5.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNV 1105
Cdd:cd03268 6 LTKTYG--KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTVEEHLWFYSRLKSMAQEEIrremDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1186 PYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03268 159 PDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1023-1230 |
7.79e-46 |
|
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: 165.23 E-value: 7.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKK--LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC 1100
Cdd:cd03266 4 ADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1181 TAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2080-2274 |
5.77e-45 |
|
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: 162.26 E-value: 5.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2159
Cdd:COG4133 2 MLEAENLSCRRGERLL-----FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEArvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2239
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 47078218 2240 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2274
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1023-1229 |
1.76e-44 |
|
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: 161.29 E-value: 1.76e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemDEIRKNLGMCPQ 1102
Cdd:cd03269 3 VENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47078218 1183 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2080-2293 |
5.51e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 161.54 E-value: 5.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIE--NLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQ 2157
Cdd:PRK13536 39 TVAIDlaGVSKSYGDKAV-----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2237
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2238 IFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1038-1182 |
2.47e-42 |
|
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: 152.80 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-RKNLGMCPQHNVLFDRLTVEEHL 1116
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1117 WFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1020-1236 |
5.04e-42 |
|
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: 155.14 E-value: 5.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRK 1095
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1096 NLGMCPQHNVLFDRLTVEEHLWFYSR-LKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA 1174
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR--VALA-----RA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1175 IIL-------DEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:COG1127 156 LALdpeillyDEPTAGLDPITSAVIDELIreLRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1023-1236 |
5.89e-42 |
|
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: 154.97 E-value: 5.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLG 1098
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1099 MCPQHNVLFDRLTVEEHLWFYSRLKS-MAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRAIIL 1177
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKR--VALA-----RALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1178 -------DEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:cd03261 154 dpelllyDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1023-1230 |
2.65e-40 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 149.21 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1102
Cdd:cd03259 3 LKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1183 GVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1023-1226 |
1.04e-39 |
|
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: 147.62 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVY--KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdirTEMDEIRKNLGMC 1100
Cdd:cd03293 3 VRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47078218 1181 TAGVDPYARRAIWDLILK--YKPGRTILLSTHHMDEADLLGDRIAIIS 1226
Cdd:cd03293 159 FSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1023-1236 |
1.65e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 150.34 E-value: 1.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1102
Cdd:PRK13537 10 FRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1183 GVDPYARRAIWD-LILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13537 168 GLDPQARHLMWErLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2081-2299 |
3.53e-39 |
|
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: 146.92 E-value: 3.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELL--QVQQ 2158
Cdd:cd03218 1 LRAENLSKRYGKRKV-----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2159 SLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2238
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2239 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1026-1236 |
1.01e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 149.21 E-value: 1.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNV 1105
Cdd:PRK13536 47 VSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1186 PYARRAIWD----LILKykpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13536 205 PHARHLIWErlrsLLAR---GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1023-1236 |
2.55e-38 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 144.34 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDE-IRKNLGMC 1100
Cdd:TIGR04406 4 AENLIKSYK--KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlPMHErARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLW-FYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1180 PTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1023-1222 |
3.50e-38 |
|
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: 143.00 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1102
Cdd:COG4133 5 AENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRRemDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREAI--DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 47078218 1183 GVDPYARRAIWDLILKYKP-GRTILLSTHhmDEADLLGDRI 1222
Cdd:COG4133 161 ALDAAGVALLAELIAAHLArGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2082-2305 |
8.18e-38 |
|
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: 142.96 E-value: 8.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQQS 2159
Cdd:cd03219 2 EVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHL----QLYTRLRGISW---KDEARVVKWA---LEKLELTKYADKPAGTYSGGNKRKLSTAI 2229
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVmvaaQARTGSGLLLArarREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2230 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2305
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1037-1236 |
9.01e-38 |
|
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: 142.96 E-value: 9.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1114
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHEIaRLGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 ------------HLWFYSRLKSMAqeEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03219 95 nvmvaaqartgsGLLLARARREER--EARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1183 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:cd03219 173 GLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1758-2038 |
1.60e-37 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 145.61 E-value: 1.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1758 AQVFYNNKGYHSMPTYLNSLNNaILRANLPKSKGNPAAYGITVTNHPMNKTSASLSLDYLLQgtdVVIAIFIIVAMSFVP 1837
Cdd:pfam12698 101 VTVYINSSNLLVSKLILNALQS-LLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAY---YLVGLILMIIILIGA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1838 ASFVVFLVAEKSTKAKHLQFVSGCNPIIYWLANYVWDMLNYLVPATCCVIILFVFDLPaytsPTNFPAVLSLFLLYGWSI 1917
Cdd:pfam12698 177 AIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIP----FGNLGLLLLLFLLYGLAY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1918 TPIMYPASFWFEVPSSAYVFLIVINLFIGItATVATFLLQLFehdkdlkvvNSYLKSCFLIFPNYNLGHGLMEMAYNEYI 1997
Cdd:pfam12698 253 IALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDP---------PSFLQWIFSIIPFFSPIDGLLRLIYGDSL 322
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 47078218 1998 NEyyakigqfdkmkspfewdiVTRGLVAMAVEGVVGFLLTI 2038
Cdd:pfam12698 323 WE-------------------IAPSLIILLLFAVVLLLLAL 344
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1022-1229 |
2.22e-37 |
|
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: 138.92 E-value: 2.22e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1022 CVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGMC 1100
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQhnvlfdrltveehlwfysrlksmaqeeirremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1181 TAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:cd00267 108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1023-1236 |
2.37e-37 |
|
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: 141.53 E-value: 2.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEiRKNLGMC- 1100
Cdd:cd03218 3 AENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK-RARLGIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 -PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:cd03218 80 lPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1180 PTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIkiLKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1015-1228 |
5.27e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.38 E-value: 5.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1015 THLPLVVCVDKLTKVY--KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemdE 1092
Cdd:COG1116 2 SAAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1093 IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1172
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1173 RAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1228
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1023-1230 |
7.74e-37 |
|
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: 139.55 E-value: 7.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYK--DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIR-K 1095
Cdd:cd03255 3 LKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFRrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1096 NLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1175
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 1176 ILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1230
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2080-2387 |
1.85e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 141.76 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYK----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAF 2143
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2144 VNGHSVLK---ELL--------QVQQslgycpqcdaLFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADK 2212
Cdd:COG4586 81 VLGYVPFKrrkEFArrigvvfgQRSQ----------LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2213 PAgtysggnkRKLS--------TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALC 2283
Cdd:COG4586 151 PV--------RQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2284 TRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQSVKDVVRFfnrnfpeAMLKERHHTKVQYQLKSEhISLAQVFS 2363
Cdd:COG4586 223 DRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRG-------GEVIEREGNRVRLEVDPR-ESLAEVLA 294
|
330 340
....*....|....*....|....
gi 47078218 2364 KmeqVSGVLGIEDYSVSQTTLDNV 2387
Cdd:COG4586 295 R---LLARYPVRDLTIEEPPIEEV 315
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1024-1236 |
3.47e-36 |
|
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: 138.59 E-value: 3.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1024 DKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMD--EIRKNLGMCP 1101
Cdd:cd03295 4 ENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-EQDpvELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIE--DLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1180 PTAGVDPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2081-2294 |
3.64e-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: 137.27 E-value: 3.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQvQQSL 2160
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQReLGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2081-2299 |
5.22e-36 |
|
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: 137.46 E-value: 5.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQQS 2159
Cdd:COG1122 1 IELENLSFSYP----GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQcDA---LFDElTAREHLQLYTRLRGISwKDEAR-VVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:COG1122 77 VGLVFQ-NPddqLFAP-TVEEDVAFGPENLGLP-REEIReRVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2236 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1037-1236 |
6.27e-36 |
|
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: 138.25 E-value: 6.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKnLGMCP--QHNVLFDRLTVE 1113
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItGLPPHRIAR-LGIARtfQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1114 EHL-----------WFYS--RLKSMAQEE--IRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:COG0411 98 ENVlvaaharlgrgLLAAllRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1179 EPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1037-1229 |
8.68e-36 |
|
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: 136.41 E-value: 8.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1114
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHERaRAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLWFYSRLKsmAQEEIRREMDKMIEDL-ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1193
Cdd:cd03224 95 NLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 47078218 1194 DLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:cd03224 173 EAIRELRDeGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1023-1236 |
1.28e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 136.70 E-value: 1.28e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTE--MDE-IRKNLGM 1099
Cdd:COG1137 6 AENLVKSYG--KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THlpMHKrARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1180 PTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMDEAdlLG--DRIAIISHGKLKCCGSP 1236
Cdd:COG1137 163 PFAGVDPIAVADIQKIIrhLKER-GIGVLITDHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1021-1229 |
1.64e-35 |
|
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: 134.05 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1021 VCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGM 1099
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQHNVLFDRlTVEEHLwfysrlksmaqeeirremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1180 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGK 1229
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2082-2293 |
1.85e-35 |
|
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: 135.29 E-value: 1.85e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQQSL 2160
Cdd:cd03225 1 ELKNLSFSYPDGAR---PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLsLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQ-------CDALFDELT-AREHLqlytrlrGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2232
Cdd:cd03225 78 GLVFQnpddqffGPTVEEEVAfGLENL-------GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2233 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2080-2294 |
3.37e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 135.54 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKelLQV--- 2156
Cdd:COG1137 3 TLEAENLVKSYGKRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH--LPMhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 -QQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:COG1137 76 aRLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2236 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1023-1236 |
3.60e-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: 135.94 E-value: 3.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMD--EIRKNLGMC 1100
Cdd:COG1120 4 AENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSrrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEE--------HLWFYSRLKsmaqEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1172
Cdd:COG1120 81 PQEPPAPFGLTVRElvalgrypHLGLFGRPS----AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1173 RAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2076-2302 |
1.54e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2076 ADNDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ 2155
Cdd:COG1121 2 MMMPAIELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VqqslGYCPQcDALFDE---LTAREHLQLYtRLRGISW------KDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLS 2226
Cdd:COG1121 77 I----GYVPQ-RAEVDWdfpITVRDVVLMG-RYGRRGLfrrpsrADREAVDE-ALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2227 TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLaIMVNGRLRCLGSIQH 2302
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1010-1236 |
1.78e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1010 MEEEPthlplVVCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE 1089
Cdd:COG1121 1 MMMMP-----AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1090 mdeiRKNLGMCPQHnVLFDR---LTVEE--------HLWFYSRLKSmaqeEIRREMDKMIEDLELSNKRHSLVQTLSGGM 1158
Cdd:COG1121 74 ----RRRIGYVPQR-AEVDWdfpITVRDvvlmgrygRRGLFRRPSR----ADREAVDEALERVGLEDLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1159 KRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLkCCGSP 1236
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPP 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1020-1236 |
2.04e-34 |
|
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: 140.81 E-value: 2.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVY---KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE 1092
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1093 IRKNLGMCPQH--NVLFDRLTVEEHLWF-YSRLKSMAQEEIRREMDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAF 1168
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1169 VGGSRAIILDEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1023-1230 |
2.37e-34 |
|
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: 132.63 E-value: 2.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKN 1096
Cdd:cd03257 4 VKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1097 LGMCPQH--NVLFDRLTVEEHLW--FYSRLKSMAQEEIRREMDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIAFVGG 1171
Cdd:cd03257 84 IQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1172 SRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1053-1236 |
2.82e-34 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 144.11 E-value: 2.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1053 FLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRR 1132
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1133 EMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTH 1210
Cdd:NF033858 377 RVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLieLSREDGVTIFISTH 456
|
170 180
....*....|....*....|....*.
gi 47078218 1211 HMDEAdLLGDRIAIISHGKLKCCGSP 1236
Cdd:NF033858 457 FMNEA-ERCDRISLMHAGRVLASDTP 481
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1026-1231 |
4.49e-34 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 131.75 E-value: 4.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHD-IRTEMdeirKNLGMCPQHN 1104
Cdd:TIGR03740 6 LSKRFG--KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKDL----HKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1105 VLFDRLTVEEHLWFYSRLKSMAQEEIrremDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1184
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47078218 1185 DPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1231
Cdd:TIGR03740 156 DPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2082-2293 |
6.61e-34 |
|
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: 128.90 E-value: 6.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSL 2160
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLT-----LKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCdalfdeltarehlqlytrlrgiswkdearvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd00267 76 GYVPQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1237 |
1.13e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCP 1101
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QH-NVLFDRLTVEEHLWFysrlkSMAQEEI-RREMDKMIEDL------ELSNKRHSlvQTLSGGMKRKlsVAIAFVGG-- 1171
Cdd:PRK13632 90 QNpDNQFIGATVEDDIAF-----GLENKKVpPKKMKDIIDDLakkvgmEDYLDKEP--QNLSGGQKQR--VAIASVLAln 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1172 SRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPL 1237
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1020-1271 |
1.21e-33 |
|
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: 138.11 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT---SGSATIYGHDIRTEMDEIR-K 1095
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1096 NLGMCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1174
Cdd:COG1123 84 RIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1175 IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLkgtYGDGYRLTLV 1252
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI---LAAPQALAAV 240
|
250
....*....|....*....
gi 47078218 1253 KRPAEPGGPQEPGLASSPP 1271
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEP 259
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1023-1230 |
1.72e-33 |
|
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: 130.39 E-value: 1.72e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKN 1096
Cdd:cd03258 4 LKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1097 LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAII 1176
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1177 LDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2082-2305 |
2.69e-33 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 130.09 E-value: 2.69e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLG 2161
Cdd:TIGR04406 3 VAENLIKSYKKRKV-----VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2162 --YCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWAL-EKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2238
Cdd:TIGR04406 78 igYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALlEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2239 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2305
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1018-1230 |
3.76e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 129.01 E-value: 3.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1018 PLVVCVDkLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMD 1091
Cdd:COG1136 3 PLLELRN-LTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1092 EIR-KNLGMCPQ-HNvLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFV 1169
Cdd:COG1136 82 RLRrRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1170 GGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1230
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1023-1229 |
4.75e-33 |
|
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: 127.30 E-value: 4.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI---RKNLGM 1099
Cdd:cd03229 3 LKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQHNVLFDRLTVEEHLWFysrlksmaqeeirremdkmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1180 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1020-1230 |
5.89e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 5.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVYKDDKKlALNKLSLNLYENQVVsFL-GHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIR 1094
Cdd:COG2884 1 MIRFENVSKRYPGGRE-ALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1095 KNLGMCPQ-HNVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGG-MKRklsVAIAfvggs 1172
Cdd:COG2884 79 RRIGVVFQdFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGeQQR---VAIA----- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1173 RAI-------ILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:COG2884 150 RALvnrpellLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2080-2294 |
1.50e-31 |
|
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: 125.54 E-value: 1.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKelLQVQQ- 2158
Cdd:COG0411 4 LLEVRGLTKRF-----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2159 -SLG----YcpQCDALFDELTAREHLQL-------YTRLRGI-----SWKDEARVVKWA---LEKLELTKYADKPAGTYS 2218
Cdd:COG0411 77 aRLGiartF--QNPRLFPELTVLENVLVaaharlgRGLLAALlrlprARREEREARERAeelLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2219 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2082-2294 |
1.56e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 1.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSL 2160
Cdd:COG4619 2 ELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDElTAREHLQLYTRLRGISWkDEARVVKWaLEKLELTK-YADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2239
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKF-DRERALEL-LERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2240 LDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1011-1249 |
1.68e-31 |
|
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: 132.58 E-value: 1.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1011 EEEPTHLPLVVCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-E 1089
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1090 MDEIRKNLGMCPQHNVLFDRlTVEEHLwfysRL-KSMAQEEirrEMDKMIEDLELsnkrHSLVQ---------------T 1153
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDT-TLRENL----RLaRPDATDE---ELWAALERVGL----GDWLAalpdgldtwlgeggrR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1154 LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCC 1233
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQ 550
|
250
....*....|....*.
gi 47078218 1234 GSPLFLKGTYGDGYRL 1249
Cdd:COG4987 551 GTHEELLAQNGRYRQL 566
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1023-1228 |
2.60e-31 |
|
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: 123.41 E-value: 2.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEmdeiRKNLGMCPQ 1102
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 H-NVLFD-RLTVEE--------HLWFYSRLKsmaqEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1172
Cdd:cd03235 76 RrSIDRDfPISVRDvvlmglygHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1173 RAIILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIA-----IISHG 1228
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLllnrtVVASG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1037-1230 |
2.79e-31 |
|
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: 123.98 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLG-MCPQHNVLFDRLTVEEH 1115
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGvVFGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1116 LWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1195
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|....*..
gi 47078218 1196 ILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03267 196 LKEYnrERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2044-2303 |
3.05e-31 |
|
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: 131.18 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2044 FLRRPQRM---PVSTKPVEDDVDVASERQRVLRgdadndmvkIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVN 2120
Cdd:COG1123 230 ILAAPQALaavPRLGAARGRAAPAAAAAEPLLE---------VRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGES 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2121 GAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQVQQSLGYCPQcD---ALFDELTAREHLQLYTRLRGISWKDE 2193
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRELRRRVQMVFQ-DpysSLNPRMTVGDIIAEPLRLHGLLSRAE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2194 AR-VVKWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVV 2270
Cdd:COG1123 380 RReRVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYL 459
|
250 260 270
....*....|....*....|....*....|...
gi 47078218 2271 LTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2303
Cdd:COG1123 460 FISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2082-2298 |
5.72e-31 |
|
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: 122.26 E-value: 5.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKELLQVQQSLG 2161
Cdd:cd03235 1 EVEDLTVSYGGHPV-----LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2162 YCPQ-CDALFD-ELTARE--HLQLYTRLRGISW--KDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:cd03235 72 YVPQrRSIDRDfPISVRDvvLMGLYGHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2236 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRlAIMVNGRLRCLG 2298
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1023-1229 |
6.17e-31 |
|
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: 123.45 E-value: 6.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIRKNLG 1098
Cdd:cd03256 3 VENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1099 MCPQHNVLFDRLTVEEH-----LWFYSRLKSMAQ----EEIRREMdKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFV 1169
Cdd:cd03256 82 MIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGlfpkEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1170 GGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1030-1230 |
7.22e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.85 E-value: 7.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKNLGMCPQHNVLF 1107
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPppEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DRlTVEEHL--WFYSRLKSMAQEEIRREMDKMIEDLELSNKRhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:COG4619 87 GG-TVRDNLpfPFQLRERKFDRERALELLERLGLPPDILDKP---VERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47078218 1186 PYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:COG4619 163 PENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2080-2299 |
8.32e-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: 8.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKELLQ 2155
Cdd:COG1120 1 MLEAENLSVGYGGRPV-----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VqqsLGYCPQ-CDALFDeLTARE--------HLQLYTRLRgiswKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLS 2226
Cdd:COG1120 76 R---IAYVPQePPAPFG-LTVRElvalgrypHLGLFGRPS----AEDREAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2227 TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1023-1236 |
9.50e-31 |
|
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: 122.35 E-value: 9.50e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1102
Cdd:cd03300 3 LENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1183 GVDPYARRaiwDLILKYKP-----GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:cd03300 160 ALDLKLRK---DMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1023-1304 |
1.04e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 125.20 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKK-------------------LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG 1083
Cdd:COG4586 4 VENLSKTYRVYEKepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1084 HDIRTEMDEIRKNLGmcpqhnVLF--------DrLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLS 1155
Cdd:COG4586 84 YVPFKRRKEFARRIG------VVFgqrsqlwwD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1156 GGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCC 1233
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1234 GSPLFLKGTYGDGYRLTLV-KRPAEPGGPQEPG-LASSPPGRAPLSSCSELQVSQFIRKhVASCLLVSDTSTE 1304
Cdd:COG4586 237 GSLEELKERFGPYKTIVLElAEPVPPLELPRGGeVIEREGNRVRLEVDPRESLAEVLAR-LLARYPVRDLTIE 308
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2081-2294 |
1.04e-30 |
|
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: 121.83 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELLQV 2156
Cdd:cd03255 1 IELKNLSKTYGGGGE-KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 -QQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2236 AFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEEcEALCTRLAIMVNGRL 2294
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2076-2305 |
1.41e-30 |
|
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: 122.40 E-value: 1.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2076 ADNDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----K 2151
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVV-----LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2152 ELLQVQQSLGYCPQCDALFDELTAREHLQL----YTRLRgiswKDEAR-VVKWALEKLELTKYADKPAGTYSGGNKRKLS 2226
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFDSLTVFENVAFplreHTDLS----EAEIReLVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2227 TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2305
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1033-1234 |
1.43e-30 |
|
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: 120.23 E-value: 1.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1033 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTeMD--EIRKNLGMCPQhnvlfdrl 1110
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-LSpkELARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 tveehlwfysrlksmaqeeirremdkMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1190
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1191 AIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1234
Cdd:cd03214 135 ELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2080-2303 |
2.08e-30 |
|
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: 121.53 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQ 2155
Cdd:cd03258 1 MIELKNVSKVFGDTG-GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKD-EARVvkwaLEKLELTKYADKpAGTY----SGGNKRKLSTAIA 2230
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEiEERV----LELLELVGLEDK-ADAYpaqlSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2231 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2303
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
2101-2245 |
3.24e-30 |
|
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: 118.13 E-value: 3.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2101 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDELTAREHL 2179
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2180 QLYTRLRGISWKDEARVVKWALEKLELTKYADKPAG----TYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2245
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1023-1236 |
3.62e-30 |
|
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: 120.90 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKklaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1102
Cdd:cd03299 3 VENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1183 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:cd03299 159 ALDVRTKEKLREELkkIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2081-2305 |
1.25e-29 |
|
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: 119.14 E-value: 1.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQV 2156
Cdd:cd03261 1 IELRGLTKSFGGRTV-----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 QQSLGYCPQCDALFDELTAREHLQL----YTRLrgiswkDEARVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAI 2229
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFplreHTRL------SEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2230 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2305
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2082-2305 |
1.31e-29 |
|
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: 118.69 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ--VQQS 2159
Cdd:cd03224 2 EVENLNAGY-----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGIswkdeaRVVKWALEKL-----ELTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRR------AKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2305
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1031-1236 |
2.28e-29 |
|
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: 119.67 E-value: 2.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1031 KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIR-KNLGMCPQHNV 1105
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRrKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1186 PYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
999-1236 |
3.12e-29 |
|
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: 125.64 E-value: 3.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 999 MESRRFEETRGMEEEPTHLPLVVCVDKLTKVYkDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGS 1078
Cdd:COG4988 315 LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1079 ATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDrLTVEEHLWFYSRLKSmaQEEIRR-----EMDKMIEDLElsNKRHSLV- 1151
Cdd:COG4988 394 ILINGVDLSDlDPASWRRQIAWVPQNPYLFA-GTIRENLRLGRPDAS--DEELEAaleaaGLDEFVAALP--DGLDTPLg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1152 ---QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHG 1228
Cdd:COG4988 469 eggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDG 547
|
....*...
gi 47078218 1229 KLKCCGSP 1236
Cdd:COG4988 548 RIVEQGTH 555
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1023-1236 |
3.38e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 3.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDD---KKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKN 1096
Cdd:PRK13637 5 IENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1097 LGMC---PQHNvLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSN---KRHSLVQtLSGGMKRKLSVAIAFVG 1170
Cdd:PRK13637 85 VGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedyKDKSPFE-LSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1171 GSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2081-2289 |
3.39e-29 |
|
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: 117.57 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKELLQVQQSL 2160
Cdd:cd03293 1 LEVRNVSKTYGGGG-GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIM 2289
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2080-2311 |
5.59e-29 |
|
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: 117.98 E-value: 5.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkellQVQQS 2159
Cdd:COG1124 1 MLEVRNLSVSYGQGG-RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-----TRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDE--------LTAREHLQLYTRLRGISwKDEARVVKwALEKLELTK-YADKPAGTYSGGNKRKLSTAIA 2230
Cdd:COG1124 75 KAFRRRVQMVFQDpyaslhprHTVDRILAEPLRIHGLP-DREERIAE-LLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2231 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGD 2309
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
..
gi 47078218 2310 GY 2311
Cdd:COG1124 233 PY 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2081-2294 |
6.81e-29 |
|
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: 117.05 E-value: 6.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYK----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFV 2144
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2145 NGHSVLKELLQVQQSLGYC-PQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKR 2223
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1023-1231 |
7.26e-29 |
|
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: 116.20 E-value: 7.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEmdEIRKNLGMCPQ 1102
Cdd:cd03226 2 IENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 ---HNVLFDrlTVEEHLWFYSRLKSMAQEEIRREMDKM-IEDLELsnkRHSlvQTLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:cd03226 79 dvdYQLFTD--SVREELLLGLKELDAGNEQAETVLKDLdLYALKE---RHP--LSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1179 EPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1231
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1026-1230 |
8.68e-29 |
|
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: 116.51 E-value: 8.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP-----PTSGSATIYGHDIRTEMD---EIRKNL 1097
Cdd:cd03260 6 LNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVdvlELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1098 GMCPQHNVLFdRLTVEEHLWFYSRLKSMAQeeiRREMDKMIEDL--------ELSNKRHSLvqTLSGGMKRKLSVAIAFV 1169
Cdd:cd03260 84 GMVFQKPNPF-PGSIYDNVAYGLRLHGIKL---KEELDERVEEAlrkaalwdEVKDRLHAL--GLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1170 GGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1024-1249 |
1.21e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.53 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1024 DKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCP 1101
Cdd:PRK10895 7 KNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRLTVEEHLWFYSRL-KSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 1181 TAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL------KGTY-GDGYRL 1249
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlqdehvKRVYlGEDFRL 241
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2080-2294 |
1.31e-28 |
|
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: 116.07 E-value: 1.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2159
Cdd:cd03257 1 LLEVKNLSVSFPTGG-GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LG----YCPQcD---ALFDELTAREHLQLYTRLRGISWKDEA--RVVKWALEKLELTK-YADKPAGTYSGGNKRKLSTAI 2229
Cdd:cd03257 80 RRkeiqMVFQ-DpmsSLNPRMTIGEQIAEPLRIHGKLSKKEArkEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2230 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1037-1229 |
1.78e-28 |
|
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: 115.85 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1114
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHRIaRLGIGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HL--WFYSRlksMAQEEIRREMDKMIEdL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1190
Cdd:COG0410 98 NLllGAYAR---RDRAEVRADLERVYE-LfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 47078218 1191 AIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:COG0410 174 EIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1030-1236 |
1.23e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.80 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDK----KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD--EIRKNLGMCPQH 1103
Cdd:PRK13633 14 YESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 --NVLFDRLtVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSR--AIILDE 1179
Cdd:PRK13633 94 pdNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR--VAIAGILAMRpeCIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1180 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1021-1230 |
1.37e-27 |
|
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: 121.86 E-value: 1.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1021 VCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGM 1099
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQHNVLFDRlTVEEHLWFYSRLKSMaqEEIRR-----EMDKMIEdlELSNKRHSLV----QTLSGGMKRKLSVAIAFVG 1170
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGDPDATD--EEIIEaarlaGLHDFIE--ALPMGYDTVVgeggSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1171 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLgDRIAIISHGKL 1230
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2080-2293 |
1.99e-27 |
|
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: 112.77 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELlq 2155
Cdd:COG0410 3 MLEVENLHAGY-----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYCPQCDALFDELTAREHLQLYTRLRGiswkdEARVVKWALEKL-----ELTKYADKPAGTYSGGNKRKLSTAIA 2230
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSLTVEENLLLGAYARR-----DRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2231 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2073-2293 |
2.66e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 121.77 E-value: 2.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2073 RGDADNDMVKIE--NLTkvyksRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL 2150
Cdd:NF033858 257 RPADDDDEPAIEarGLT-----MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2151 KELLQVQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2230
Cdd:NF033858 332 AGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2231 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEaLCTRLAIMVNGR 2293
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2078-2303 |
2.75e-27 |
|
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: 118.85 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKELL 2154
Cdd:COG1123 2 TPLLEVRDLSVRYPG---GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 QVQ-QSLGYCPQ-CDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2232
Cdd:COG1123 79 ALRgRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2233 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2303
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1029-1214 |
2.87e-27 |
|
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: 112.87 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1029 VYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSG-SATIYGHDI-RTEMDEIRKNLGMCpqHNVL 1106
Cdd:COG1119 11 VRRGGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLV--SPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1107 FDRLTVEEHLW------FYSrlkSM-----AQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1175
Cdd:COG1119 88 QLRFPRDETVLdvvlsgFFD---SIglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 47078218 1176 ILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDE 1214
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1021-1230 |
6.05e-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: 110.81 E-value: 6.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1021 VCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMC 1100
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1181 TAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03301 158 LSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2084-2299 |
8.68e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.52 E-value: 8.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2084 ENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH--SVLKELLQVQQSLG 2161
Cdd:PRK10895 7 KNLAKAYKGRRV-----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2162 YCPQCDALFDELTAREHLQLYTRLR-GISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1030-1215 |
1.02e-26 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 109.43 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMCPQH--N 1104
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1105 VLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1184
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 47078218 1185 DPYARRAIWDLILKYKP-GRTILLSTHHMDEA 1215
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAeGMTVVISTHDVDLA 190
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2093-2327 |
1.61e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 113.68 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2093 RKIGRILAVDRLCLGVRPGECFGLLGVNGAG--KTSTFKMLTGDESTTGGEAFVNGHSVLKELlqvQQSLG-YCPQCDAL 2169
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRAL---RRTIG*HRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2170 FDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2249
Cdd:NF000106 98 RESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2250 KARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGdGYMITVRTKSSQSVKDVV 2327
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPAHAAELDRMV 254
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2081-2299 |
2.06e-26 |
|
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: 110.08 E-value: 2.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQQS 2159
Cdd:cd03295 1 IEFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGisWKdEARVVKWALEKLEL-----TKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLK--WP-KEKIRERADELLALvgldpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2078-2300 |
2.41e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.17 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYK-----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGG 2140
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2141 EAFVNGH-SVLKELlqvqqSLGycpqcdalFD-ELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYS 2218
Cdd:COG1134 82 RVEVNGRvSALLEL-----GAG--------FHpELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2219 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDP----KARRFlwnlILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLAR----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....*.
gi 47078218 2295 RCLGSI 2300
Cdd:COG1134 225 VMDGDP 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2078-2294 |
2.41e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 109.36 E-value: 2.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KEL 2153
Cdd:COG1136 2 SPLLELRNLTKSYGTGE-GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2154 LQV-QQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2232
Cdd:COG1136 81 ARLrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2233 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSmEECEALCTRLAIMVNGRL 2294
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2082-2298 |
5.86e-26 |
|
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: 106.75 E-value: 5.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSL 2160
Cdd:cd03214 1 EVENLSVGYGGRTV-----LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQcdalfdeltarehlqlytrlrgiswkdearvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03214 76 AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2298
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1025-1230 |
6.00e-26 |
|
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: 107.88 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1025 KLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMC 1100
Cdd:cd03292 5 NVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1181 TAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1021-1237 |
6.19e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 111.70 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1021 VCVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMC 1100
Cdd:COG3839 4 LELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRAII---- 1176
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR--VALG-----RALVrepk 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1177 ---LDEPTAGVDP----YARRAIWDLILKYkpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPL 1237
Cdd:COG3839 154 vflLDEPLSNLDAklrvEMRAEIKRLHRRL--GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1018-1230 |
6.75e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 6.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1018 PLVVCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRK 1095
Cdd:COG3845 3 PPALELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1096 NLGMCPQHNVLFDRLTVEEHLW--------FYSRLKSmAQEEIRREMDKMIEDLELsnkrHSLVQTLSGGMKRKlsVAI- 1166
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVlgleptkgGRLDRKA-ARARIRELSERYGLDVDP----DAKVEDLSVGEQQR--VEIl 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 1167 -AFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:COG3845 154 kALYRGARILILDEPTAVLTPQEADELFEILrrLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2081-2307 |
7.75e-26 |
|
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: 108.09 E-value: 7.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKeLLQVQQSL 2160
Cdd:cd03300 1 IELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-LPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2241 DEPTTGMDPKARRflwNLILDLI----KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRF 2307
Cdd:cd03300 155 DEPLGALDLKLRK---DMQLELKrlqkELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRF 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1031-1234 |
9.53e-26 |
|
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: 107.74 E-value: 9.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1031 KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIRTemDEIRKNLGMCPQHNVLF 1107
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP--DQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DRLTVEEHLWFYS--RLKSMAQEEIRREM--DKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:cd03234 94 PGLTVRETLTYTAilRLPRKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1184 VDP------------YARRaiwdlilkykpGRTILLSTHHmDEADL--LGDRIAIISHGKLKCCG 1234
Cdd:cd03234 174 LDSftalnlvstlsqLARR-----------NRIVILTIHQ-PRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1030-1230 |
2.11e-25 |
|
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: 106.52 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLF- 1107
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 ----DRLTV------EEHLWFYSRLkSMAQEEIRREMDKMieDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIIL 1177
Cdd:cd03245 92 gtlrDNITLgapladDERILRAAEL-AGVTDFVNKHPNGL--DLQIGERG----RGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1178 DEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLgDRIAIISHGKL 1230
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1020-1236 |
2.67e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.18 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLG 1098
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1099 MCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRA--I 1175
Cdd:PRK13635 85 MVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQR--VAIAGVLALQPdiI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1176 ILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2083-2292 |
2.88e-25 |
|
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: 105.80 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2083 IENLTkvYKSRKIGRILAVDRLCLgvRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKELlqvQQSLG 2161
Cdd:cd03226 2 IENIS--FSYKKGTEILDDLSLDL--YAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKER---RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2162 YCPQ--CDALFDELTAREhlqLYTRLRGISwkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2239
Cdd:cd03226 75 YVMQdvDYQLFTDSVREE---LLLGLKELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2240 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2292
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1019-1239 |
4.44e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.51 E-value: 4.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1019 LVVCVDKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNL 1097
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1098 GMCPQ--HNVLFDrLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1175
Cdd:PRK13647 82 GLVFQdpDDQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1176 ILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1239
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2080-2294 |
5.47e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.03 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKelLQVQQ- 2158
Cdd:COG3842 5 ALELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--LPPEKr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2159 SLGYCPQCDALFDELTAREHLQLYTRLRGISwKDEARV-VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2237
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRMRGVP-KAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2238 IFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQReLGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1030-1236 |
9.53e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.80 E-value: 9.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1108
Cdd:COG1132 349 YPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 RlTVEEHLwFYSRLKSmAQEEIRR-----EMDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:COG1132 428 G-TIRENI-RYGRPDA-TDEEVEEaakaaQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1180 PTAGVDPYARRAIWDLILKYKPGRTILLSTH------HMdeadllgDRIAIISHGKLKCCGSP 1236
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA-------DRILVLDDGRIVEQGTH 558
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1034-1230 |
1.25e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1034 KKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-----MDEIRKNLGMCPQ--HNVL 1106
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1107 FDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNK--RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1184
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDliSKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47078218 1185 DPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK13641 177 DPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1035-1242 |
1.38e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.26 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1035 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDE-----IRKNLGMC---PQHNvL 1106
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkpLRKKVGIVfqfPEHQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1107 FDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSnkrHSLVQ----TLSGG-MKRklsVAIAFVGG--SRAIILDE 1179
Cdd:PRK13634 99 FEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP---EELLArspfELSGGqMRR---VAIAGVLAmePEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 1180 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGT 1242
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPreIFADPD 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2108-2294 |
1.45e-24 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 104.28 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKEllQVQQSLGYCPQCDALFDELTAREHLQLYTR 2184
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2185 LRGISWKDEARVVKWAlEKLELTKYADKPAGTY-----SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPkarrFLWNLI 2259
Cdd:cd03234 108 LRLPRKSSDAIRKKRV-EDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47078218 2260 L----DLIKTGRSVVLTSHS-MEECEALCTRLAIMVNGRL 2294
Cdd:cd03234 183 VstlsQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2080-2277 |
2.04e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.98 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKsrkiGRILAVDRLCLGVRPGE-CFgLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELL 2154
Cdd:COG2884 1 MIRFENVSKRYP----GGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 QVQQSLGYCPQcDA-LFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIG 2233
Cdd:COG2884 76 YLRRRIGVVFQ-DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47078218 2234 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2277
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1025-1234 |
2.27e-24 |
|
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: 103.77 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1025 KLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhDIRTEMDEirkNLGMCPQhn 1104
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGL---GGGFNPE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1105 vlfdrLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKL--SVAIAFvgGSRAIILDEPTA 1182
Cdd:cd03220 99 -----LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1183 GVDPY----ARRAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1234
Cdd:cd03220 172 VGDAAfqekCQRRLRELL---KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1023-1230 |
2.40e-24 |
|
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: 103.38 E-value: 2.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGM 1099
Cdd:cd03262 3 IKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQHNVLFDRLTVEEHLWFYSR-LKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA---- 1174
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQR--VAIA-----RAlamn 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1175 ---IILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03262 154 pkvMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2084-2294 |
2.43e-24 |
|
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: 102.63 E-value: 2.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2084 ENLTK-VYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVLKELLQvqQSL 2160
Cdd:cd03213 7 RNLTVtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR--KII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGIswkdearvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03213 85 GYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSM-EECEALCTRLAIMVNGRL 2294
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2078-2293 |
2.81e-24 |
|
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: 104.40 E-value: 2.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDES-TTGGEAFVNGHSVLKE-LLQ 2155
Cdd:COG1119 1 DPLLELRNVTVRRGGKTI-----LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRGGEdVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYC-PQCDALFDE-LTARE--------HLQLYtrlRGISWKDEARVVKWaLEKLELTKYADKPAGTYSGGNKRKL 2225
Cdd:COG1119 76 LRKRIGLVsPALQLRFPRdETVLDvvlsgffdSIGLY---REPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2226 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTG-RSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2081-2298 |
3.23e-24 |
|
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: 103.38 E-value: 3.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRK-----------------IGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAF 2143
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2144 VNG--HSVLkellqvqqSLGYcpqcdALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGN 2221
Cdd:cd03220 81 VRGrvSSLL--------GLGG-----GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2298
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1023-1236 |
3.25e-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: 103.96 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1102
Cdd:cd03296 5 VRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSMAQE----EIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1179 EPTAGVDPYARRAI--WDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:cd03296 162 EPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1029-1236 |
5.32e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 5.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1029 VYK-DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---TEMDEIRKNLGMCPQH- 1103
Cdd:PRK13639 8 KYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 -NVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:PRK13639 88 dDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1183 GVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2080-2294 |
5.74e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.57 E-value: 5.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MV--KIENLTKvYKSRKIGR-ILAVDRLCLG---------VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH 2147
Cdd:COG1129 236 MVgrELEDLFP-KRAAAPGEvVLEVEGLSVGgvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2148 SVlkELLQVQQS----LGYCP---QCDALFDELTARE-----HLQLYTRLRGISWKDEARVVKWALEKLEL-TKYADKPA 2214
Cdd:COG1129 315 PV--RIRSPRDAiragIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2215 GTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1025-1230 |
5.95e-24 |
|
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: 102.19 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1025 KLTKVYKDDKKLALNkLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHN 1104
Cdd:cd03298 2 RLDKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1105 VLFDRLTVEEH--LWFYSRLKSMAQEeiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03298 80 NLFAHLTVEQNvgLGLSPGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1183 GVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03298 158 ALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1023-1230 |
6.45e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.55 E-value: 6.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKK--LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE-----IRK 1095
Cdd:COG1135 4 LENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSErelraARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1096 NLGMCPQH-NvLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA 1174
Cdd:COG1135 83 KIGMIFQHfN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR--VGIA-----RA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1175 I-----IL--DEPTAGVDPYARRAIWDLILK--YKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:COG1135 155 LannpkVLlcDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2081-2298 |
9.66e-24 |
|
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: 101.56 E-value: 9.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK------ELL 2154
Cdd:cd03301 1 VELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 QVQQSLgycpqcdALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:cd03301 76 MVFQNY-------ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2298
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1021-1230 |
1.11e-23 |
|
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: 99.81 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1021 VCVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLG 1098
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1099 MCPQhnvlfdrltveehlwfysrlksmaqeeirremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1179 EPTAGVDPYARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03216 108 EPTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2081-2294 |
1.77e-23 |
|
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: 101.10 E-value: 1.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-----DESTTGGEAFVNGHSVLK---E 2152
Cdd:cd03260 1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldvD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2153 LLQVQQSLGYCPQCDALFDeLTAREHLQLYTRLRGISWKDEAR-VVKWALEKLELTKY-ADKPAGTY-SGGNKRKLSTAI 2229
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDeRVEEALRKAALWDEvKDRLHALGlSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2230 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2081-2293 |
2.06e-23 |
|
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: 99.57 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQ--- 2157
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDALFDELTAREHLQLytrlrgiswkdearvvkwALekleltkyadkpagtySGGNKRKLSTAIALIGYPAF 2237
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIAL------------------GL----------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2238 IFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1023-1230 |
2.37e-23 |
|
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: 101.42 E-value: 2.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVY--KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGM 1099
Cdd:COG1124 4 VRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQH--NVLFDRLTVEEHLwfySR-LKSMAQEEIRREMDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1175
Cdd:COG1124 84 VFQDpyASLHPRHTVDRIL---AEpLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 1176 ILDEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1033-1236 |
6.11e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.46 E-value: 6.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1033 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMCPQH--NVLF 1107
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1187
Cdd:PRK13636 97 SA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1188 ARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13636 176 GVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1029-1230 |
6.86e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1029 VYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTT---TMSILTGLFP--PTSGSATIYGHDI---RTEMDEIRKNLGMC 1100
Cdd:PRK14239 13 VYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTDTVDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDrLTVEEHLWFYSRLKSMAQEEIrreMDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1172
Cdd:PRK14239 92 FQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1173 RAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2080-2294 |
7.26e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.46 E-value: 7.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVL----KELL 2154
Cdd:COG1135 1 MIELENLSKTFPTKG-GPVTALDDVSLTIEKGEIFGIIGYSGAGK-STLiRCINLLERPTSGSVLVDGVDLTalseRELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 QVQQSLGYCPQCDALFDELTAREHLQLYTRLRGISwKDE--ARVvkwaLEKLELTKYADKpAGTY----SGGNKRKLSTA 2228
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVP-KAEirKRV----AELLELVGLSDK-ADAYpsqlSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2229 IALIGYPAFIFLDEPTTGMDPKARRflwnLILDLIK-----TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTR----SILDLLKdinreLGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1028-1230 |
7.70e-23 |
|
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: 98.39 E-value: 7.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1028 KVYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGL--FPPTSGSATIYGHDIRteMDEIRKNLGMCPQHNV 1105
Cdd:cd03213 16 SPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD--KRSFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTVEEHLWFYSRLKSmaqeeirremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:cd03213 93 LHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47078218 1186 PYARRAIWDLILKY-KPGRTILLSTHHM-DEADLLGDRIAIISHGKL 1230
Cdd:cd03213 144 SSSALQVMSLLRRLaDTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1030-1236 |
9.60e-23 |
|
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: 99.11 E-value: 9.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1108
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 ---RLTV-------EEHLWfySRLKSMAQEEIRREMDKMIEDLELSNKRHslvqtLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:cd03244 92 gtiRSNLdpfgeysDEELW--QALERVGLKEFVESLPGGLDTVVEEGGEN-----LSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1179 EPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDE-ADLlgDRIAIISHGKLKCCGSP 1236
Cdd:cd03244 165 EATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDSP 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1035-1230 |
9.83e-23 |
|
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: 97.50 E-value: 9.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1035 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCP---QHNVLFDR 1109
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 LTVEEHLwfysrlksmaqeeirremdkmiedlelsnkrhSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1189
Cdd:cd03215 93 LSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 47078218 1190 RAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03215 141 AEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1030-1236 |
9.97e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.21 E-value: 9.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsaTIYGHDIRTEMD---EIRKNLGMCPQH-NV 1105
Cdd:PRK13648 17 YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAITDDnfeKLRKHIGIVFQNpDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK13648 95 QFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1186 PYARRAIWDLILKYKPGR--TILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTP 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2080-2293 |
9.99e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.06 E-value: 9.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLtkvykSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQ 2157
Cdd:PRK11300 5 LLSVSGL-----MMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDALFDELTARE------HLQLYTRLRGISWKDEA----------RVVKWaLEKLELTKYADKPAGTYSGGN 2221
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIEnllvaqHQQLKTGLFSGLLKTPAfrraesealdRAATW-LERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2081-2301 |
1.31e-22 |
|
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: 98.95 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKigrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKELLQVQQSL 2160
Cdd:cd03299 1 LKVENLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKTGRSVVL-TSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2301
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1020-1236 |
1.89e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 1.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSA---TIYGHDIRTE-MDEIRK 1095
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNskiTVDGITLTAKtVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1096 NLGMCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1174
Cdd:PRK13640 85 KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1175 IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1026-1230 |
2.61e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.03 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKDDKK--LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGM 1099
Cdd:PRK11153 7 ISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQH-NVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRAIIL- 1177
Cdd:PRK11153 87 IFQHfNLLSSR-TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR--VAIARALASNPKVLl 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1178 -DEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK11153 164 cDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1037-1225 |
2.79e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG--HDIRTEMDEIRKNLGMCPQHNVLFDRLTVEE 1114
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLWF---YSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGmKRKLsVAI--AFVGGSRAIILDEPTAGVDPYAR 1189
Cdd:COG1129 99 NIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-QQQL-VEIarALSRDARVLILDEPTASLTEREV 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 47078218 1190 RAIWDLI--LKYKpGRTILLSTHHMDEADLLGDRIAII 1225
Cdd:COG1129 177 ERLFRIIrrLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1036-1236 |
3.07e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 3.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1036 LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCP--QHNVLFDRLTVE 1113
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1114 EHL-----------WFYSRLKSMAQEEIRRE-MDKMIEDLE------LSNKRHSlvqTLSGGMKRKLSVAIAFVGGSRAI 1175
Cdd:PRK11300 99 ENLlvaqhqqlktgLFSGLLKTPAFRRAESEaLDRAATWLErvglleHANRQAG---NLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1176 ILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2103-2274 |
3.35e-22 |
|
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: 96.66 E-value: 3.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2103 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLY 2182
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2183 TRLRGiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA-IALIGYPAFIfLDEPTTGMDPKARRFLWNLILD 2261
Cdd:TIGR01189 98 AAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALArLWLSRRPLWI-LDEPTTALDKAGVALLAGLLRA 172
|
170
....*....|...
gi 47078218 2262 LIKTGRSVVLTSH 2274
Cdd:TIGR01189 173 HLARGGIVLLTTH 185
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1037-1235 |
3.44e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 98.27 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIR-KNLGMC-----PqhNVlFDRL 1110
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDEHEiARLGIGrkfqkP--TV-FEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 TVEEHL---------WFYSrLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:COG4674 101 TVFENLelalkgdrgVFAS-LFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1182 AGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS 1235
Cdd:COG4674 180 AGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1037-1236 |
3.79e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 99.05 E-value: 3.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-----EMDEIRKNLGMCPQ--HNVLFDR 1109
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 lTVEEHLWFYSRLKSMAQEE---IRREMDKMI---EDLELSNKRHslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEaeaLAREKLALVgisESLFEKNPFE-----LSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1184 VDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13649 176 LDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1036-1236 |
6.35e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.88 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1036 LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMDEIR-KNLGMCPQHNVLFDRL 1110
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 TVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1190
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47078218 1191 AIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK10070 202 EMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2098-2294 |
7.58e-22 |
|
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: 95.19 E-value: 7.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2098 ILAVDRLCLG---------VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ--VQQSLGYCP-- 2164
Cdd:cd03215 4 VLEVRGLSVKgavrdvsfeVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAYVPed 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2165 -QCDALFDELTAREHLQLYTRLrgiswkdearvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEP 2243
Cdd:cd03215 84 rKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2244 TTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2081-2299 |
8.83e-22 |
|
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: 96.64 E-value: 8.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQvQQSL 2160
Cdd:cd03296 3 IEVRNVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWK-DEARV---VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2236
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSERpPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2237 FIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1037-1230 |
9.28e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.49 E-value: 9.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE---IRKNLGMCPQHNVLFDRLTVE 1113
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTakiMREAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1114 EHL----WFYSRlkSMAQEEIRRemdkmIEDL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1187
Cdd:PRK11614 99 ENLamggFFAER--DQFQERIKW-----VYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47078218 1188 ARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK11614 172 IIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2077-2294 |
9.95e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 9.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2077 DNDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVL----K 2151
Cdd:COG1129 1 AEPLLEMRGISKSF-----GGVKALDGVSLELRPGEVHALLGENGAGK-STLmKILSGVYQPDSGEILLDGEPVRfrspR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2152 ELLQ-----VQQSLgycpqcdALFDELTAREHL---QLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKR 2223
Cdd:COG1129 75 DAQAagiaiIHQEL-------NLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1023-1229 |
1.11e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.08 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVY---KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKN--- 1096
Cdd:COG1101 4 LKNLSKTFnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKRAkyi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1097 --------LGMCPqhnvlfdRLTVEEHLWF-YSRLKSM--------AQEEIRREMDKMIeDLELSNKRHSLVQTLSGGMK 1159
Cdd:COG1101 83 grvfqdpmMGTAP-------SMTIEENLALaYRRGKRRglrrgltkKRRELFRELLATL-GLGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1160 RKLSVAIAFVGGSRAIILDEPTAGVDPyaRRAiwDLILKY------KPGRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDP--KTA--ALVLELtekiveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1026-1267 |
1.34e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQH- 1103
Cdd:PRK13652 9 LCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVGLVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 -NVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:PRK13652 88 dDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1183 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGTYGDGYRLTLVKRPAEP 1258
Cdd:PRK13652 167 GLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDLPSLPKLI 246
|
....*....
gi 47078218 1259 GGPQEPGLA 1267
Cdd:PRK13652 247 RSLQAQGIA 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2081-2294 |
1.84e-21 |
|
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: 96.56 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSR-------------------KIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2141
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2142 AFVNGHSVL----KELLQVQ-QSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGT 2216
Cdd:cd03294 81 VLIDGQDIAamsrKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2217 YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2078-2294 |
2.09e-21 |
|
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: 101.03 E-value: 2.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNghsVLKELL--- 2154
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGDEWVdmt 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 --------QVQQSLGYCPQCDALFDELTAREHLqlyTRLRGISWKDEARVVKwALEKLELTKYADKPA--------GTYS 2218
Cdd:TIGR03269 354 kpgpdgrgRAKRYIGILHQEYDLYPHRTVLDNL---TEAIGLELPDELARMK-AVITLKMVGFDEEKAeeildkypDELS 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2219 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKArEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2108-2274 |
2.41e-21 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 102.49 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTGDEST---TGGEAFVNGHSVLKELlqvQQSLGYCPQCDALFDELTAREHLQLYTR 2184
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2185 LR---GISWKDEARVVKWALEKLELTKYADKPAGTYSGG----NKRKLSTAIALIGYPA-FIFLDEPTTGMDPKARRFLW 2256
Cdd:TIGR00956 863 LRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*...
gi 47078218 2257 NLILDLIKTGRSVVLTSH 2274
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIH 960
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2081-2300 |
2.62e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 2.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE---LLQVQ 2157
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCD--ALFDElTAREHLQLYTRLRGISWKDEARVVKWALE--KLELTKYADKPAGTYSGGNKRKLSTAIALIG 2233
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2234 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2300
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1032-1211 |
3.15e-21 |
|
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: 100.51 E-value: 3.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1032 DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1110
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 TVEEHLwfysRL--KSMAQEEIRREMDKM-----IEDLE--LSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:TIGR02868 424 TVRENL----RLarPDATDEELWAALERVgladwLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|
gi 47078218 1182 AGVDPYARRAIWDLILKYKPGRTILLSTHH 1211
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1033-1236 |
4.20e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.76 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1033 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdiRT----EMdeirkNLGMCPQhnvlfd 1108
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVsallEL-----GAGFHPE------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 rLTVEEHLWFYSRLKSMAQEEIRREMDKmIEDL-ELSNKRHSLVQTLSGGMKRKLSVAIAFvggsrAI-----ILDEPTA 1182
Cdd:COG1134 103 -LTGRENIYLNGRLLGLSRKEIDEKFDE-IVEFaELGDFIDQPVKTYSSGMRARLAFAVAT-----AVdpdilLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1183 GVDPY----ARRAIWDLILKykpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:COG1134 176 VGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1030-1231 |
5.25e-21 |
|
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: 92.76 E-value: 5.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDr 1109
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 ltveehlwfysrlksmaqeeirremdkmiedlelSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1189
Cdd:cd03247 89 ----------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1190 RAIWDLILKYKPGRTILLSTHHmdeadLLG----DRIAIISHGKLK 1231
Cdd:cd03247 135 RQLLSLIFEVLKDKTLIWITHH-----LTGiehmDKILFLENGKII 175
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1020-1236 |
6.18e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.97 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNL 1097
Cdd:NF033858 1 VARLEGVSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1098 GMCPQ---HNvLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1174
Cdd:NF033858 79 AYMPQglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1175 IILDEPTAGVDPYARRAIWDLI---LKYKPGRTILLSTHHMDEADLLgDRIAIISHGKLKCCGSP 1236
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIdriRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1030-1261 |
6.24e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 95.07 E-value: 6.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMC---PQH 1103
Cdd:PRK13638 11 YQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 NVLFDrlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:PRK13638 89 QIFYT--DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1184 VDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGTYGDGYRLT---LVKRPAE 1257
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPgeVFACTEAMEQAGLTqpwLVKLHTQ 246
|
....
gi 47078218 1258 PGGP 1261
Cdd:PRK13638 247 LGLP 250
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1037-1251 |
8.08e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.23 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-----EMDEIRKNLGMCPQ--HNVLFDR 1109
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 lTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSnkRHSLVQT---LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1186
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1187 YARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGTYGDGYRLTL 1251
Cdd:PRK13646 179 QSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPkeLFKDKKKLADWHIGL 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1032-1241 |
8.47e-21 |
|
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: 93.44 E-value: 8.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1032 DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1110
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 TVEEHLwFYSRLKSMAQEEIRRE----MDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03254 92 TIMENI-RLGRPNATDEEVIEAAkeagAHDFIMKLP--NGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1183 GVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP--LFLKG 1241
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNA----DKILVLDDGKIIEEGTHdeLLAKK 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1023-1241 |
8.79e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDK-KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKNLGM 1099
Cdd:PRK13650 7 VKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENvwDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRA--II 1176
Cdd:PRK13650 86 VFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR--VAIAGAVAMRPkiII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1177 LDEPTAGVDPYARRaiwDLI-----LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP--LFLKG 1241
Cdd:PRK13650 164 LDEATSMLDPEGRL---ELIktikgIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPreLFSRG 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1032-1243 |
9.10e-21 |
|
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: 93.83 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1032 DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1110
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 TVEEHLwFYSRLkSMAQEEIRREMDK-MIED--LELSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:cd03253 90 TIGYNI-RYGRP-DATDEEVIEAAKAaQIHDkiMRFPDGYDTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1184 VDPYARRAIWDLILKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPLFL---KGTY 1243
Cdd:cd03253 168 LDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELlakGGLY 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1033-1236 |
1.00e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1033 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQH-NVLFDR 1109
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNpETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 LTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1189
Cdd:PRK13644 93 RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47078218 1190 RAIWDLILK-YKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13644 173 IAVLERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEP 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1030-1235 |
1.05e-20 |
|
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: 93.70 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1108
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 RlTVEEHLWFYSRLKSMAQ-EEIRREMDKMIEDLELSNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:cd03252 90 R-SIRDNIALADPGMSMERvIEAAKLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1184 VDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLKCCGS 1235
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2081-2294 |
1.55e-20 |
|
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: 90.57 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKellqvqqsl 2160
Cdd:cd03216 1 LELRGITKRF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 gycpqcdalfdeLTAREHLQLytrlrGIswkdeaRVVkwalekleltkyadkpagtY--SGGNKRKLSTAIALIGYPAFI 2238
Cdd:cd03216 67 ------------ASPRDARRA-----GI------AMV-------------------YqlSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2239 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2082-2293 |
1.97e-20 |
|
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: 93.02 E-value: 1.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQVQ 2157
Cdd:cd03256 2 EVENLSKTYPNGKK----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDALFDELTAREHLqLYTRLRGISW---------KDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA 2228
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENV-LSGRLGRRSTwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2229 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2080-2294 |
2.04e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.25 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQ 2155
Cdd:PRK11153 1 MIELKNISKVFPQGG-RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKD-EARVvkwaLEKLELTKYADKpAGTY----SGGNKRKLSTAIA 2230
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEiKARV----TELLELVGLSDK-ADRYpaqlSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2231 LIGYPAFIFLDEPTTGMDPKARRflwnLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTR----SILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1023-1226 |
2.18e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 2.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVY--KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEiRknlGMC 1100
Cdd:COG4525 6 VRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-R---GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47078218 1181 TAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIIS 1226
Cdd:COG4525 162 FGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1030-1229 |
2.94e-20 |
|
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: 92.29 E-value: 2.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1108
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 RlTVEEHLwFYSRLKSmAQEEIRR-----EMDKMIEDLElsNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:cd03251 90 D-TVAENI-AYGRPGA-TREEVEEaaraaNAHEFIMELP--EGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1180 PTAGVDPYARRAIWDLILKYKPGRTIL-----LSThhMDEAdllgDRIAIISHGK 1229
Cdd:cd03251 165 ATSALDTESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1010-1236 |
3.28e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.40 E-value: 3.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1010 MEEEPTHLPLVVCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTE 1089
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1090 MDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIR-REMD--KMIEDLELSNKRhslVQTLSGGMKRKLSVAI 1166
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITpRVMEalRMVQLEEFAQRK---PHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1167 AFVGGSRAIILDEPTAGVDpYARRAIWDLILKY---KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD-YKLRKQMQNELKAlqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1037-1215 |
4.15e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtemdeirKNLGMCPQHNVLFDRL--TVEE 1114
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 --------HLWFYSRLKSMAQEEIRREMDKM-IEDLElsnKRHslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:NF040873 77 lvamgrwaRRGLWRRLTRDDRAAVDDALERVgLADLA---GRQ--LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|.
gi 47078218 1186 PYARRAIWDLILKY-KPGRTILLSTHHMDEA 1215
Cdd:NF040873 152 AESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1030-1236 |
5.26e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVL-F 1107
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAVLPQHSSLsF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DrLTVEE--HLWFYSRLKSMAQEeiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFV--------GGSRAIIL 1177
Cdd:PRK13548 90 P-FTVEEvvAMGRAPHGLSRAED--DALVAAALAQVDLAHLAGRDYPQLSGGEQQR--VQLARVlaqlwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 1178 DEPTAGVDPY--------ARRaiwdliLKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13548 165 DEPTSALDLAhqhhvlrlARQ------LAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
2110-2295 |
5.89e-20 |
|
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: 90.82 E-value: 5.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2110 PGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG----HSVLKELLQVQQ-SLGYCPQCDALFDELTAREHLqLYTR 2184
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQrKIGLVFQQYALFPHLNVRENL-AFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2185 LRGISWKDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK 2264
Cdd:cd03297 101 KRKRNREDRISVDE-LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|..
gi 47078218 2265 T-GRSVVLTSHSMEECEALCTRLAIMVNGRLR 2295
Cdd:cd03297 180 NlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2108-2274 |
5.97e-20 |
|
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: 90.00 E-value: 5.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVLKELlqvQQSLGYCPQCDALFDELTAREHLQLYTRL 2185
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2186 RGISwkdearvvkwaLEkleltkyadkpagtysggNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT 2265
Cdd:cd03232 107 RGLS-----------VE------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
....*....
gi 47078218 2266 GRSVVLTSH 2274
Cdd:cd03232 158 GQAILCTIH 166
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2080-2343 |
6.54e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 6.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKELLQVQQS 2159
Cdd:PRK11607 19 LLEIRNLTKSFDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2239
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2240 LDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS----IQHLKNRFGDGYMIT 2314
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFIGS 252
|
250 260
....*....|....*....|....*....
gi 47078218 2315 VrtkssqsvkdvvrffnrNFPEAMLKERH 2343
Cdd:PRK11607 253 V-----------------NVFEGVLKERQ 264
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2100-2294 |
7.74e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 7.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKELLQVQQSLGYCPQC--DALF---- 2170
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKTVGIVFQNpdDQLFaptv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2171 DELTAREHLQLytrlrGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2250
Cdd:PRK13639 97 EEDVAFGPLNL-----GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47078218 2251 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2083-2274 |
1.14e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2083 IENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkellqvqQSLGY 2162
Cdd:COG0488 1 LENLSKSFGGRPL-----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2163 CPQCDALFDELTAREHL--------QLYTRLRGIS-------------------------WKDEARVVKwALEKLELTK- 2208
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVldgdaelrALEAELEELEaklaepdedlerlaelqeefealggWEAEARAEE-ILSGLGFPEe 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2209 YADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLildLIKTGRSVVLTSH 2274
Cdd:COG0488 145 DLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LKNYPGTVLVVSH 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2080-2274 |
1.25e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTkvykSRKIGRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2159
Cdd:PRK13538 1 MLEARNLA----CERDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGISwkDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTA-IALIGYPAFI 2238
Cdd:PRK13538 76 LLYLGHQPGIKTELTALENLRFYQRLHGPG--DDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALArLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 47078218 2239 fLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2274
Cdd:PRK13538 153 -LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1026-1236 |
1.44e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNV 1105
Cdd:PRK11607 25 LTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1186 PYARR----AIWDLILKYkpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK11607 182 KKLRDrmqlEVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2080-2305 |
2.82e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQ 2157
Cdd:PRK09700 5 YISMAGIGK-----SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDALFDELTAREHL---QLYTR----LRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2230
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2231 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2305
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1038-1228 |
2.96e-19 |
|
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: 89.06 E-value: 2.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrtemDEIRKNLGMCPQHNVLFDRLTVEEH-- 1115
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRMVVFQNYSLLPWLTVRENia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1116 LWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1195
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 47078218 1196 ILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1228
Cdd:TIGR01184 157 LMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1017-1236 |
3.83e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.34 E-value: 3.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1017 LPLVVCVDKLTKVYkddkklaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIrtEMDEI 1093
Cdd:TIGR00955 27 LRGCFCRERPRKHL-------LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1094 RKNLGMCPQHNVLFDRLTVEEHLWFYSRLK---SMAQEEIRREMDKMIEDLELSNKRHSLVQT------LSGGMKRKLSV 1164
Cdd:TIGR00955 98 RAISAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1165 AIAFVGGSRAIILDEPTAGVDPYAR----RAIWDLILKykpGRTILLSTHHmDEADL--LGDRIAIISHGKLKCCGSP 1236
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAysvvQVLKGLAQK---GKTIICTIHQ-PSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1042-1230 |
4.41e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1042 SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLGMCP---QHNVLFDRLTVEE-- 1114
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYVPedrKGEGLVLDLSIREni 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 ---HLWFYSRLKSMAQEEIRREMDKMIEDLEL-SNKRHSLVQTLSGGMKRKlsVAIA--FVGGSRAIILDEPTAGVDPYA 1188
Cdd:COG1129 352 tlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPTRGIDVGA 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47078218 1189 RRAIWDLILKY-KPGRTILLSTHHMDEadLLG--DRIAIISHGKL 1230
Cdd:COG1129 430 KAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1037-1236 |
6.11e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 6.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSA-----TIYGHDIRTEMDEIRKNLGMCPQ--HNVLFDR 1109
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 lTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNK--RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1187
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1188 ARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK13643 179 ARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1029-1235 |
7.34e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.57 E-value: 7.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1029 VYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP------PTSGSATIYGHDI-RTEMDEIRKNLGMCP 1101
Cdd:PRK14246 18 LYINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRLTVEEHLWFysRLKSMAQEEiRREMDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSR 1173
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAY--PLKSHGIKE-KREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1174 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS 1235
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1023-1224 |
7.80e-19 |
|
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: 90.11 E-value: 7.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIRT----EMDEI 1093
Cdd:COG0444 4 VRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1094 R-KNLGMCPQhnvlfD-------RLTVEEHLW-FYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQ---TLSGGMKRK 1161
Cdd:COG0444 84 RgREIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1162 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAI 1224
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1033-1211 |
8.06e-19 |
|
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: 87.03 E-value: 8.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1033 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTV 1112
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1113 EEHLWFYSRLKSMAQeeirREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1192
Cdd:TIGR01189 91 LENLHFWAAIHGGAQ----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|
gi 47078218 1193 WDLILKY-KPGRTILLSTHH 1211
Cdd:TIGR01189 167 AGLLRAHlARGGIVLLTTHQ 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2078-2295 |
8.27e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 8.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkellqvq 2157
Cdd:COG0488 313 KKVLELEGLSKSYGDKTL-----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETV-------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 qSLGYCPQ-CDALFDELTAREHLQlytrlRGISWKDEARVVKWaLEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:COG0488 379 -KIGYFDQhQEELDPDKTVLDELR-----DGAPGGTEQEVRGY-LGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2236 AFIFLDEPTTGMDPKARrflwNLILDLIKT--GrSVVLTSHSMEECEALCTRLAIMVNGRLR 2295
Cdd:COG0488 452 NVLLLDEPTNHLDIETL----EALEEALDDfpG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2098-2294 |
1.16e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2098 ILAVDRLC--------LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQQSLGYCP--- 2164
Cdd:PRK15439 268 VLTVEDLTgegfrnisLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2165 QCDALFDELTAREHLQLYTRLRGISWKDEARvvkwalEKLELTKY----------ADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:PRK15439 348 QSSGLYLDAPLAWNVCALTHNRRGFWIKPAR------ENAVLERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2080-2294 |
1.19e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL---KELLQV 2156
Cdd:PRK09493 1 MIEFKNVSKHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 QQSLGYCPQCDALFDELTAREHLQL-YTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2236 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1023-1236 |
1.34e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.14 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1102
Cdd:PRK10851 5 IANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWF----YSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:PRK10851 82 HYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1179 EPTAGVDPYARRAI--WDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK10851 162 EPFGALDAQVRKELrrWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2081-2294 |
1.70e-18 |
|
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: 86.31 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQV 2156
Cdd:cd03292 1 IEFINVTKTYP----NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 QQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2236
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2237 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1037-1237 |
2.52e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT------EMDEIRKNLGMC---PQHNVLF 1107
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikEVKRLRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DrlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSN---KRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1184
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyvKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1185 DPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPL 1237
Cdd:PRK13645 182 DPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1029-1245 |
5.23e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 5.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1029 VYKDDKKLALNKL---SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQH- 1103
Cdd:PRK13642 11 VFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1184 VDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPLFLKGTYGD 1245
Cdd:PRK13642 171 LDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
2100-2278 |
5.24e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.21 E-value: 5.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvlkellqvqqSLGYCPQCDALFDEL--TARE 2177
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2178 --------HLQLYTRLRGiswKDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2249
Cdd:NF040873 77 lvamgrwaRRGLWRRLTR---DDRAAVDD-ALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*....
gi 47078218 2250 KARRFLWNLILDLIKTGRSVVLTSHSMEE 2278
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2109-2313 |
7.55e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2109 RPGECFGLLGVNGAGKTS-----TFKMLTGdeSTTGGEAFVNGHSVLKEllQVQQSLGYCPQCDALFDELTAREHLQLYT 2183
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPIDAK--EMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2184 RLR---GISWKDEARVVKWALEKLELTKYADKPAGT------YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2254
Cdd:TIGR00955 125 HLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2255 LWNLILDLIKTGRSVVLTSH--SMEECEaLCTRLAIMVNGRLRCLGSIQHLKNRFGD-GYMI 2313
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDlGHPC 265
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2080-2289 |
7.80e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.68 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKellqvqqs 2159
Cdd:COG4525 3 MLTVRHVSVRYPGGG-QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 lgycP--------QCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIAL 2231
Cdd:COG4525 74 ----PgadrgvvfQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2232 IGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIM 2289
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1012-1231 |
8.27e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1012 EEPTHLP-LVVCVDKLTKVYkDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIRtem 1090
Cdd:COG0488 306 PPPERLGkKVLELEGLSKSY-GDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1091 deirknLGMCPQHNVLFD-RLTVEEHLWfysRLKSMAQE-EIRremdKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIA 1167
Cdd:COG0488 380 ------IGYFDQHQEELDpDKTVLDELR---DGAPGGTEqEVR----GYLGRFLFSGDDaFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1168 FVGGSRAIILDEPTAGVDPYARRAIWDLILKYkPGrTILLSTHHMDEADLLGDRIAIISHGKLK 1231
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2098-2294 |
8.79e-18 |
|
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: 84.56 E-value: 8.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2098 ILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKEL--LQVQQSLGYCPQCDALFDElTA 2175
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD-IRQLdpADLRRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2176 REHLQLytrlrGISWKDEARVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPT 2244
Cdd:cd03245 95 RDNITL-----GAPLADDERILR-AAELAGVTDFVNKhPNGldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2245 TGMDPKA-RRFLWNliLDLIKTGRSVVLTSH--SMEEceaLCTRLAIMVNGRL 2294
Cdd:cd03245 169 SAMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGRI 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1037-1234 |
8.99e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 8.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCPQHNVLFDRLTVEE 1114
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLwFYSRL---KSMA-----QEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1186
Cdd:PRK09700 100 NL-YIGRHltkKVCGvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1187 YARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1234
Cdd:PRK09700 179 KEVDYLFLIMnqLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2081-2294 |
9.47e-18 |
|
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: 84.12 E-value: 9.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL---KELLQVQ 2157
Cdd:cd03262 1 IEIKNLHKSFGDFHV-----LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDALFDELTAREHLQL-YTRLRGISwKDEARvvKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIG 2233
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMS-KAEAE--ERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2234 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1024-1230 |
9.69e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1024 DKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGM 1099
Cdd:PRK10908 5 EHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQ-HNVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:PRK10908 84 IFQdHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1179 EPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1034-1230 |
1.34e-17 |
|
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: 83.88 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1034 KKLALNKLSLNL-YENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsaTIYGHDirTEMDEIRKNLGMCP---------QH 1103
Cdd:cd03297 8 KRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGG--TIVLNG--TVLFDSRKKINLPPqqrkiglvfQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 NVLFDRLTVEEHLWFysRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:cd03297 84 YALFPHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 47078218 1184 VDPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1023-1236 |
1.59e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGMCP 1101
Cdd:PRK11231 5 TENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRLTVEE--------HLWFYSRLKSMAQEEIRREMDKMiEDLELSNKRhslVQTLSGGMKRKLSVAIAFVGGSR 1173
Cdd:PRK11231 83 QHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQT-RINHLADRR---LTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1174 AIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1037-1230 |
1.60e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.29 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDE-----IRKNLGMCPQHNVLFDR 1109
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairlLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 LTVEEHLWFYS-RLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1188
Cdd:COG4161 97 LTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47078218 1189 RRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:COG4161 177 TAQVVEIIRELSqTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2101-2298 |
2.02e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 2.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2101 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKELLQVQQSLGYCPQCDALFDELTAREHL 2179
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2180 QL-----YTRLRGISWKDEaRVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD-PKARR 2253
Cdd:PRK09536 99 EMgrtphRSRFDTWTETDR-AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47078218 2254 FLwNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2298
Cdd:PRK09536 178 TL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2100-2308 |
2.09e-17 |
|
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: 88.67 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKELL--QVQQSLGYCPQCDALFDElTARE 2177
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD-LRDLDedDLRRRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2178 HLQLyTRLRGiswkDEARVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTG 2246
Cdd:COG4987 428 NLRL-ARPDA----TDEELWA-ALERVGLGDWLAAlPDGldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2247 MDPKARRFLWNLILDLIKtGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2308
Cdd:COG4987 502 LDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1020-1228 |
2.21e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP--PTSGS-ATIYGHDIRTE---MDEI 1093
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQREgrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1094 RKN---LGMCPQHNVLFDRLTVEEHL----------------WFYSRLKSMAQEEIRRemdkmiedLELSNKRHSLVQTL 1154
Cdd:PRK09984 82 RKSranTGYIFQQFNLVNRLSVLENVligalgstpfwrtcfsWFTREQKQRALQALTR--------VGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1155 SGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHG 1228
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1038-1229 |
2.68e-17 |
|
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: 83.74 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHL 1116
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1117 WF--YSRLKSMAQEEIRR-EMDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1189
Cdd:cd03249 98 RYgkPDATDEEVEEAAKKaNIHDFIMSLP--DGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47078218 1190 RAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGK 1229
Cdd:cd03249 176 KLVQEALDRAMKGRTTIVIAHRLStirNA----DLIAVLQNGQ 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1023-1230 |
2.94e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.14 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYkdDKKL-----ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-------- 1089
Cdd:PRK13651 5 VKNIVKIF--NKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1090 -----------------MDEIRKNLGMCPQ--HNVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIE--DLELSNKRH 1148
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIElvGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1149 SLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISH 1227
Cdd:PRK13651 162 SPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
...
gi 47078218 1228 GKL 1230
Cdd:PRK13651 241 GKI 243
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1026-1230 |
3.09e-17 |
|
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: 87.85 E-value: 3.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHN 1104
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1105 VLFDRlTVEEHLwFYSRLKSMAQEEIRREMdKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSRAII 1176
Cdd:TIGR02203 416 VLFND-TIANNI-AYGRTEQADRAEIERAL-AAAYAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1177 LDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1230
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1033-1211 |
3.27e-17 |
|
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: 82.54 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1033 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTV 1112
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1113 EEHLWFYSRLKSMAQEEirremdKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1192
Cdd:cd03231 91 LENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 47078218 1193 WDLILKY-KPGRTILLSTHH 1211
Cdd:cd03231 165 AEAMAGHcARGGMVVLTTHQ 184
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1023-1230 |
3.40e-17 |
|
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: 81.49 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1101
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDrltveehlwfysrlKSMAqEEIrremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:cd03246 83 QDDELFS--------------GSIA-ENI-----------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1182 AGVDPYARRAIWDLILKYK-PGRTILLSTHHMdEADLLGDRIAIISHGKL 1230
Cdd:cd03246 125 SHLDVEGERALNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2080-2299 |
3.65e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 3.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG----HSVLKELlq 2155
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpisMLSSRQL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 vQQSLGYCPQCDALFDELTARE--------HLQLYTRLrgiSWKDEARVvKWALEKLELTKYADKPAGTYSGGNKRKLST 2227
Cdd:PRK11231 75 -ARRLALLPQHHLTPEGITVRElvaygrspWLSLWGRL---SAEDNARV-NQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2228 AIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1010-1236 |
3.69e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.90 E-value: 3.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1010 MEEEPTHLPLVVCVDKLTKVYkDDKK----LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI---- 1081
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYCVF-DEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1082 YGHDIRTEMD-------------EIRKNLGMC---PQHNVLFDrlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSN 1145
Cdd:PRK13631 90 IGDKKNNHELitnpyskkiknfkELRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1146 ---KRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDR 1221
Cdd:PRK13631 168 sylERSPF--GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEVADE 245
|
250
....*....|....*
gi 47078218 1222 IAIISHGKLKCCGSP 1236
Cdd:PRK13631 246 VIVMDKGKILKTGTP 260
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2080-2294 |
4.81e-17 |
|
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: 84.72 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVL----KE 2152
Cdd:COG0444 1 LLEVRNLKVYFPTRR-GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLklseKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2153 LLQV-QQSLGYCPQcDAL------------FDElTAREHlqlytrlRGISWKD-EARVVKwALEKLELT---KYADKPAG 2215
Cdd:COG0444 80 LRKIrGREIQMIFQ-DPMtslnpvmtvgdqIAE-PLRIH-------GGLSKAEaRERAIE-LLERVGLPdpeRRLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2216 TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2056-2308 |
5.31e-17 |
|
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: 87.58 E-value: 5.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2056 KPVEDDVDVASERQRVLRGDadndmVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDE 2135
Cdd:COG2274 454 LPPEREEGRSKLSLPRLKGD-----IELENVSFRYPGDSP---PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2136 STTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDElTAREHLQLytrlrGISWKDEARVVkWALEKLELTKYADK-P 2213
Cdd:COG2274 526 EPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITL-----GDPDATDEEII-EAARLAGLHDFIEAlP 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2214 AG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMeECEALC 2283
Cdd:COG2274 599 MGydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLA 676
|
250 260
....*....|....*....|....*
gi 47078218 2284 TRLAIMVNGRLRCLGSIQHLKNRFG 2308
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1041-1210 |
5.87e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 5.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1041 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGmcpQHNVLFDRLTVEEHLWFY 1119
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG---HRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1120 SRLKSMAQEEIrremDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY 1199
Cdd:PRK13539 98 AAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|..
gi 47078218 1200 -KPGRTILLSTH 1210
Cdd:PRK13539 174 lAQGGIVIAATH 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1035-1228 |
9.90e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 9.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1035 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEirknLGMCPQHNVLFDRLTVEE 1114
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWD 1194
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 47078218 1195 LILK--YKPGRTILLSTHHMDEADLLGDRIAIISHG 1228
Cdd:PRK11248 170 LLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2081-2308 |
1.03e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.10 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--KELLQVQQ 2158
Cdd:NF033858 2 ARLEGVSHRY-----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdaRHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2159 SLGYCPQC--DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2236
Cdd:NF033858 77 RIAYMPQGlgKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2237 FIFLDEPTTGMDPKARRFLWNLIlDLIKTGR---SVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2308
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELI-DRIRAERpgmSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1024-1231 |
1.39e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 82.17 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1024 DKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdirtEMDEIRKNLGMCPQh 1103
Cdd:PRK13546 26 DALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 nvlfdrLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP-TA 1182
Cdd:PRK13546 100 ------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1183 GVDPYARRAIwDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLK 1231
Cdd:PRK13546 174 GDQTFAQKCL-DKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1114-1256 |
1.40e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 84.02 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1114 EHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1193
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1194 DLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGTYGDgyrLTLVKRPA 1256
Cdd:NF000106 185 DEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGG---RTLQIRPA 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2077-2294 |
1.58e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.44 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2077 DNDMVKIENLTKVYKSRKIG-RILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE--L 2153
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEStEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEenL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2154 LQVQQSLGYCPQ------CDALFDELTA--REHLqlytrlrGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKL 2225
Cdd:PRK13633 81 WDIRNKAGMVFQnpdnqiVATIVEEDVAfgPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2226 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECeALCTRLAIMVNGRL 2294
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1028-1247 |
1.92e-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: 79.88 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1028 KVYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGlFP---PTSGSATIYGHDIrTEM--DEI-RKNLGMCP 1101
Cdd:cd03217 7 HVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLppEERaRLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRLTVEEHLwfysrlksmaqeeirREMDKmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:cd03217 84 QYPPEIPGVKNADFL---------------RYVNE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1182 AGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLL-GDRIAIISHGKLKCCGSPLFLKGTYGDGY 1247
Cdd:cd03217 133 SGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1037-1236 |
1.98e-16 |
|
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: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIR--------KNLGMCPQHNVLFD 1108
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGpdgrgrakRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 RLTVEEHLwfysrLKSMAQeEIRREMDKM----------IEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:TIGR03269 379 HRTVLDNL-----TEAIGL-ELPDELARMkavitlkmvgFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1179 EPTAGVDPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1037-1230 |
2.03e-16 |
|
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: 85.95 E-value: 2.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEH 1115
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1116 LWFYSRLKSMAQE--------EIRREMDKMIEDLELSNKRHSlvQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1187
Cdd:TIGR01193 568 LLLGAKENVSQDEiwaaceiaEIKDDIENMPLGYQTELSEEG--SSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47078218 1188 ARRAIWDLILKYKPgRTILLSTHHMDEADLLgDRIAIISHGKL 1230
Cdd:TIGR01193 646 TEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1010-1230 |
3.33e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.85 E-value: 3.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1010 MEEEPTHLPLVVCVDKLTkVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTT---TMSILTGLFPP--TSGSATIYGH 1084
Cdd:COG1117 1 MTAPASTLEPKIEVRNLN-VYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1085 DIRT-EMD--EIRKNLGMCPQH----------NVLFD-RLtveeHlwfysRLKSmaqeeiRREMDKMIEDL--------E 1142
Cdd:COG1117 79 DIYDpDVDvvELRRRVGMVFQKpnpfpksiydNVAYGlRL----H-----GIKS------KSELDEIVEESlrkaalwdE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1143 LSNKRHSLVQTLSGGMKRKLSVAiafvggsRAI------IL-DEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEA 1215
Cdd:COG1117 144 VKDRLKKSALGLSGGQQQRLCIA-------RALavepevLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQA 216
|
250
....*....|....*
gi 47078218 1216 DLLGDRIAIISHGKL 1230
Cdd:COG1117 217 ARVSDYTAFFYLGEL 231
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
2080-2299 |
3.88e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTG----GEAFVNGHSVLKELL 2154
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGkvtvGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 QVQQSLGYCPQC--DALFDElTAREHLQLYTRLRGISwKDEARvvKWALEKLELT----KYADKPAGTYSGGNKRKLSTA 2228
Cdd:PRK13643 81 PVRKKVGVVFQFpeSQLFEE-TVLKDVAFGPQNFGIP-KEKAE--KIAAEKLEMVgladEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2229 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1037-1216 |
3.91e-16 |
|
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: 84.26 E-value: 3.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEH 1115
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1116 LWFYSRLKS--MAQEEIRR-EMDKMIEDLELSnkRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1188
Cdd:TIGR02857 416 IRLARPDASdaEIREALERaGLDEFVAALPQG--LDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|.
gi 47078218 1189 RRAIWDLILKYKPGRTILLSTH---HMDEAD 1216
Cdd:TIGR02857 494 EAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2084-2328 |
4.19e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2084 ENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELLQVQ-Q 2158
Cdd:PRK10070 27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVRrK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2159 SLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2238
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2239 FLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMIT--- 2314
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTffr 266
|
250
....*....|....*
gi 47078218 2315 -VRTKSSQSVKDVVR 2328
Cdd:PRK10070 267 gVDISQVFSAKDIAR 281
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2103-2274 |
4.81e-16 |
|
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: 79.07 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2103 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLY 2182
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2183 TRLRGiswkDEArvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2262
Cdd:cd03231 98 HADHS----DEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|..
gi 47078218 2263 IKTGRSVVLTSH 2274
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1041-1230 |
5.48e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.27 E-value: 5.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1041 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLF-----PPTSGSATIYGHDIRTE-MD--EIRKNLGMCPQHNVLFDRLTV 1112
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPdVDpiEVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1113 EEHLWFYSRLKSMAQEeiRREMDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1184
Cdd:PRK14267 103 YDNVAIGVKLNGLVKS--KKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1185 DPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK14267 181 DPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
1023-1230 |
5.96e-16 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 80.26 E-value: 5.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE------ 1092
Cdd:TIGR02323 6 VSGLSKSYGGGK--GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAElelyQLSEaerrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1093 IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQE---EIRREMDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIAF 1168
Cdd:TIGR02323 84 MRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1169 VGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2109-2274 |
7.14e-16 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 84.51 E-value: 7.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2109 RPGECFGLLGVNGAGKTSTFKMLTGDEstTGGeaFVNGHSVLKELLQVQQSL----GYCPQCDALFDELTAREHLQLYTR 2184
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESLIYSAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2185 LR---GISWKDEARVVKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLW 2256
Cdd:PLN03140 980 LRlpkEVSKEEKMMFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
170
....*....|....*...
gi 47078218 2257 NLILDLIKTGRSVVLTSH 2274
Cdd:PLN03140 1060 RTVRNTVDTGRTVVCTIH 1077
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2078-2303 |
9.13e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 81.30 E-value: 9.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQvQ 2157
Cdd:PRK11432 4 KNFVVLKNITKRF-----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2237
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2238 IFLDEPTTGMDPKARRFLWNLILDLIKtgrSVVLTS----HSMEECEALCTRLAIMVNGRLRCLGSIQHL 2303
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQ---QFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2115-2306 |
9.40e-16 |
|
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: 81.31 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2115 GLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhSVLKE------LLQVQQSLGYCPQCDALFDELTAREHLQL-YTRLRG 2187
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-RTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYgMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2188 iswkdEARVVKWA--LEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARR----FLWNLILD 2261
Cdd:TIGR02142 106 -----SERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYeilpYLERLHAE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47078218 2262 LiktGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNR 2306
Cdd:TIGR02142 181 F---GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2081-2293 |
1.24e-15 |
|
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: 76.65 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQS 2159
Cdd:cd03228 1 IEFKNVSFSYPGRPK---PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDElTAREHLqlytrlrgiswkdearvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIF 2239
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2240 LDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMEECEaLCTRLAIMVNGR 2293
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2080-2311 |
1.43e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIgrILAVDrlcLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKE---- 2152
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA--LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVQREgrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2153 --LLQVQQSLGYCPQCDALFDELTAREHLQL---------YTRLRGISWKDEARVVKwALEKLELTKYADKPAGTYSGGN 2221
Cdd:PRK09984 79 rdIRKSRANTGYIFQQFNLVNRLSVLENVLIgalgstpfwRTCFSWFTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2300
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
250
....*....|..
gi 47078218 2301 QHLKN-RFGDGY 2311
Cdd:PRK09984 238 QQFDNeRFDHLY 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2077-2294 |
1.56e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.26 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2077 DNDMVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVLKE-LL 2154
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEN---NALKNVSFEINEGEYVAILGHNGSGK-STIsKILTGLLKPQSGEIKIDGITISKEnLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 QVQQSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIG 2233
Cdd:PRK13632 80 EIRKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2234 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2294
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKL 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1021-1229 |
1.89e-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: 75.56 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1021 VCVDKLTKVYkDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsatiyghdirtemdeirknlgmc 1100
Cdd:cd03221 1 IELENLSKTY-GGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG----------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 pqhnvlfdrlTVEEHlwfysrlksmaqeeirremdkmiedlelSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:cd03221 56 ----------IVTWG----------------------------STVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1181 TAGVDPYARRAIWDLILKYKpgRTILLSTHhmDEA--DLLGDRIAIISHGK 1229
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1038-1236 |
1.90e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.21 E-value: 1.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---TEMDEIRKNLGMCPQHNVLFDRLTVEE 1114
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVFQQFYLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLWFYS-RLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR---- 1189
Cdd:PRK09493 97 NVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRhevl 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47078218 1190 RAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK09493 177 KVMQDLA---EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2106-2295 |
2.67e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2106 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQ---QSLGYCPQCDALFDELTAREHLQ 2180
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqMDEEARAKlraKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2181 LYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2260
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 47078218 2261 DLIKT-GRSVVLTSHSmEECEALCTRLAIMVNGRLR 2295
Cdd:PRK10584 191 SLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2080-2294 |
3.01e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 3.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKEllqvqq 2158
Cdd:COG3845 5 ALELRGITKRF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrIRS------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2159 slgycPQcDA-------------LFDELTAREHLQLY---TRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNK 2222
Cdd:COG3845 74 -----PR-DAialgigmvhqhfmLVPNLTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2223 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2080-2293 |
3.72e-15 |
|
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: 77.09 E-value: 3.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIG--RILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVN-GHSVL------ 2150
Cdd:COG4778 4 LLEVENLSKTFTLHLQGgkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVdlaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2151 -KELLQV-QQSLGYC-------PQCDALfdELTArEHLqlytRLRGISwKDEARV-VKWALEKLEL-TKYADKPAGTYSG 2219
Cdd:COG4778 84 pREILALrRRTIGYVsqflrviPRVSAL--DVVA-EPL----LERGVD-REEARArARELLARLNLpERLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2220 GNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1038-1230 |
4.49e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 4.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMD----------EIRKN----LGMCP 1101
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDglangivyisEDRKRdglvLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVlfdRLTVEEHLwfysrlkSMAQEEIRREMDKM-IED-LELSN-KRHSLVQT---LSGGMKRKLSVAIAFVGGSRAI 1175
Cdd:PRK10762 348 KENM---SLTALRYF-------SRAGGSLKHADEQQaVSDfIRLFNiKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1176 ILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEadLLG--DRIAIISHGKL 1230
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1038-1230 |
5.10e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.26 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLF-----PPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVLFDRLT 1111
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1112 VEEHLWFYSRLKSMA------QEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK14247 99 IFENVALGLKLNRLVkskkelQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47078218 1186 PYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2080-2294 |
5.99e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.45 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYksrkIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELLQ 2155
Cdd:PRK10908 1 MIRFEHVSKAY----LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2236 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1036-1223 |
6.20e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 6.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1036 LALNKLSLNLYENQVVSFLGHNGAGKTTTMSI---LTGLFPP--TSGSATIYGHDIR-TEMD--EIRKNLGMCPQHNVLF 1107
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYaPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DRlTVEEHLWFYSRLKSMaqeeiRREMDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:PRK14243 104 PK-SIYDNIAYGARINGY-----KGDMDELVERSlrqaalwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47078218 1180 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIA 1223
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2079-2342 |
6.56e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.46 E-value: 6.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2079 DMVKIENLTKVYKSRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQ 2157
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKYTL--NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2236
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2237 FIFLDEPTTGMDPKARrflwnliLDLIKTGRS--------VVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFG 2308
Cdd:PRK13650 161 IIILDEATSMLDPEGR-------LELIKTIKGirddyqmtVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
250 260 270
....*....|....*....|....*....|....
gi 47078218 2309 DGYMITVRTKSSQSVKDVVRFFNRNFPEAMLKER 2342
Cdd:PRK13650 233 DLLQLGLDIPFTTSLVQSLRQNGYDLPEGYLTEK 266
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1034-1236 |
6.97e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 6.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1034 KKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNVLFDRLTVE 1113
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1114 EHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1193
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47078218 1194 DLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK11432 177 EKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1023-1230 |
8.89e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 8.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTkVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKnLGMC 1100
Cdd:COG3845 260 VENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSprERRR-LGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 -----PQHNVLFDRLTVEEHLWF-------YSRLKSMAQEEIRREMDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIA 1167
Cdd:COG3845 337 yipedRLGRGLVPDMSVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDVRTPGpDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1168 FVGGSRAIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1037-1236 |
9.71e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.21 E-value: 9.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDE-----IRKNLGMCPQHNVLFDR 1109
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkaireLRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 LTVEEHLWFYS-RLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1188
Cdd:PRK11124 97 LTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1189 RRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIA------IISHGKLKCCGSP 1236
Cdd:PRK11124 177 TAQIVSIIRELaETGITQVIVTHEVEVARKTASRVVymenghIVEQGDASCFTQP 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1030-1235 |
1.02e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.87 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE--IRKNLGMCPQHNVLF 1107
Cdd:PRK11160 348 YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DRlTVEEHLwfysrlkSMAQEEIRREmdKMIEDLE---LSNkrhsLVQT--------------LSGGMKRKLSVAIAFVG 1170
Cdd:PRK11160 427 SA-TLRDNL-------LLAAPNASDE--ALIEVLQqvgLEK----LLEDdkglnawlgeggrqLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1171 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTH------HMdeadllgDRIAIISHGKLKCCGS 1235
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltgleQF-------DRICVMDNGQIIEQGT 556
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2100-2313 |
1.19e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.81 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKELLQVQQSLGYCPQC--DALFDElT 2174
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdNQLFSA-S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2175 AREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2254
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2255 LWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLknrFGDGYMI 2313
Cdd:PRK13636 180 IMKLLVEMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV---FAEKEML 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1040-1236 |
1.25e-14 |
|
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: 77.84 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1040 KLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-----RKNLGMCPQHNVLFDRLTVEE 1114
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLwFYSRLKSMAQEEIRREmDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD--------P 1186
Cdd:TIGR02142 95 NL-RYGMKRARPSERRISF-ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdprkyeilP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1187 YARRaiwdliLKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:TIGR02142 173 YLER------LHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2104-2275 |
2.46e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2104 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkELLQVQQSLGYCPQCDALFDELTAREHLQLYT 2183
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2184 RLRGiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI 2263
Cdd:PRK13539 99 AFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHL 174
|
170
....*....|..
gi 47078218 2264 KTGRSVVLTSHS 2275
Cdd:PRK13539 175 AQGGIVIAATHI 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2093-2293 |
2.46e-14 |
|
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: 78.33 E-value: 2.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2093 RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVLKELLQVQQSLGYC--PQCDA 2168
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASNIRDTERAGIViiHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2169 LFDELTAREHLQLYTR--LRGISWKDEARVVKWA--LEKLELTKYAD-KPAGTYSGGNKRKLSTAIALIGYPAFIFLDEP 2243
Cdd:TIGR02633 89 LVPELSVAENIFLGNEitLPGGRMAYNAMYLRAKnlLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 2244 TTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2080-2294 |
2.60e-14 |
|
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: 75.61 E-value: 2.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKS----RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---- 2151
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2152 ------ELLQV--QQSLG-YCPQCDAlfdELTAREHLQLYTRLrgiswkDEARVVKWALEKLEL----TKYADKPAGTYS 2218
Cdd:TIGR02769 82 qrrafrRDVQLvfQDSPSaVNPRMTV---RQIIGEPLRHLTSL------DESEQKARIAELLDMvglrSEDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2219 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDpkarRFLWNLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
.
gi 47078218 2294 L 2294
Cdd:TIGR02769 229 I 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2098-2294 |
3.10e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2098 ILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKELLQ-----VQQSLGYCPqcda 2168
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAagvaiIYQELHLVP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2169 lfdELTAREHL---QLYTRLrgiSWKDEARVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDE 2242
Cdd:PRK11288 93 ---EMTVAENLylgQLPHKG---GIVNRRLLNYEAREQLEhlgVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2243 PTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
737-943 |
3.44e-14 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 76.66 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 737 MMPLCMVISWVYSVAMTIQHIVAEKEHRLKEVMKTMGLNNAVHWVAWFITGFVqLSISVTALTAILKYGQVLMHSHVVII 816
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFL-VGLLQLLIILLLLFGIGIPFGNLGLL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 817 WLFLAVYAVATIMFCFLVSVLYSKAKLASACGGIIYFLSYVPYMYVAIREEVAHdkitaFEKCIASLMSTTAFGLGSKYF 896
Cdd:pfam12698 242 LLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPS-----FLQWIFSIIPFFSPIDGLLRL 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47078218 897 ALYEVAgvgiqwhtfsqspvegddFNLLLAVTMLMVDAVVYGILTWY 943
Cdd:pfam12698 317 IYGDSL------------------WEIAPSLIILLLFAVVLLLLALL 345
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2099-2294 |
3.60e-14 |
|
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: 72.73 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2099 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDElTAREH 2178
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2179 LQlyTRLrgiswkdearvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNL 2258
Cdd:cd03247 95 LG--RRF--------------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 47078218 2259 ILDLIKtGRSVVLTSHSMEECEALcTRLAIMVNGRL 2294
Cdd:cd03247 141 IFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1037-1229 |
4.19e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 4.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE--MDEIRKNLGMCPQHNVLFDRLTVEE 1114
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLW----FYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1190
Cdd:PRK10762 99 NIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47078218 1191 AIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:PRK10762 179 SLFRVIRELKSqGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2101-2294 |
4.88e-14 |
|
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: 72.25 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2101 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDElTAREHL 2179
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2180 qlytrlrgiswkdearvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2259
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*
gi 47078218 2260 LDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRL 2294
Cdd:cd03246 140 AALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2058-2294 |
4.95e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 4.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2058 VEDDVDVASERQRVLRGDAdndMVKIENLTkVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDEST 2137
Cdd:COG3845 238 VGREVLLRVEKAPAEPGEV---VLEVENLS-VRDDRGV---PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2138 TGGEAFVNGHSVL----KELLQvqQSLGYCP---QCDALFDELTAREHLQL-------YTRLRGISWKdeaRVVKWALEK 2203
Cdd:COG3845 311 ASGSIRLDGEDITglspRERRR--LGVAYIPedrLGRGLVPDMSVAENLILgryrrppFSRGGFLDRK---AIRAFAEEL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2204 LEltKY------ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2277
Cdd:COG3845 386 IE--EFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLD 463
|
250
....*....|....*..
gi 47078218 2278 ECEALCTRLAIMVNGRL 2294
Cdd:COG3845 464 EILALSDRIAVMYEGRI 480
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1031-1211 |
5.39e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1031 KDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRL 1110
Cdd:PRK13538 11 RDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 TVEEHLWFYSRLKSMAQEeirremDKMIEDLE---LSNKRHSLVQTLSGGMKRKlsVAIA--FVGGSRAIILDEP----- 1180
Cdd:PRK13538 90 TALENLRFYQRLHGPGDD------EALWEALAqvgLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPftaid 161
|
170 180 190
....*....|....*....|....*....|.
gi 47078218 1181 TAGVDPYARRaiwdLILKYKPGRTILLSTHH 1211
Cdd:PRK13538 162 KQGVARLEAL----LAQHAEQGGMVILTTHQ 188
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2081-2307 |
6.45e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.14 E-value: 6.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---ELLQVQ 2157
Cdd:PRK09452 15 VELRGISKSFDGKEV-----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 ---QSlgYcpqcdALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:PRK09452 90 tvfQS--Y-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRF 2307
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1014-1230 |
7.19e-14 |
|
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: 73.27 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1014 PTHLPLVVCVDKLTKVYKD-DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMD 1091
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1092 EIRKNLGMCPQHNVLFDRlTVEEHLWFysRLKSMAQEEIRREMDK-----MIEDLEL-----SNKRHSLvqtLSGGMKRK 1161
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAY--GLQSCSFECVKEAAQKahahsFISELASgydteVGEKGSQ---LSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1162 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1230
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
2106-2300 |
8.80e-14 |
|
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: 73.27 E-value: 8.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2106 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---ELLQVQQSLgycpqcdALFDELTAREHLQLY 2182
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNY-------SLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2183 TR--LRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2260
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 47078218 2261 DLIKTGR-SVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2300
Cdd:TIGR01184 159 QIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2081-2274 |
8.84e-14 |
|
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: 70.56 E-value: 8.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIGRILAvdrlcLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEafVNGHSVLKellqvqqsL 2160
Cdd:cd03221 1 IELENLSKTYGGKLLLKDIS-----LTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--VTWGSTVK--------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQcdalfdeltarehlqlytrlrgiswkdearvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:cd03221 66 GYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....
gi 47078218 2241 DEPTTGMDPKARRFLWNLildLIKTGRSVVLTSH 2274
Cdd:cd03221 95 DEPTNHLDLESIEALEEA---LKEYPGTVILVSH 125
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1023-1231 |
9.29e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 9.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYkDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATiyghdirtemdeIRKNL--GMC 1100
Cdd:COG0488 1 LENLSKSF-GGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS------------IPKGLriGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNVLFDRLTVEEHLW--FYSRLKSMAQ-EEIRREMDKMIEDL----ELSNK--------------------------R 1147
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgDAELRALEAElEELEAKLAEPDEDLerlaELQEEfealggweaearaeeilsglgfpeedL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1148 HSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRaiW--DLILKYkPGrTILLSTH--H-MDEadlLGDRI 1222
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNY-PG-TVLVVSHdrYfLDR---VATRI 219
|
....*....
gi 47078218 1223 AIISHGKLK 1231
Cdd:COG0488 220 LELDRGKLT 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2111-2305 |
9.58e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 9.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2111 GECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKELLQVQQSLGYCPQCDALFDELTAREHL-QLY 2182
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNLiEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2183 TRLRGISwKDEARV-VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2261
Cdd:PRK11124 108 CRVLGLS-KDQALArAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47078218 2262 LIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2305
Cdd:PRK11124 187 LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1037-1230 |
9.61e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 9.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCPQHNVLFDRLTVEE 1114
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLW---FYSRL----KSMAQEEIRREMDKMIEDLELSNKrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDpy 1187
Cdd:PRK11288 99 NLYlgqLPHKGgivnRRLLNYEAREQLEHLGVDIDPDTP----LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 47078218 1188 AR------RAIWDLilkYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK11288 173 AReieqlfRVIREL---RAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2080-2293 |
1.01e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKE----- 2152
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2153 -LLQVQQ--SLGYCPqcdalfdELTAREHLQL-YTR--LRGISW---KDEARVVKWALEKLE--LTKYADKPAGTYSGGN 2221
Cdd:COG1101 81 yIGRVFQdpMMGTAP-------SMTIEENLALaYRRgkRRGLRRgltKKRRELFRELLATLGlgLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRsvvLTS----HSMEECEALCTRLAIMVNGR 2293
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEGR 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2075-2303 |
1.19e-13 |
|
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: 76.34 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2075 DADNDMVKIENLTKVYKSRKigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKELL 2154
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGR----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD-LSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 --QVQQSLGYCPQCDALFdELTAREHLQLYTRlrGISwkDEArvVKWALEKLELTKYADK-PAG----------TYSGGN 2221
Cdd:COG4988 406 paSWRRQIAWVPQNPYLF-AGTIRENLRLGRP--DAS--DEE--LEAALEAAGLDEFVAAlPDGldtplgeggrGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQ 2301
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHE 556
|
..
gi 47078218 2302 HL 2303
Cdd:COG4988 557 EL 558
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2116-2303 |
1.20e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.68 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2116 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQQSLGYCPQC--DALFDElTAREHLQLYTRLRGISWKD 2192
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVGLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2193 EARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVL 2271
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIF 193
|
170 180 190
....*....|....*....|....*....|..
gi 47078218 2272 TSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2303
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2110-2294 |
1.90e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2110 PGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKELLQVQQSLGYCPQCDALFDELTAREHL-QL 2181
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVFQQYNLWPHLTVMENLiEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2182 YTRLRGISwKDEARV-VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2260
Cdd:COG4161 107 PCKVLGLS-KEQAREkAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIR 185
|
170 180 190
....*....|....*....|....*....|....
gi 47078218 2261 DLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:COG4161 186 ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2106-2294 |
1.93e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2106 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG-----HSVLKELLQVQQSLGYCPQC--DALFDElTAREH 2178
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitsTSKNKDIKQIRKKVGLVFQFpeSQLFEE-TVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2179 LQLYTRLRGISwKDEArvVKWALEKLELTKYA----DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2254
Cdd:PRK13649 107 VAFGPQNFGVS-QEEA--EALAREKLALVGISeslfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47078218 2255 LWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2090-2302 |
2.23e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2090 YKSRKIGRI-LAVDRL---------CLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--KELLQVQ 2157
Cdd:PRK11288 248 YRPRPLGEVrLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDAIR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQcDALFDELTA----REHLQLYTR---LRG---ISWKDEARVVKWALEKLEL-TKYADKPAGTYSGGNKRK-- 2224
Cdd:PRK11288 328 AGIMLCPE-DRKAEGIIPvhsvADNINISARrhhLRAgclINNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKai 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2225 ----LSTAIALIgypafiFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRclGSI 2300
Cdd:PRK11288 407 lgrwLSEDMKVI------LLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GEL 478
|
..
gi 47078218 2301 QH 2302
Cdd:PRK11288 479 AR 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2075-2295 |
2.27e-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: 75.25 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2075 DADNDMVKIENLTKVY-KSRKIGRilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTGGEAFVNGHSV-LK 2151
Cdd:TIGR02633 252 EIGDVILEARNLTCWDvINPHRKR---VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2152 ELLQ-VQQSLGYCPQ---CDALFDELTAREH-----LQLYTRLRGISWKDEARVVKWALEKLEL-TKYADKPAGTYSGGN 2221
Cdd:TIGR02633 329 NPAQaIRAGIAMVPEdrkRHGIVPILGVGKNitlsvLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2295
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1041-1236 |
2.35e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1041 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMCPQHNVLFDRLTVEEHL 1116
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1117 WFYSRLKSMAQEEIRREMDKM-IEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1195
Cdd:PRK11831 106 AYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47078218 1196 I--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK11831 186 IseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2080-2301 |
2.59e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.50 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKEL--LQVQ 2157
Cdd:PRK13548 2 MLEARNLSV-----RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWspAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDAL-FDeLTARE--HLQLYTrlRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI-- 2232
Cdd:PRK13548 76 RRRAVLPQHSSLsFP-FTVEEvvAMGRAP--HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2233 ----GYPAFIFLDEPTTGMDPK--------ARRFLWnlildliKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2300
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAhqhhvlrlARQLAH-------ERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
.
gi 47078218 2301 Q 2301
Cdd:PRK13548 226 A 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1049-1210 |
2.72e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1049 QVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE-----IR-KNLGMCPQHNVLFDRLTVEEHLWFYSRL 1122
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-HQMDEearakLRaKHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1123 KSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYK 1200
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNRE 195
|
170
....*....|
gi 47078218 1201 PGRTILLSTH 1210
Cdd:PRK10584 196 HGTTLILVTH 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1023-1230 |
3.03e-13 |
|
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: 72.15 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVY-------KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMD 1091
Cdd:TIGR02769 5 VRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1092 EIRKNLGMCPQ--HNVLFDRLTVE----EHLWFYSRLKSMAQEEIRREMDKMIE-DLELSNKrhsLVQTLSGGMKRKLSV 1164
Cdd:TIGR02769 85 AFRRDVQLVFQdsPSAVNPRMTVRqiigEPLRHLTSLDESEQKARIAELLDMVGlRSEDADK---LPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1165 AIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1030-1223 |
3.33e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 3.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTS-----GSATIYGHDI---RTEMDEIRKNLGMC- 1100
Cdd:PRK14258 16 YYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLNRLRRQVSMVh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQHNvLFDrLTVEEHLWFYSRLKSMAQeeiRREMDKMIE------DL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1172
Cdd:PRK14258 95 PKPN-LFP-MSVYDNVAYGVKIVGWRP---KLEIDDIVEsalkdaDLwdEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1173 RAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIA 1223
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1023-1249 |
3.82e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 3.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1101
Cdd:PRK11176 344 FRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRlTVEEHLwFYSRLKSMAQEEIRREMdKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSR 1173
Cdd:PRK11176 424 QNVHLFND-TIANNI-AYARTEQYSREQIEEAA-RMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1174 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP---LFLKGTYGDGYRL 1249
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGTHaelLAQNGVYAQLHKM 578
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1038-1236 |
4.31e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGMCPQHNVL---FD-RLTV 1112
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDTSLsfeFDvRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1113 E----EHLwfySRLKSMAQEEiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDpyA 1188
Cdd:PRK09536 99 EmgrtPHR---SRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1189 RRAIWDLILKYK---PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK09536 173 NHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2080-2281 |
4.71e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.59 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDES---TTGGEAFVNGHSVLKelLQV 2156
Cdd:COG4136 1 MLSLENLTITLGGRPL-----LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTA--LPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 QQ-SLGYCPQCDALFDELTAREHLQLYTRlRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:COG4136 74 EQrRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 2236 AFIFLDEPTTGMDP----KARRFLWNLILDLiktGRSVVLTSHSMEECEA 2281
Cdd:COG4136 153 RALLLDEPFSKLDAalraQFREFVFEQIRQR---GIPALLVTHDEEDAPA 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1031-1230 |
5.75e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1031 KDDKKLalNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQH---NV 1105
Cdd:PRK09700 274 RDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrdNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTVEEHLWFYSRLKS---------MAQEEIRREMDKMIEDLELsnKRHSLVQT---LSGGMKRKLSVAIAFVGGSR 1173
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELLAL--KCHSVNQNiteLSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1174 AIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2068-2294 |
6.72e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2068 RQRVLRGDADNDMVKIENLTkvykSRKIGRilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH 2147
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT----SRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2148 --SVLKELLQVQQSLGYCPQC---DALFDELTAREHLQLYTRLRGISWK---------DEARVVKWALEKLELTKYA-DK 2212
Cdd:PRK09700 326 diSPRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKDGGYKgamglfhevDEQRTAENQRELLALKCHSvNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2213 PAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2292
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
..
gi 47078218 2293 RL 2294
Cdd:PRK09700 486 RL 487
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1026-1229 |
6.90e-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: 73.71 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIY--GHDIRTE--MDEIRKNLGMCP 1101
Cdd:TIGR02633 7 IVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLKASniRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRLTVEEHLWFYSRL----KSMAQEEIRREMDKMIEDLELSNKRHSL-VQTLSGGMKRKLSVAIAFVGGSRAII 1176
Cdd:TIGR02633 85 QELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1177 LDEPTAGVDPYARRAIWDLI--LKYKPGRTILLStHHMDEADLLGDRIAIISHGK 1229
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIrdLKAHGVACVYIS-HKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1023-1267 |
7.69e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKkLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1101
Cdd:PRK10790 343 IDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNV-----LFDRLTV-----EEHLWfySRLKSMAQEEIRREMDKMIEDL--ELSNkrhslvqTLSGGMKRKLSVAIAFV 1169
Cdd:PRK10790 422 QDPVvladtFLANVTLgrdisEEQVW--QALETVQLAELARSLPDGLYTPlgEQGN-------NLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1170 GGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP---LFLKGTY 1243
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHqqlLAAQGRY 568
|
250 260
....*....|....*....|....
gi 47078218 1244 GDGYRLTLVKRPAEPGGPQEPGLA 1267
Cdd:PRK10790 569 WQMYQLQLAGEELAASVREEESLS 592
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
2104-2277 |
9.04e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.19 E-value: 9.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2104 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKELLQVQQSLGYC---PQCDALFDELTARE 2177
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2178 HLQLytRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2257
Cdd:PRK13638 100 AFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180
....*....|....*....|
gi 47078218 2258 LILDLIKTGRSVVLTSHSME 2277
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDID 197
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1026-1239 |
9.64e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKDDKKLALNK-LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatIYGHDIRteMDEI---RKNLGMCP 1101
Cdd:PRK11000 6 LRNVTKAYGDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD--LFIGEKR--MNDVppaERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1182 AGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1239
Cdd:PRK11000 162 SNLDAALRVQMRIEIsrLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1018-1219 |
1.17e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1018 PLVVCvDKLTKVYKDDKKLA--LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMD 1091
Cdd:PRK11629 4 ILLQC-DNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1092 EIRKN-LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVG 1170
Cdd:PRK11629 83 ELRNQkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1171 GSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLG 1219
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2096-2294 |
1.28e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2096 GRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-----DESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDAL 2169
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2170 FDELTAREHLQLYTRLRGI--SWKDEARVVKWALEKLEL----TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEP 2243
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2244 TTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2111-2292 |
1.29e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2111 GECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELlqvQQSL-GYCPQ---CDALFDELTarEHLQLYTRLR 2186
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAYVPQseeVDWSFPVLV--EDVVMMGRYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2187 GISW-----KDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2261
Cdd:PRK15056 108 HMGWlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
170 180 190
....*....|....*....|....*....|.
gi 47078218 2262 LIKTGRSVVLTSHSMEECEALCTrLAIMVNG 2292
Cdd:PRK15056 188 LRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2078-2306 |
1.42e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ-V 2156
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGT----KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 QQSLGYCPQC--DALFdELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:PRK13647 78 RSKVGLVFQDpdDQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNR 2306
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
985-1231 |
1.44e-12 |
|
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: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 985 TPRLSVMEEDQACAMESRRfEETRGMEEEPTHLPLVVC-VDKLTKVYKDDKKLA-LNKLSLNLYENQVVSFLGHNGAGKT 1062
Cdd:TIGR02633 222 TKDMSTMSEDDIITMMVGR-EITSLYPHEPHEIGDVILeARNLTCWDVINPHRKrVDDVSFSLRRGEILGVAGLVGAGRT 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1063 TTMSILTGLFPPT-SGSATIYGH--DIRTEMDEIRKNLGMCPQ--------------HNVlfdRLTVEEHLWFYSRLKSM 1125
Cdd:TIGR02633 301 ELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrhgivpilgvgKNI---TLSVLKSFCFKMRIDAA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1126 AQEEIrreMDKMIEDLELSNKRHSL-VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGR 1203
Cdd:TIGR02633 378 AELQI---IGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGV 454
|
250 260
....*....|....*....|....*...
gi 47078218 1204 TILLSTHHMDEADLLGDRIAIISHGKLK 1231
Cdd:TIGR02633 455 AIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1036-1230 |
1.96e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1036 LALNKLSLnLYENQVVSF------------LGHNGAGKTTTMSILTGLFPPTSGSATIYGHDiRTEMDEIRKNLGMCPQH 1103
Cdd:PRK10771 2 LKLTDITW-LYHHLPMRFdltvergervaiLGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 NVLFDRLTVEEH--LWFYSRLKSMAQEeiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:PRK10771 80 NNLFSHLTVAQNigLGLNPGLKLNAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1182 AGVDPYARRAIWDLILKYKPGR--TILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1012-1230 |
2.92e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1012 EEPTHL----PLVVcvDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsATIYGhdiR 1087
Cdd:PRK11247 2 MNTARLnqgtPLLL--NAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---T 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1088 TEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFysRLKSMAQEEIRREMdkmiEDLELSNKRHSLVQTLSGGMKRKLSVAIA 1167
Cdd:PRK11247 74 APLAEAREDTRLMFQDARLLPWKKVIDNVGL--GLKGQWRDAALQAL----AAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1168 FVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2113-2294 |
3.37e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.10 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2113 CFGLLGVNGAGKTS---TFKMLT--GDESTTGGEAFVNGHSVLKE---LLQVQQSLGYCPQCDALFDELTAREHLQLYTR 2184
Cdd:PRK14267 32 VFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSPdvdPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2185 LRGI--SWKDEARVVKWALEKLEL-----TKYADKPaGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2257
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 47078218 2258 LILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK14267 191 LLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1021-1212 |
3.47e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1021 VCVDKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMdeiRKNL-GM 1099
Cdd:PRK15056 7 IVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1100 CPQ-HNVLFDRLTVEEHLWFYSRLKSM-----AQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSR 1173
Cdd:PRK15056 83 VPQsEEVDWSFPVLVEDVVMMGRYGHMgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47078218 1174 AIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHM 1212
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNL 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2078-2294 |
4.24e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKELLQVQ 2157
Cdd:PRK11614 3 KVMLSFDKVSAHY-----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDITDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 ------QSLGYCPQCDALFDELTAREHLQLytrlrGISWKDEARV---VKWALEKL-ELTKYADKPAGTYSGGNKRKLST 2227
Cdd:PRK11614 74 takimrEAVAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFqerIKWVYELFpRLHERRIQRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2228 AIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2110-2274 |
4.34e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2110 PGECFGLLGVNGAGKTSTFKMLTGDESTTG--GEAFVNGHSVLKellQVQQSLGYCPQCDALFDELTAREHLQLYTRLR- 2186
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVFCSLLRl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2187 --GISWKDEARVVKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2259
Cdd:PLN03211 170 pkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*
gi 47078218 2260 LDLIKTGRSVVLTSH 2274
Cdd:PLN03211 250 GSLAQKGKTIVTSMH 264
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1023-1230 |
4.84e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.62 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE---------MDEI 1093
Cdd:PRK11264 6 VKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1094 RKNLGMCPQHNVLFDRLTVEEHLWFYSRL-KSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1172
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1173 RAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
1041-1236 |
4.84e-12 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 68.16 E-value: 4.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1041 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP----TSGSATIYGHDIrTEMDEIRKNLGMCPQH-----NVLFdrlT 1111
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL-LPLSIRGRHIATIMQNprtafNPLF---T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1112 VEEH----LWFYSRLKSMAQEEIRREMDKM-IEDLELSNKRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1186
Cdd:TIGR02770 81 MGNHaietLRSLGKLSKQARALILEALEAVgLPDPEEVLKKYPF--QLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1187 YARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:TIGR02770 159 VNQARVLKLLreLRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1006-1234 |
5.17e-12 |
|
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: 71.32 E-value: 5.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1006 ETRGMEEEPTHLP-----LVVcvDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAT 1080
Cdd:COG4618 313 AAVPAEPERMPLPrpkgrLSV--ENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1081 IYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHLwfySRLKSMAQEEI-----RREMDKMIedLELSNKRHSLV--- 1151
Cdd:COG4618 391 LDGADLSQwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDADPEKVvaaakLAGVHEMI--LRLPDGYDTRIgeg 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1152 -QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMdeaDLLG--DRIAIIS 1226
Cdd:COG4618 465 gARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIraLKAR-GATVVVITHRP---SLLAavDKLLVLR 540
|
....*...
gi 47078218 1227 HGKLKCCG 1234
Cdd:COG4618 541 DGRVQAFG 548
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2100-2275 |
7.74e-12 |
|
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: 70.47 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDElTAREH 2178
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2179 LQLytrLRGISWKDEARvvkWALEKLELTKY-ADKPAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2247
Cdd:TIGR02868 429 LRL---ARPDATDEELW---AALERVGLADWlRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*...
gi 47078218 2248 DPKARRFLWNLILDlIKTGRSVVLTSHS 2275
Cdd:TIGR02868 503 DAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2101-2294 |
8.15e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 8.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2101 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ--VQQSLGYCPQ---CDALFDELTA 2175
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdgLANGIVYISEdrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2176 REHLQLyTRLRGISWKdeARVVKWALEKLELTKY----------ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2245
Cdd:PRK10762 348 KENMSL-TALRYFSRA--GGSLKHADEQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 47078218 2246 GMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1032-1230 |
8.61e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 8.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1032 DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1110
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 TVEEHLwfysRL-KSMAQEEIRREMDKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:PRK13657 424 SIEDNI----RVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgergrqLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1182 AGVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKL 1230
Cdd:PRK13657 500 SALDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNGRV 547
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1041-1230 |
9.13e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 9.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1041 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC------PQHNVLFDR----- 1109
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 ---LTVEEHLWFYSRLKSMAQ-EEIRREMDKMIEDLELSnkrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK15439 362 vcaLTHNRRGFWIKPARENAVlERYRRALNIKFNHAEQA------ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1186 PYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK15439 436 VSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1023-1236 |
9.83e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.69 E-value: 9.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDE---------- 1092
Cdd:PRK10619 8 VIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1093 ----IRKNLGMCPQHNVLFDRLTVEEHLW-----FYSRLKSMAQEEIRREMDKMIEDlELSNKRHSLvqTLSGGMKRKLS 1163
Cdd:PRK10619 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMeapiqVLGLSKQEARERAVKYLAKVGID-ERAQGKYPV--HLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 1164 VAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2081-2302 |
1.04e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.32 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL-----KELLQ 2155
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYCPQC--DALFDElTAREHLQLYTRLRGISwKDEAR--VVKWaLEKLEL-TKYADKPAGTYSGGNKRKLSTAIA 2230
Cdd:PRK13641 83 LRKKVSLVFQFpeAQLFEN-TVLKDVEFGPKNFGFS-EDEAKekALKW-LKKVGLsEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2231 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLrclgsIQH 2302
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL-----IKH 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2081-2301 |
1.17e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKELLQVQQSL 2160
Cdd:PRK10851 3 IEIANIKKSF-----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQ-----LYTRLRGISWKDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAfgltvLPRRERPNAAAIKAKVTQ-LLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2236 AFIFLDEPTTGMDPKA----RRFLWNLILDLIKTGrsvVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2301
Cdd:PRK10851 156 QILLLDEPFGALDAQVrkelRRWLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1038-1230 |
1.23e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLG--MCPQHNVLFDRLTVEEH 1115
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiyLVPQEPLLFPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1116 LWF--------YSRLKSMAQE-EIRREMDKMIEDLELSNKRhsLVQTLSGGMKRklsvaiafvggSRAIILDEPTAGVDP 1186
Cdd:PRK15439 107 ILFglpkrqasMQKMKQLLAAlGCQLDLDSSAGSLEVADRQ--IVEILRGLMRD-----------SRILILDEPTASLTP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47078218 1187 YARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK15439 174 AETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1030-1228 |
1.51e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-RKNLGMCPQHNVLFD 1108
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 RlTVEEHLWFYSRLKsmaqeEIRREMDKMIEDL-------ELSNKRhslVQTLSGGMKRKLSVA--IAFVggSRAIILDE 1179
Cdd:PRK10247 95 D-TVYDNLIFPWQIR-----NQQPDPAIFLDDLerfalpdTILTKN---IAELSGGEKQRISLIrnLQFM--PKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1180 PTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1228
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1032-1228 |
1.52e-11 |
|
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: 66.30 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1032 DDKKL-ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSaTIYGHDIRT---------EMDEIRKN-LGMC 1100
Cdd:COG4778 20 GGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS-ILVRHDGGWvdlaqasprEILALRRRtIGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1101 PQH-NVLfDRLT----VEEHLwfysRLKSMAQEEIRREMDKMIEDLELSNKRHSLV-QTLSGGMKRKLSVAIAFVGGSRA 1174
Cdd:COG4778 99 SQFlRVI-PRVSaldvVAEPL----LERGVDREEARARARELLARLNLPERLWDLPpATFSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1175 IILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHG 1228
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKArGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2080-2299 |
1.60e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.32 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQ 2157
Cdd:PRK13644 1 MIRLENVSYSYPDGTP----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2236
Cdd:PRK13644 77 KLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2237 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGS 2299
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1030-1211 |
1.97e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDR 1109
Cdd:PRK13540 11 YHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 LTVEEHLWFYSRLKSMAQeeirrEMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1189
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAV-----GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|...
gi 47078218 1190 RAIWDLILKY-KPGRTILLSTHH 1211
Cdd:PRK13540 164 LTIITKIQEHrAKGGAVLLTSHQ 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2114-2313 |
2.45e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2114 FGLLGVNGAGKTSTFKMLT------GDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDELTAREHLQLYTRLR 2186
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2187 GISWKDE-ARVVKWALEKLELTKYA----DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2261
Cdd:PRK14246 119 GIKEKREiKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2262 LiKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRFGDGYMI 2313
Cdd:PRK14246 199 L-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1049-1211 |
2.50e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 2.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1049 QVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDiRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRL---KSM 1125
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1126 AQEEIRREMDKMIEDLELSNKRH-----SLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY-ARRAIWDLILKY 1199
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATaAYRLVLTLGSLA 253
|
170
....*....|..
gi 47078218 1200 KPGRTILLSTHH 1211
Cdd:PLN03211 254 QKGKTIVTSMHQ 265
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1024-1236 |
2.86e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 2.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1024 DKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQ 1102
Cdd:PRK10253 11 EQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEE--------HLWFYSRLKSMAQEEIRREMDKM-IEDLELSNkrhslVQTLSGGMKRKLSVAIAFVGGSR 1173
Cdd:PRK10253 89 NATTPGDITVQElvargrypHQPLFTRWRKEDEEAVTKAMQATgITHLADQS-----VDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1174 AIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1018-1229 |
3.10e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 3.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1018 PLVVcVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE- 1092
Cdd:PRK11701 5 PLLS-VRGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLrdlyALSEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1093 -----IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLksMAQ-----EEIRREMDKMIEDLELSNKR-HSLVQTLSGGMKRK 1161
Cdd:PRK11701 82 errrlLRTEWGFVHQHPRDGLRMQVSAGGNIGERL--MAVgarhyGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1162 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1034-1230 |
3.41e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1034 KKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMDE--IRKNLGMCPQHNVLFDRlT 1111
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHhyLHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1112 VEEHLWFysRLKSMAQEEIRREMDKMIED---LELSNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1184
Cdd:TIGR00958 571 VRENIAY--GLTDTPDEEIMAAAKAANAHdfiMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1185 DPYARRAIWDliLKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1230
Cdd:TIGR00958 649 DAECEQLLQE--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSV 691
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1030-1218 |
3.66e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL-----TGLFppTSGSATIYGHDIRTEMDEIrknLGMCPQHN 1104
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRS---IGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1105 VLFDRLTVEEHLWFYSRL---KSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGM----KRKLSVAIAFVGGSRAII- 1176
Cdd:TIGR00956 846 LHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47078218 1177 LDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHH-----MDEADLL 1218
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQpsailFEEFDRL 973
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2077-2294 |
4.15e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.80 E-value: 4.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2077 DNDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFK----MLTGDESTTGGEAFVNGHSVLKE 2152
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2153 llqvQQSLGYCPQCDALFDELTAR-------EHLQLY--TRLRGISW--------KDEAR-VVKWALEKLEL-TKYADKP 2213
Cdd:PRK13631 98 ----ELITNPYSKKIKNFKELRRRvsmvfqfPEYQLFkdTIEKDIMFgpvalgvkKSEAKkLAKFYLNKMGLdDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2214 AGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
.
gi 47078218 2294 L 2294
Cdd:PRK13631 254 I 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2082-2295 |
4.46e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLT---KVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGdeSTTG---GEAFVNGHSV-LKELL 2154
Cdd:PRK13549 261 EVRNLTawdPVNPHIKR-----VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGrweGEIFIDGKPVkIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2155 Q-VQQSLGYCPQ---CDALFDELTAREHLQL--YTRLRGISWKDEARVVKWALE---KLEL-TKYADKPAGTYSGGNKRK 2224
Cdd:PRK13549 334 QaIAQGIAMVPEdrkRDGIVPVMGVGKNITLaaLDRFTGGSRIDDAAELKTILEsiqRLKVkTASPELAIARLSGGNQQK 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2225 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2295
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2078-2300 |
4.73e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.61 E-value: 4.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTK---VYKSRKiGRI-------------LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2141
Cdd:PRK13546 2 NVSVNIKNVTKeyrIYRTNK-ERMkdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2142 AFVNGhsvlkELLQVQQSLGycpqcdaLFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGN 2221
Cdd:PRK13546 81 VDRNG-----EVSVIAISAG-------LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2300
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1037-1229 |
5.66e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQHNVLFDRLTVEE 1114
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLWF--YSrLKSM--AQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1190
Cdd:PRK10982 93 NMWLgrYP-TKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47078218 1191 AIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1229
Cdd:PRK10982 172 HLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2099-2291 |
6.36e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2099 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ-VQQSLGYCPQC-DALFDELTAR 2176
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVFQNpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2177 EHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLW 2256
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190
....*....|....*....|....*....|....*
gi 47078218 2257 NLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVN 2291
Cdd:PRK13648 183 DLVRKV-KSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2078-2294 |
7.23e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.42 E-value: 7.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVnGHSVLKE--LLQ 2155
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT---YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEetVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:PRK13635 79 VRRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2294
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEI 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2108-2248 |
7.70e-11 |
|
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: 63.82 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTG---GEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLYTR 2184
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2185 LRGiswKDEARVVkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEPTTGMD 2248
Cdd:cd03233 110 CKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1023-1236 |
8.53e-11 |
|
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: 63.97 E-value: 8.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1101
Cdd:cd03369 9 VENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRlTVEEHLWFYSRlksMAQEEIRremdkmiEDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:cd03369 89 QDPTLFSG-TIRSNLDPFDE---YSDEEIY-------GALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1182 AGVDPYARRAIWDLILKYKPGRTILLSTHHMDE-ADLlgDRIAIISHGKLKCCGSP 1236
Cdd:cd03369 154 ASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVKEYDHP 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2085-2293 |
8.98e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 8.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2085 NLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGhsvlkELLQVQ----- 2157
Cdd:PRK13549 10 NITK-----TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEG-----EELQASnirdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 ---------QSLgycpqcdALFDELTAREHLQL---YTRLRGISW-KDEARVVKWaLEKLELTKYADKPAGTYSGGNKRK 2224
Cdd:PRK13549 80 eragiaiihQEL-------ALVKELSVLENIFLgneITPGGIMDYdAMYLRAQKL-LAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2225 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1038-1230 |
8.99e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.44 E-value: 8.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEI----RKNLGMCPQHNVLFDRLTV 1112
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaqlrREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1113 EEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1192
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47078218 1193 WDlILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1230
Cdd:PRK10535 184 MA-ILHQlrDRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2081-2346 |
9.46e-11 |
|
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: 67.13 E-value: 9.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE---LLQVQ 2157
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFT-----IEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEkcgYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGY-CPQC---------------DALFDELTAREHLQLYtrlRGISWKDEARVVKWALEKLELTKYADKP-------- 2213
Cdd:TIGR03269 76 SKVGEpCPVCggtlepeevdfwnlsDKLRRRIRKRIAIMLQ---RTFALYGDDTVLDNVLEALEEIGYEGKEavgravdl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2214 -------------AGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEEC 2279
Cdd:TIGR03269 153 iemvqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2280 EALCTRLAIMVNGRLRCLGSIQHLKNRFgdgymitvrtksSQSVKDVVRFFNRNFPEAMLKERHHTK 2346
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVAVF------------MEGVSEVEKECEVEVGEPIIKVRNVSK 287
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1037-1229 |
9.96e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 9.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIY-------GHDIR-TEmdeiRKNLGMCPQHNVLFD 1108
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfegeelqASNIRdTE----RAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 RLTVEEHLWF---YSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK13549 96 ELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1186 PYARRAIWDLI--LKYKPGRTILLStHHMDEADLLGDRIAIISHGK 1229
Cdd:PRK13549 176 ESETAVLLDIIrdLKAHGIACIYIS-HKLNEVKAISDTICVIRDGR 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2100-2292 |
1.04e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKELLQVQQS-LGYCPQCDALFDELTARE 2177
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtFNGPKSSQEAgIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2178 HLQL----YTRLRGISWK---DEARVVkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2250
Cdd:PRK10762 99 NIFLgrefVNRFGRIDWKkmyAEADKL---LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 47078218 2251 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2292
Cdd:PRK10762 176 ETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2116-2274 |
1.56e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2116 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREH--LQLYTRLRGISWKDE 2193
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENclYDIHFSPGAVGITEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2194 ARVVKwalekleLTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTS 2273
Cdd:PRK13540 112 CRLFS-------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTS 184
|
.
gi 47078218 2274 H 2274
Cdd:PRK13540 185 H 185
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1026-1185 |
1.75e-10 |
|
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: 62.67 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1026 LTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT---SGSATIYGHDIRTEMDEIRKNLGMCPQ 1102
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 HNVLFDRLTVEEHLWFYSRLKSmaqeeirremdkmiedlelsnkrHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
...
gi 47078218 1183 GVD 1185
Cdd:cd03233 148 GLD 150
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2048-2298 |
1.87e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2048 PQRMPVSTKPVEDDVDVASERQRVLRGDAdndMVKIENLTKVYKSR-----KIGR-ILAVDRLCLGVRPGECFGLLGVNG 2121
Cdd:PRK10261 284 PRRFPLISLEHPAKQEPPIEQDTVVDGEP---ILQVRNLVTRFPLRsgllnRVTReVHAVEKVSFDLWPGETLSLVGESG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2122 AGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKEL--------------LQVQQSLGYcpqcdalfdelTAREHLQ 2180
Cdd:PRK10261 361 SGKSTTGRALLRLVESQGGEIIFNGQRIdtlspgkLQALrrdiqfifqdpyasLDPRQTVGD-----------SIMEPLR 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2181 LYTRLRGiswKDEARVVKWALEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2259
Cdd:PRK10261 430 VHGLLPG---KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 47078218 2260 LDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2298
Cdd:PRK10261 507 LDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2082-2293 |
1.87e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEA-FVNGHSVLKELLQVQQS- 2159
Cdd:PRK11701 8 SVRGLTKLY-----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 --------LGYCPQ--CDALFDELTAREHLQlyTRLRGISWKDEARV----VKWaLEKLEL--TKYADKPAgTYSGGNKR 2223
Cdd:PRK11701 83 rrrllrteWGFVHQhpRDGLRMQVSAGGNIG--ERLMAVGARHYGDIrataGDW-LERVEIdaARIDDLPT-TFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMD--PKARrflwnlILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDvsVQAR------LLDLLRGlvrelGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2083-2299 |
1.90e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2083 IENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV------LKELLQV 2156
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 QQSLGYCPQCD--ALFDELTARE------HLQlytrlrgiswKDEARVVKWALEKLELTK----YADKPAGTYSGGNKRK 2224
Cdd:PRK13645 89 RKEIGLVFQFPeyQLFQETIEKDiafgpvNLG----------ENKQEAYKKVPELLKLVQlpedYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2225 LSTA--IALIGYPafIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:PRK13645 159 VALAgiIAMDGNT--LVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1038-1239 |
1.92e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 1.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRLTVEE-- 1114
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRElv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 ----HLWfYSRLKSMAQEEiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1190
Cdd:PRK10575 107 aigrYPW-HGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1191 AIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1239
Cdd:PRK10575 185 DVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2078-2294 |
2.40e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLtkVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQV 2156
Cdd:PRK13642 2 NKILEVENL--VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 QQSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2235
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2236 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2294
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEI 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2103-2294 |
2.50e-10 |
|
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: 62.51 E-value: 2.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2103 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkellqvqQSLGYCPQCD----ALFDELTAREH 2178
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-----------VDVTAAPPADrpvsMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2179 LQLYT-----RLRGISWKDEAR-VVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKAR 2252
Cdd:cd03298 85 LTVEQnvglgLSPGLKLTAEDRqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47078218 2253 RFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:cd03298 165 AEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2074-2277 |
2.57e-10 |
|
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: 65.77 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2074 GDADNDMVKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKEL 2153
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYP----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2154 LQ--VQQSLGYCPQCDALFdELTAREHLQLYTRlrgiSWKDEArvVKWALEKLELTKY-ADKPAGTY----------SGG 2220
Cdd:TIGR02857 390 DAdsWRDQIAWVPQHPFLF-AGTIAENIRLARP----DASDAE--IREALERAGLDEFvAALPQGLDtpigeggaglSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2221 NKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSME 2277
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2080-2294 |
3.25e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 3.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKIgrILAVDrlcLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGG-----EAFVNGHSVLKE-- 2152
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV--LHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2153 --LLQVQQSLGYCPQCDALFDELTAREH-LQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAI 2229
Cdd:PRK11264 78 glIRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2230 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2108-2294 |
3.86e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGG---------------EAFVNGHSVLKEllqVQQSLGYCPQCDALFDE 2172
Cdd:PRK10982 271 LHKGEILGIAGLVGAKRTDIVETLFGIREKSAGtitlhgkkinnhnanEAINHGFALVTE---ERRSTGIYAYLDIGFNS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2173 LTAreHLQLY-TRLRGISWKDEARVVKWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2250
Cdd:PRK10982 348 LIS--NIRNYkNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVG 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47078218 2251 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK10982 426 AKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1038-1230 |
5.23e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 5.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMC---------PQHN 1104
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRDIQMVfqdsisavnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1105 VlfdRLTVEEHLWFYSRLKSMAQEEIRREMDKMIE-DLELSNKRHslvQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:PRK10419 108 V---REIIREPLRHLLSLDKAERLARASEMLRAVDlDDSVLDKRP---PQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 47078218 1184 VDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK10419 182 LDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2083-2294 |
5.66e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2083 IENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEafvnghsvlkeLLQVQQSLGy 2162
Cdd:PRK11247 15 LNAVSKRYGERTV-----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-----------LLAGTAPLA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2163 cpqcdalfdelTAREHlqlyTRL-----RGISWKdeaRVV---------KW---ALEKLELTKYADK----PAgTYSGGN 2221
Cdd:PRK11247 78 -----------EARED----TRLmfqdaRLLPWK---KVIdnvglglkgQWrdaALQALAAVGLADRanewPA-ALSGGQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2222 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK11247 139 KQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1042-1230 |
6.59e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 6.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1042 SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLGMCPQhnvlfDR--------LT 1111
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPE-----DRkaegiipvHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1112 VEE---------HLWFYSRLKSmAQEeiRREMDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:PRK11288 348 VADninisarrhHLRAGCLINN-RWE--AENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1182 AGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1035-1231 |
7.11e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 7.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1035 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyghdirtemdeIRKNLGMCPQHNVLFDRlTVEE 1114
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLWFYSRLKSmaqEEIRREMD--KMIEDLELSnKRHSLVQ------TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1186
Cdd:PLN03232 698 NILFGSDFES---ERYWRAIDvtALQHDLDLL-PGRDLTEigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1187 YARRAIWDLILKYK-PGRTILLSTHHMDEADLLgDRIAIISHGKLK 1231
Cdd:PLN03232 774 HVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1038-1236 |
7.94e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFpPTSGSATIYGHDIRT----EMDEIRKNLgmCPQHNVLFDRltve 1113
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYL--SQQQTPPFAM---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1114 eHLWFY---SRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI-------ILDEPTAG 1183
Cdd:PRK03695 85 -PVFQYltlHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 1184 VDpYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1236
Cdd:PRK03695 164 LD-VAQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2084-2299 |
1.03e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2084 ENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGY 2162
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVE-----IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2163 CPQ-----CDALFDELTAR---EHLQLYTRLRgiswKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:PRK10253 86 LAQnattpGDITVQELVARgryPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2080-2294 |
1.07e-09 |
|
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: 61.30 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKE--LLQ 2155
Cdd:COG4181 8 IIELRGLTKTVGTGA-GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaLDEdaRAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 V-QQSLGYCPQCDALFDELTAREHLQLYTRLRGISwKDEARVVKWaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:COG4181 87 LrARHVGFVFQSFQLLPTLTALENVMLPLELAGRR-DARARARAL-LERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47078218 2235 PAFIFLDEPTTGMDPKARRflwnLILDLI-----KTGRSVVLTSHSmEECEALCTRLAIMVNGRL 2294
Cdd:COG4181 165 PAILFADEPTGNLDAATGE----QIIDLLfelnrERGTTLVLVTHD-PALAARCDRVLRLRAGRL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2108-2292 |
1.97e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLG-Y-CPQCDALFDELTAREHLQLytRL 2185
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYlVPQEPLLFPNLSVKENILF--GL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2186 RGiSWKDEARvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT 2265
Cdd:PRK15439 112 PK-RQASMQK-MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ 189
|
170 180
....*....|....*....|....*..
gi 47078218 2266 GRSVVLTSHSMEECEALCTRLAIMVNG 2292
Cdd:PRK15439 190 GVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2081-2293 |
2.15e-09 |
|
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: 59.79 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkellqvqqSL 2160
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDElTAREHLqlytrLRGISWkDEAR---VVK-WALEK-LELTkyadkPAG----------TYSGGNKRKL 2225
Cdd:cd03250 69 AYVSQEPWIQNG-TIRENI-----LFGKPF-DEERyekVIKaCALEPdLEIL-----PDGdlteigekgiNLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2226 STAIALIGYPAFIFLDEPTTGMDPKARRFLW-NLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGR 2293
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2100-2303 |
2.38e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKELLQVQ--QSLGYCPQCDALFDElTARE 2177
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-IADYSEAAlrQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2178 HLQLytrlrGISWKDEARVVKwALEKLELTKYADKPAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2247
Cdd:PRK11160 433 NLLL-----AAPNASDEALIE-VLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2248 DPKARRFLWNLILDLIKtGRSVVLTSH---SMEECEALCtrlaIMVNGRLRCLGSIQHL 2303
Cdd:PRK11160 507 DAETERQILELLAEHAQ-NKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQEL 560
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1058-1231 |
2.44e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1058 GAGKTTTMSILTGLFP-PTSGSATIYGH--DIRTEMDEIRKNLGMCP--------------QHNVLfdrLTVEEHLWFYS 1120
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkrdgivpvmgvGKNIT---LAALDRFTGGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1121 RLKSMAQEE-IRREMDKM---IEDLELSnkrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI 1196
Cdd:PRK13549 375 RIDDAAELKtILESIQRLkvkTASPELA------IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI 448
|
170 180 190
....*....|....*....|....*....|....*.
gi 47078218 1197 LKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1231
Cdd:PRK13549 449 NQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2080-2369 |
2.49e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKEllqvQQS 2159
Cdd:PRK11248 1 MLQISHLYADYGGKP-----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP----GAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2239
Cdd:PRK11248 72 RGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2240 LDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLgsiQHLKNRFGDGYmitVRTK 2318
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWqETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRF---VAGE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2319 SSQSVKDVVRFFNRNfpeamlkerhhtkvqyqlksEHIsLAQVFSKMEQVS 2369
Cdd:PRK11248 226 SSRSIKSDPQFIAMR--------------------EYV-LSRVFEQREAFS 255
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2078-2309 |
2.73e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 2.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYK--SRKIGRI-------------LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEA 2142
Cdd:PRK13545 2 NYKVKFEHVTKKYKmyNKPFDKLkdlffrskdgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2143 FVNGHSVLkellqVQQSLGycpqcdaLFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNK 2222
Cdd:PRK13545 82 DIKGSAAL-----IAISSG-------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2223 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2302
Cdd:PRK13545 150 SRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKE 229
|
....*..
gi 47078218 2303 LKNRFGD 2309
Cdd:PRK13545 230 VVDHYDE 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1038-1210 |
2.77e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatiyghdIRTEmDEIRknLGMCPQhNVLFDR---LTVEE 1114
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRN-GKLR--IGYVPQ-KLYLDTtlpLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1115 HLwfysRLKSMAQEeirremDKMIEDLELSNKRHSL---VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1191
Cdd:PRK09544 89 FL----RLRPGTKK------EDILPALKRVQAGHLIdapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|.
gi 47078218 1192 IWDLI--LKYKPGRTILLSTH 1210
Cdd:PRK09544 159 LYDLIdqLRRELDCAVLMVSH 179
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1055-1209 |
2.98e-09 |
|
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: 62.53 E-value: 2.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1055 GHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLF-DrlTVEEHLWfYSRLKSmAQEEIRR 1132
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFnD--TIAYNIA-YGRPDA-SEEEVEA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1133 -----EMDKMIEDLElsNKRHSLVQ----TLSGGMKRKlsVAIAfvggsRAI-------ILDEPTAGVDPYARRAIWDLI 1196
Cdd:COG5265 467 aaraaQIHDFIESLP--DGYDTRVGerglKLSGGEKQR--VAIA-----RTLlknppilIFDEATSALDSRTERAIQAAL 537
|
170
....*....|....*...
gi 47078218 1197 LKYKPGRTIL-----LST 1209
Cdd:COG5265 538 REVARGRTTLviahrLST 555
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2108-2286 |
3.74e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.09 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPqcdALFDELTAREHLQLYTRLR 2186
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLP---GLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2187 GISWKdeaRVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTG 2266
Cdd:PRK13543 111 GRRAK---QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
170 180
....*....|....*....|
gi 47078218 2267 RSVVLTSHSMEECEALCTRL 2286
Cdd:PRK13543 188 GAALVTTHGAYAAPPVRTRM 207
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2078-2280 |
3.81e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVL-KEL 2153
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKP---ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTaKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2154 LQVQQSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2232
Cdd:PRK13640 80 WDIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 47078218 2233 GYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECE 2280
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1035-1230 |
4.01e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1035 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSG-----SATIYGHDIRTEMD--EIRKNLGMCPQHNVLF 1107
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQT----LSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1183
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47078218 1184 VDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1052-1210 |
4.04e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.56 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1052 SFLGHNGAGKTTTMSILTGlfPPTSGsaTIYGhDIRT-----EMDEIRKNLGMCPQHNVLFDRLTVEEHLWF--YSRL-K 1123
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRIsgfpkKQETFARISGYCEQNDIHSPQVTVRESLIYsaFLRLpK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1124 SMAQEEIRREMDKMIEDLELSNKRHSLV-----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA----RRAIWD 1194
Cdd:PLN03140 985 EVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAaaivMRTVRN 1064
|
170
....*....|....*.
gi 47078218 1195 LIlkyKPGRTILLSTH 1210
Cdd:PLN03140 1065 TV---DTGRTVVCTIH 1077
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
999-1230 |
5.35e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 5.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 999 MESRRFEETRGMEEEPTHLPLVVCVDKLTkVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGlFPPTSGS 1078
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1079 ATIYGHDIRT-EMDEIRKNL---GMCPQ--HNVLFDRLTVEEHlwfysrlkSMAQEEIRREMDK-----MIEDLELSnkR 1147
Cdd:PRK11174 406 LKINGIELRElDPESWRKHLswvGQNPQlpHGTLRDNVLLGNP--------DASDEQLQQALENawvseFLPLLPQG--L 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1148 HSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDeaDLLG-DRI 1222
Cdd:PRK11174 476 DTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQwDQI 553
|
....*...
gi 47078218 1223 AIISHGKL 1230
Cdd:PRK11174 554 WVMQDGQI 561
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1033-1230 |
5.44e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.53 E-value: 5.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1033 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQHNVLFDRLT 1111
Cdd:PRK10522 334 DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRKLFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1112 VEEhlwfySRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1191
Cdd:PRK10522 414 GPE-----GKPANPALVEKWLERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 47078218 1192 IWDLILKY--KPGRTILLSTHHmDEADLLGDRIAIISHGKL 1230
Cdd:PRK10522 488 FYQVLLPLlqEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2099-2308 |
5.80e-09 |
|
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: 59.04 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2099 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKELLQVQQSLGYCPQCDALFDElTARE 2177
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2178 HlqlytrlrgISWKDEA----RVVKWA--------LEKLEL---TKYADKPAGtYSGGNKRKLSTAIALIGYPAFIFLDE 2242
Cdd:cd03252 95 N---------IALADPGmsmeRVIEAAklagahdfISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2243 PTTGMDPKARRFLWNLILDlIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2308
Cdd:cd03252 165 ATSALDYESEHAIMRNMHD-ICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1019-1223 |
7.52e-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: 61.10 E-value: 7.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1019 LVVCVDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIR-TEMDEIRKNL 1097
Cdd:TIGR03719 321 KVIEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlAYVDQSRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1098 GmcPQHNVlfdrltveehlWfysrlksmaqEEIRREMDKM-IEDLELSNK------------RHSLVQTLSGGMKRKLSV 1164
Cdd:TIGR03719 398 D--PNKTV-----------W----------EEISGGLDIIkLGKREIPSRayvgrfnfkgsdQQKKVGQLSGGERNRVHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1165 AIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYkPGRTILLStHhmDEADLlgDRIA 1223
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF-AGCAVVIS-H--DRWFL--DRIA 507
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1036-1210 |
8.52e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 57.57 E-value: 8.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1036 LALNKLSLNLYENQV----VSFL--------GHNGAGKTTTMSILTGLFPPTSGSatIYGHDIRTemDEIRKNLGMCPQH 1103
Cdd:PRK13541 2 LSLHQLQFNIEQKNLfdlsITFLpsaityikGANGCGKSSLLRMIAGIMQPSSGN--IYYKNCNI--NNIAKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 NV-LFDRLTVEEHLWFYSRLKSMAQeeirrEMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1182
Cdd:PRK13541 78 NLgLKLEMTVFENLKFWSEIYNSAE-----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180
....*....|....*....|....*....
gi 47078218 1183 GVDPYARRAIWDLI-LKYKPGRTILLSTH 1210
Cdd:PRK13541 153 NLSKENRDLLNNLIvMKANSGGIVLLSSH 181
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1031-1210 |
9.27e-09 |
|
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: 57.64 E-value: 9.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1031 KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL-----TGLfppTSGSATIYGHDIRtemDEIRKNLGMCPQHNV 1105
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLD---KNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTVEEHLWFYSRLKSMAQEEirremdkmiedlelsnkrhslvqtlsggmKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:cd03232 90 HSPNLTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*.
gi 47078218 1186 PYARRAIWDLILKY-KPGRTILLSTH 1210
Cdd:cd03232 141 SQAAYNIVRFLKKLaDSGQAILCTIH 166
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2082-2299 |
1.18e-08 |
|
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: 57.54 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2082 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDEST--TGGEAFVNGHSVLkellqvqqs 2159
Cdd:cd03217 2 EIKDLHVSVGGKEI-----LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDIT--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 lgycpqcdalfdeltareHLQLYTRLR---GISWKDEARV--VKWAleklELTKYADKpagTYSGGNKRKLSTAIALIGY 2234
Cdd:cd03217 68 ------------------DLPPEERARlgiFLAFQYPPEIpgVKNA----DFLRYVNE---GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAL-CTRLAIMVNGRLRCLGS 2299
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2079-2276 |
1.23e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2079 DMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGeafvnghsVLKEllQVQQ 2158
Cdd:PRK09544 3 SLVSLENVSVSFGQRRV-----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKR--NGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2159 SLGYCPQcdALFDELTAREHLQLYTRLR-GISWKDearvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2237
Cdd:PRK09544 68 RIGYVPQ--KLYLDTTLPLTVNRFLRLRpGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47078218 2238 IFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSM 2276
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2106-2298 |
1.38e-08 |
|
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: 60.15 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2106 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKELLQvqQSLGYCPQCDALFDElTAREHLqly 2182
Cdd:COG4618 353 FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwDREELG--RHIGYLPQDVELFDG-TIAENI--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2183 TRLRGIswkDEARVVKWAlekleltKYAD-------KPAGtY-----------SGGNKRKLSTAIALIGYPAFIFLDEPT 2244
Cdd:COG4618 427 ARFGDA---DPEKVVAAA-------KLAGvhemilrLPDG-YdtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2245 TGMDPKARRFLWNLILDLIKTGRSVVLTSHSMeecEAL--CTRLAIMVNGRLRCLG 2298
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2080-2294 |
1.49e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT--GD---ESTTGGEAFVNGHSVLK--- 2151
Cdd:PRK14239 5 ILQVSDLSVYYNKKK-----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNIYSprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2152 ELLQVQQSLGYCPQCDALFdELTAREHLQLYTRLRGIswKDEArVVKWALEKL--------ELTKYADKPAGTYSGGNKR 2223
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGI--KDKQ-VLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2085-2294 |
2.10e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2085 NLTKVYKSRKIGRILAVDrLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-------ELLqvQ 2157
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHN-VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaELR--N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLGYCPQCDALFDELTAREHLQLYTRLRGiswKDEARVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:PRK11629 87 QKLGFIYQFHHLLPDFTALENVAMPLLIGK---KKPAEINSRALEMLAavgLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAiMVNGRL 2294
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1041-1238 |
2.17e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.79 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1041 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP----TSGS----------ATIYGHDIRTEMDEIRKNLGmcPQHNVl 1106
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRvlldgkpvapCALRGRKIATIMQNPRSAFN--PLHTM- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1107 fdRLTVEEHLWFYSRLKSMAQeeIRREMDKM-IEDLELSNKRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK10418 99 --HTHARETCLALGKPADDAT--LTAALEAVgLENAARVLKLYPF--EMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 1186 PYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS--PLF 1238
Cdd:PRK10418 173 VVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDveTLF 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2081-2294 |
2.33e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.17 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG------------------DESTTGGEA 2142
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2143 FVNGHSV-------LKELLQVQQSLGYCPQCD--ALFDElTAREHLQLYTRLRGISwKDEARvvKWALEKLELT----KY 2209
Cdd:PRK13651 83 VLEKLVIqktrfkkIKKIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVS-KEEAK--KRAAKYIELVgldeSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2210 ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIM 2289
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*
gi 47078218 2290 VNGRL 2294
Cdd:PRK13651 239 KDGKI 243
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1037-1230 |
3.13e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.49 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH-----DIRTEMDEIRknlgMCPQ--HNVLFDR 1109
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIR----MIFQdpSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1110 LTVEEHLWFYSRLKSMAQEEIRREmdKMIEDLE----LSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK15112 104 QRISQILDFPLRLNTDLEPEQREK--QIIETLRqvglLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 47078218 1186 PYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK15112 182 MSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2078-2305 |
3.28e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.47 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----EL 2153
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCI-----FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2154 LQVQQSLGYCPQCDALFDELTA--------REHLQLYTRLRgiswkdeARVVKWALEKLELTKYADKPAGTYSGGNKRK- 2224
Cdd:PRK11831 80 YTVRKRMSMLFQSGALFTDMNVfdnvayplREHTQLPAPLL-------HSTVMMKLEAVGLRGAAKLMPSELSGGMARRa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2225 -LSTAIALigYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2302
Cdd:PRK11831 153 aLARAIAL--EPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
...
gi 47078218 2303 LKN 2305
Cdd:PRK11831 231 LQA 233
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2108-2274 |
3.37e-08 |
|
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: 56.99 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTGdesttggeafvnghsvlkellQVQQSLG-YC--PQCDALFDELTAREhLQLY-T 2183
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAG---------------------KLKPNLGkFDdpPDWDEILDEFRGSE-LQNYfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2184 RLRG--------------------------ISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2237
Cdd:cd03236 81 KLLEgdvkvivkpqyvdlipkavkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 47078218 2238 IFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2274
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2078-2274 |
6.34e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkELLQVQ 2157
Cdd:TIGR03719 320 DKVIEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGETV--KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2158 QSLgycpqcDALFDELTAREHL---QLYTRLRGISWKDEARVVKWALekleltKYAD--KPAGTYSGGNKRKLSTAIALI 2232
Cdd:TIGR03719 392 QSR------DALDPNKTVWEEIsggLDIIKLGKREIPSRAYVGRFNF------KGSDqqKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 47078218 2233 GYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2274
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVISH 498
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
2104-2275 |
9.62e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2104 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKellqVQQS-LGYCPQCDALFDELTAREHLQLY 2182
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPyCTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2183 TRLRgiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2262
Cdd:PRK13541 95 SEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|...
gi 47078218 2263 IKTGRSVVLTSHS 2275
Cdd:PRK13541 170 ANSGGIVLLSSHL 182
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2064-2303 |
9.98e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2064 VASERQRVLRGDADNDM----VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-DESTT 2138
Cdd:PRK14271 1 MACERLGGQSGAADVDAaapaMAAVNLTLGFAGKTV-----LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2139 G----GEAFVNGHSVL--KELLQVQQSLGYC-----PQCDALFDELTA--REH-LQLYTRLRGISwkdEARVVKWALEKL 2204
Cdd:PRK14271 76 GyrysGDVLLGGRSIFnyRDVLEFRRRVGMLfqrpnPFPMSIMDNVLAgvRAHkLVPRKEFRGVA---QARLTEVGLWDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2205 ELTKYADKPAgTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTgRSVVLTSHSMEECEALCT 2284
Cdd:PRK14271 153 VKDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISD 230
|
250
....*....|....*....
gi 47078218 2285 RLAIMVNGRLRCLGSIQHL 2303
Cdd:PRK14271 231 RAALFFDGRLVEEGPTEQL 249
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2053-2294 |
1.06e-07 |
|
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: 57.42 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2053 VSTKPVEDDVDVASERqrvLRGDadndmVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT 2132
Cdd:TIGR02203 311 LDSPPEKDTGTRAIER---ARGD-----VEFRNVTFRYPGRDRP---ALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2133 GDESTTGGEAFVNGHSVLKELLQ-VQQSLGYCPQCDALFDELTAREhlQLYTRLRGIswkDEARVVKwALEKLELTKYAD 2211
Cdd:TIGR02203 380 RFYEPDSGQILLDGHDLADYTLAsLRRQVALVSQDVVLFNDTIANN--IAYGRTEQA---DRAEIER-ALAAAYAQDFVD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2212 K-PAGTY----------SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRfLWNLILDLIKTGRSVVLTSHSMEECE 2280
Cdd:TIGR02203 454 KlPLGLDtpigengvllSGGQRQRLAIARALLKDAPILILDEATSALDNESER-LVQAALERLMQGRTTLVIAHRLSTIE 532
|
250
....*....|....
gi 47078218 2281 AlCTRLAIMVNGRL 2294
Cdd:TIGR02203 533 K-ADRIVVMDDGRI 545
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2100-2293 |
1.09e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKELLQ-----VQQSLGYCPQCDALF 2170
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALEngismVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2171 DELTAR--------EHLQLYTRLRGIswkdearvvkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDE 2242
Cdd:PRK10982 93 NMWLGRyptkgmfvDQDKMYRDTKAI------------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2243 PTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2293
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2218-2294 |
1.36e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.56 E-value: 1.36e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2218 SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2081-2291 |
1.75e-07 |
|
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: 54.54 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQS 2159
Cdd:cd03254 3 IEFENVNFSYDEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDElTAREHLqLYTRLRgISWKDEARVVKWA-----LEKLE--LTKYADKPAGTYSGGNKRKLSTAIALI 2232
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENI-RLGRPN-ATDEEVIEAAKEAgahdfIMKLPngYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2233 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHsmeecealctRLAIMVN 2291
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAH----------RLSTIKN 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1023-1231 |
2.32e-07 |
|
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: 56.84 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFpPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1101
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1102 QHNVLFDRlTVEEHLWFYSRlksMAQEEIRREMDK-----MIE------DLELSNKRHslvqTLSGGMKRKLSVAIAFVG 1170
Cdd:TIGR01271 1299 QKVFIFSG-TFRKNLDPYEQ---WSDEEIWKVAEEvglksVIEqfpdklDFVLVDGGY----VLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 1171 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLK 1231
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV-EALLECQQFLVIEGSSVK 1430
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1031-1229 |
2.41e-07 |
|
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: 53.63 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1031 KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtemdeirknLGMCPQ-------- 1102
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQepwiqngt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 --HNVLFDRltVEEHLWFYSRLKSMAQEEirremdkmieDLE-LSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAI 1175
Cdd:cd03250 82 irENILFGK--PFDEERYEKVIKACALEP----------DLEiLPDGDLTEIGekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 1176 ILDEPTAGVDPYARRAIWD-LILKY-KPGRTILLSTHHMdeaDLLG--DRIAIISHGK 1229
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFEnCILGLlLNNKTRILVTHQL---QLLPhaDQIVVLDNGR 204
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2100-2297 |
2.74e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKtSTFKM-LTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDA-LFDELTARE 2177
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGK-STLAMlLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFhLFDQLLGPE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2178 HLQlytrlrgiswKDEARVVKWaLEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKAR 2252
Cdd:PRK10522 417 GKP----------ANPALVEKW-LERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 2253 RFLWNLILDLIK-TGRSVVLTSHSMEECEaLCTRLAIMVNGRLRCL 2297
Cdd:PRK10522 486 REFYQVLLPLLQeMGKTIFAISHDDHYFI-HADRLLEMRNGQLSEL 530
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1010-1186 |
3.15e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.31 E-value: 3.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1010 MEEEPTHLPLVVCVDKLTkvYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT- 1088
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1089 EMDEIRKNLGMCPQhnvLFDRLTVEEHLWFysrLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAF 1168
Cdd:PRK13543 79 DRSRFMAYLGHLPG---LKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLW 152
|
170
....*....|....*...
gi 47078218 1169 VGGSRAIILDEPTAGVDP 1186
Cdd:PRK13543 153 LSPAPLWLLDEPYANLDL 170
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2106-2277 |
3.75e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.82 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2106 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--------------KELLQVQQSLGYCPQCDALFD 2171
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQLRLLRTRLTMVFQHFNLWS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2172 ELTAREH-LQLYTRLRGISwKDEA--RVVKWaLEKLELTKYA-DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2247
Cdd:PRK10619 106 HMTVLENvMEAPIQVLGLS-KQEAreRAVKY-LAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190
....*....|....*....|....*....|
gi 47078218 2248 DPKARRFLWNLILDLIKTGRSVVLTSHSME 2277
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1037-1210 |
4.46e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDI----RTEMDEIR-KNLGMCPQhnvlfD 1108
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRaEQISMIFQ-----D 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 RLT-----------VEEHLWFYSRL-KSMAQEEIRREMD--KMIEdlelSNKRHSLV-QTLSGGMKRKLSVAIAFVGGSR 1173
Cdd:PRK09473 106 PMTslnpymrvgeqLMEVLMLHKGMsKAEAFEESVRMLDavKMPE----ARKRMKMYpHEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 47078218 1174 AIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTH 1210
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITH 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2101-2278 |
4.53e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 4.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2101 VDRLCLGVRPGEcFGLL-GVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---EllQVQQSLGYCPQCDALFDElTAR 2176
Cdd:PRK10247 23 LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpE--IYRQQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2177 EHLQLYTRLRGISwKDEARVVKwALEKLELTKYA-DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFL 2255
Cdd:PRK10247 99 DNLIFPWQIRNQQ-PDPAIFLD-DLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180
....*....|....*....|....
gi 47078218 2256 WNLILDLIK-TGRSVVLTSHSMEE 2278
Cdd:PRK10247 177 NEIIHRYVReQNIAVLWVTHDKDE 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1030-1185 |
7.15e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1030 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1108
Cdd:PLN03130 1247 YRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1109 ---RLTVE---EH----LWfYSRLKSMAQEEIRREMDKMieDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:PLN03130 1327 gtvRFNLDpfnEHndadLW-ESLERAHLKDVIRRNSLGL--DAEVSEAG----ENFSVGQRQLLSLARALLRRSKILVLD 1399
|
....*..
gi 47078218 1179 EPTAGVD 1185
Cdd:PLN03130 1400 EATAAVD 1406
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2187-2303 |
8.66e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 8.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2187 GISWKDEARVVKWALEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT 2265
Cdd:PRK13634 115 GVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKE 194
|
90 100 110
....*....|....*....|....*....|....*....
gi 47078218 2266 -GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2303
Cdd:PRK13634 195 kGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2213-2277 |
9.68e-07 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 53.16 E-value: 9.68e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47078218 2213 PAGTYSGGNKRKLSTAIALI---GYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2277
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2093-2303 |
1.11e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2093 RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKtstfkmltgdeSTTG----------GEAFVNGHSVlkELLQVQQSLGY 2162
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGK-----------STTGlallrlinsqGEIWFDGQPL--HNLNRRQLLPV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2163 CPQCDALFDE----LTAR--------EHLQLYTRLRGISWKdEARVVKwALEKLEL---TKYadKPAGTYSGGNKRKLST 2227
Cdd:PRK15134 361 RHRIQVVFQDpnssLNPRlnvlqiieEGLRVHQPTLSAAQR-EQQVIA-VMEEVGLdpeTRH--RYPAEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2228 AIALIGYPAFIFLDEPTTGMDpkarRFLWNLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2302
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLD----KTVQAQILALLKSlqqkhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
.
gi 47078218 2303 L 2303
Cdd:PRK15134 513 V 513
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1047-1225 |
1.11e-06 |
|
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: 52.37 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1047 ENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAT------------------IYGHDIRT-EMDEIRKnlgmcPQHnvlF 1107
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqNYFTKLLEgDVKVIVK-----PQY---V 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1108 DRL------TVEEHLwfysrlksmAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1181
Cdd:cd03236 97 DLIpkavkgKVGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 47078218 1182 AGVDPYAR----RAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAII 1225
Cdd:cd03236 168 SYLDIKQRlnaaRLIRELA---EDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
982-1230 |
1.19e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 982 WARTPRLSVMEEDQACAMESRRFEETRGMEEEPTHLPLVVCVDKLTKVykddKKLALNKLSLNLYENQVVSFLGHNGAGK 1061
Cdd:PRK10982 212 WIATQPLAGLTMDKIIAMMVGRSLTQRFPDKENKPGEVILEVRNLTSL----RQPSIRDVSFDLHKGEILGIAGLVGAKR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1062 TTTMSILTGLFPPTSGSATIYGHDI--RTEMDEI----------RKNLGMCPQHNVLFDRL--TVEEHLwfySRLKSMAQ 1127
Cdd:PRK10982 288 TDIVETLFGIREKSAGTITLHGKKInnHNANEAInhgfalvteeRRSTGIYAYLDIGFNSLisNIRNYK---NKVGLLDN 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1128 EEIRREMDKMIEDLELSNKRHS-LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTI 1205
Cdd:PRK10982 365 SRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI 444
|
250 260
....*....|....*....|....*..
gi 47078218 1206 LLSTHHMDEadLLG--DRIAIISHGKL 1230
Cdd:PRK10982 445 IIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2097-2291 |
1.29e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2097 RILAVDRLCLgvRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE---AFVngHSVLKELLQVQQSLGYCPQ---CDALF 2170
Cdd:PRK10938 17 KTLQLPSLTL--NAGDSWAFVGANGSGKSALARALAGELPLLSGErqsQFS--HITRLSFEQLQKLVSDEWQrnnTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2171 -DE----LTAREHLQLYTrlrgiswKDEARVVKWAlEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2245
Cdd:PRK10938 93 pGEddtgRTTAEIIQDEV-------KDPARCEQLA-QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 2246 GMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVN 2291
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1023-1214 |
1.44e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1023 VDKLTKVYKDDKK----LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAtiyghDIRTEMDEIRKNLG 1098
Cdd:PRK13545 21 FDKLKDLFFRSKDgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1099 mcpqhnvLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1178
Cdd:PRK13545 96 -------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 47078218 1179 EPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDE 1214
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEqGKTIFFISHSLSQ 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2078-2274 |
1.47e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE-AFVNGhsvLKellqv 2156
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRII-----LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiGLAKG---IK----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2157 qqsLGYCPQCDALF---DElTAREHLqlytrlrgiswkdeARVVKWALEKlELTKY-------ADK---PAGTYSGGNKR 2223
Cdd:PRK10636 377 ---LGYFAQHQLEFlraDE-SPLQHL--------------ARLAPQELEQ-KLRDYlggfgfqGDKvteETRRFSGGEKA 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2274
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVSH 485
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1038-1229 |
1.67e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.07 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLN----LYENQVVSFL-------GHNGAGKTTTMS----ILTGLFPPTSgsatiYGHDIRTEMdeIRKNlgmcpq 1102
Cdd:cd03240 1 IDKLSIRnirsFHERSEIEFFspltlivGQNGAGKTTIIEalkyALTGELPPNS-----KGGAHDPKL--IREG------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1103 hnvlfdRLTVEEHLWFYSRLKsmAQEEIRR--------------EMDKMIEDLelsnkrhslVQTLSGGMKRKLSV---- 1164
Cdd:cd03240 68 ------EVRAQVKLAFENANG--KKYTITRslailenvifchqgESNWPLLDM---------RGRCSGGEKVLASLiirl 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1165 AIAFVGGSRA--IILDEPTAGVDPYARR-AIWDLI--LKYKPGRTILLSTHHMDEADLLGD--RIAIISHGK 1229
Cdd:cd03240 131 ALAETFGSNCgiLALDEPTTNLDEENIEeSLAEIIeeRKSQKNFQLIVITHDEELVDAADHiyRVEKDGRQK 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2043-2341 |
2.10e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2043 NFLRRPQRMPVSTKPVEddVDVASERQRVLRGDAD--------NDMVKI-ENLTKVYKSRKIGRILAVDRLCLGV-RPGE 2112
Cdd:TIGR00956 11 NFRKLIDSDPIYYKPYK--LGVAYKNLSAYGVAADsdyqptfpNALLKIlTRGFRKLKKFRDTKTFDILKPMDGLiKPGE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2113 CFGLLGVNGAGKTSTFKMLTGD----ESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLYTRLR-- 2186
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIASNtdgfHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKtp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2187 -----GISWKDEA-RVVKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK-ARRF 2254
Cdd:TIGR00956 169 qnrpdGVSREEYAkHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAtALEF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2255 LWNL--ILDLIKTGRSVVLTSHSMEECEaLCTRLAIMVNGRLRCLGSIQHLKNRFGD-GYM-------------ITVRT- 2317
Cdd:TIGR00956 249 IRALktSANILDTTPLVAIYQCSQDAYE-LFDKVIVLYEGYQIYFGPADKAKQYFEKmGFKcpdrqttadfltsLTSPAe 327
|
330 340 350
....*....|....*....|....*....|....*
gi 47078218 2318 ---------KSSQSVKDVVRFFnRNFPE--AMLKE 2341
Cdd:TIGR00956 328 rqikpgyekKVPRTPQEFETYW-RNSPEyaQLMKE 361
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1028-1185 |
2.29e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1028 KVY---KDDKKL---------ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMD 1091
Cdd:PRK15079 15 KVHfdiKDGKQWfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1092 EIRKNLGMCPQHNV--LFDRLTV----EEHLWFYSrlKSMAQEEIRREMDKMIEDLEL-SNKRHSLVQTLSGGMKRKLSV 1164
Cdd:PRK15079 95 AVRSDIQMIFQDPLasLNPRMTIgeiiAEPLRTYH--PKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGI 172
|
170 180
....*....|....*....|.
gi 47078218 1165 AIAFVGGSRAIILDEPTAGVD 1185
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALD 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2081-2312 |
4.08e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 4.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKELLQVQQSL 2160
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLD-----IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2240
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2241 DEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRFGDGYM 2312
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFVAGFI 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2106-2274 |
4.59e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2106 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE-------------------------AFVNG-----HSVLKELLQ 2155
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdlivarlqqdpprnvegtvyDFVAEgieeqAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYCPQcDALFDELtAR-----EHLQLytrlrgisWKDEARVvKWALEKLELTkyADKPAGTYSGGNKRKLSTAIA 2230
Cdd:PRK11147 104 ISHLVETDPS-EKNLNEL-AKlqeqlDHHNL--------WQLENRI-NEVLAQLGLD--PDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 47078218 2231 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2274
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFISH 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2081-2274 |
5.93e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 5.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkellqvqqSL 2160
Cdd:PRK11819 325 IEAENLSKSFGDR-----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT-IKIGETV---------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 GYCPQC-DALFDELTAREhlqlytrlrgiswkdearVVKWALEKLELTKY---------------AD--KPAGTYSGGNK 2222
Cdd:PRK11819 390 AYVDQSrDALDPNKTVWE------------------EISGGLDIIKVGNReipsrayvgrfnfkgGDqqKKVGVLSGGER 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2223 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2274
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PGCAVVISH 500
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2078-2294 |
7.13e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 7.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2078 NDMVKIENLTkVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTST----FKMLTGDESTTGGEAFVNGHSVLKEL 2153
Cdd:PRK10418 2 PQQIELRNIA-LQAAQPL-----VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2154 LQ------VQQSlgycPQcdALFDEL-TAREHLQLYTRLRGISwKDEARVVKwALEKLELTKyADKPAGTY----SGGNK 2222
Cdd:PRK10418 76 LRgrkiatIMQN----PR--SAFNPLhTMHTHARETCLALGKP-ADDATLTA-ALEAVGLEN-AARVLKLYpfemSGGML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2223 RKLSTAIALIGYPAFIFLDEPTTGMDPKAR-RFLwNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQaRIL-DLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2108-2252 |
7.92e-06 |
|
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: 49.71 E-value: 7.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkellqvqqslGYCPQCDALFDELTAREHLQLYTRLRG 2187
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2188 IS--WKDEarvvkwALEKLELTKYADKPAGTYSGGNKRKlsTAIAL-IGYPAFIFL-DEPTTGMDPKAR 2252
Cdd:cd03237 91 THpyFKTE------IAKPLQIEQILDREVPELSGGELQR--VAIAAcLSKDADIYLlDEPSAYLDVEQR 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2101-2294 |
9.45e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 9.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2101 VDRLCLGVRPGECFGLLGVNGAGKT----STFKMLTGdeSTTGGEAFVNGHSVlkELLQVQQS----LGYcpqcdALFDe 2172
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTelamSVFGRSYG--RNISGTVFKDGKEV--DVSTVSDAidagLAY-----VTED- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2173 ltaREHLQL-----------YTRLRGIS---WKDEARVVKWALE---KLEL-TKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:NF040905 346 ---RKGYGLnliddikrnitLANLGKVSrrgVIDENEEIKVAEEyrkKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2294
Cdd:NF040905 423 PDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1013-1192 |
9.56e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1013 EPTHLP-LVVCVDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIRtemd 1091
Cdd:PRK10636 304 APESLPnPLLKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1092 eirknLGMCPQHNVLFDRLTvEEHLWFYSRLKSMAQEEIRREM--------DKMIEDLElsnkrhslvqTLSGGMKRKLS 1163
Cdd:PRK10636 377 -----LGYFAQHQLEFLRAD-ESPLQHLARLAPQELEQKLRDYlggfgfqgDKVTEETR----------RFSGGEKARLV 440
|
170 180
....*....|....*....|....*....
gi 47078218 1164 VAIAFVGGSRAIILDEPTAGVDPYARRAI 1192
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2106-2274 |
1.09e-05 |
|
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: 49.15 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2106 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKELLQ--VQQSLGYCPQCDALFDElTAREHLQlYT 2183
Cdd:cd03253 22 FTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-REVTLdsLRRAIGVVPQDTVLFND-TIGYNIR-YG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2184 RLrgiSWKDEA--RVVKWALEKLELTKYADKPA------GTY-SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2254
Cdd:cd03253 99 RP---DATDEEviEAAKAAQIHDKIMRFPDGYDtivgerGLKlSGGEKQRVAIARAILKNPPILLLDEATSALDTHTERE 175
|
170 180
....*....|....*....|
gi 47078218 2255 LWNLILDLIKtGRSVVLTSH 2274
Cdd:cd03253 176 IQAALRDVSK-GRTTIVIAH 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1147-1210 |
1.26e-05 |
|
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: 47.74 E-value: 1.26e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1147 RHSLVQTLSGGMKRKLSVAIAFVGGSRA----IILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTH 1210
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILALASLKprplYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITH 139
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2100-2248 |
1.78e-05 |
|
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: 50.12 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKEL--LQVQQSLGYCPQCDALFDElTARE 2177
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LKDIdrHTLRQFINYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2178 HLQLYTRlRGISWKDEARVVKWA-----LEKLEL---TKYADKpAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD 2248
Cdd:TIGR01193 567 NLLLGAK-ENVSQDEIWAACEIAeikddIENMPLgyqTELSEE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1038-1185 |
1.93e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSaTIYGHDI---RTEMDEIRKNLGmcpqhNVlFDRLT--- 1111
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGR-IIYEQDLivaRLQQDPPRNVEG-----TV-YDFVAegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1112 --VEEHLWFYSRL-KSMAQEEIRR---EMDKMIEDLELSN-----KR------------HSLVQTLSGGMKRKLSVAIAF 1168
Cdd:PRK11147 92 eeQAEYLKRYHDIsHLVETDPSEKnlnELAKLQEQLDHHNlwqleNRinevlaqlgldpDAALSSLSGGWLRKAALGRAL 171
|
170
....*....|....*..
gi 47078218 1169 VGGSRAIILDEPTAGVD 1185
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLD 188
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1020-1235 |
1.95e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.85 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1020 VVCVDKLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---------- 1087
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1088 ----TEMDEIR-KNLGMCPQH-----NVLFdrlTVEEHLWFYSRL-KSMAQEEIRREMDKMIEDLELSNKRHSLVQ---T 1153
Cdd:PRK10261 92 eqsaAQMRHVRgADMAMIFQEpmtslNPVF---TVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1154 LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1231
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....
gi 47078218 1232 CCGS 1235
Cdd:PRK10261 249 ETGS 252
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2060-2285 |
2.06e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2060 DDVDvASERQR-VLRGDADNDM----VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD 2134
Cdd:PRK15064 295 EEVK-PSSRQNpFIRFEQDKKLhrnaLEVENLTKGFDNGPL-----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2135 ESTTGGEafvnghsvlkellqVQQS----LGYCPQcD--ALFDE-LTAREHLQLYTRLrgiswKDEARVVKWALEKLELT 2207
Cdd:PRK15064 369 LEPDSGT--------------VKWSenanIGYYAQ-DhaYDFENdLTLFDWMSQWRQE-----GDDEQAVRGTLGRLLFS 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 2208 K-YADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLwNLILDLIKTgrSVVLTSHSMEECEALCTR 2285
Cdd:PRK15064 429 QdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL-NMALEKYEG--TLIFVSHDREFVSSLATR 504
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2080-2262 |
2.15e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSR----KIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkellq 2155
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 vQQSLG---YCPQC-DALFDE----LTAREH--------LQLYTRLRGISwkDEARVVKWALEKLELTKYADKPAGTYSG 2219
Cdd:PRK15112 76 -PLHFGdysYRSQRiRMIFQDpstsLNPRQRisqildfpLRLNTDLEPEQ--REKQIIETLRQVGLLPDHASYYPHMLAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47078218 2220 GNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2262
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2081-2249 |
2.34e-05 |
|
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: 47.87 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTST----FKMLtgdeSTTGGEAFVNGHSVLK-ELLQ 2155
Cdd:cd03244 3 IEFKNVSLRYRP---NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKiGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQQSLGYCPQCDALFDElTAREHLQLYTRlrgisWKDEARvvkW-ALEKLELTKYADKPAGT-----------YSGGNKR 2223
Cdd:cd03244 76 LRSRISIIPQDPVLFSG-TIRSNLDPFGE-----YSDEEL---WqALERVGLKEFVESLPGGldtvveeggenLSVGQRQ 146
|
170 180
....*....|....*....|....*.
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMDP 2249
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDP 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1039-1290 |
2.61e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.32 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1039 NKLSLNLYENQVVSFLGHNGAGKT-TTMSILTGL-FPP---TSGSATIYGHDI----RTEMDEIRKN-LGMCPQH----- 1103
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLlhasEQTLRGVRGNkIAMIFQEpmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1104 NVLFdrlTVEEHLW-FYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLV---QTLSGGMKRKLSVAIAFVGGSRAIILDE 1179
Cdd:PRK15134 106 NPLH---TLEKQLYeVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1180 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGklKCC----GSPLFLKGTYGDGYRLTlvk 1253
Cdd:PRK15134 183 PTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNG--RCVeqnrAATLFSAPTHPYTQKLL--- 257
|
250 260 270
....*....|....*....|....*....|....*..
gi 47078218 1254 rPAEPGGPQEPglasSPPGRAPLSSCSELQVSQFIRK 1290
Cdd:PRK15134 258 -NSEPSGDPVP----LPEPASPLLDVEQLQVAFPIRK 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2012-2305 |
2.95e-05 |
|
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: 49.91 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2012 SPFEWDIVTrglvAMAVEGVvgfLLTIMCQYNFLRRPQRMPV---STKPVEDDVDVASERQRVLRGDADNDMVKIENLTK 2088
Cdd:TIGR01271 1153 STLQWAVNS----SIDVDGL---MRSVSRVFKFIDLPQEEPRpsgGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTA 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2089 VYKSRkiGRILAVDrLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTgGEAFVNGHSVLKELLQV-QQSLGYCPQCD 2167
Cdd:TIGR01271 1226 KYTEA--GRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTwRKAFGVIPQKV 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2168 ALFDElTAREHLQLYTRlrgisWKDEA--RVVKWALEKLELTKYADK-----PAGTY--SGGNKRKLSTAIALIGYPAFI 2238
Cdd:TIGR01271 1302 FIFSG-TFRKNLDPYEQ-----WSDEEiwKVAEEVGLKSVIEQFPDKldfvlVDGGYvlSNGHKQLMCLARSILSKAKIL 1375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47078218 2239 FLDEPTTGMDPkarrFLWNLILDLIKTGRS---VVLTSHSME---ECEALctrlaIMVNG-RLRCLGSIQHLKN 2305
Cdd:TIGR01271 1376 LLDEPSAHLDP----VTLQIIRKTLKQSFSnctVILSEHRVEallECQQF-----LVIEGsSVKQYDSIQKLLN 1440
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2100-2274 |
2.97e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.39 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2100 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKELlqvQQSLGYCPQcDA-LFDElT 2174
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdltLESL---RRQIGVVPQ-DTfLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2175 AREHLqLYTRLrGISwkDEArvVKWALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEP 2243
Cdd:COG1132 430 IRENI-RYGRP-DAT--DEE--VEEAAKAAQAHEFIEAlPDGydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190
....*....|....*....|....*....|.
gi 47078218 2244 TTGMDPKARRFLWNLILDLIKtGRSVVLTSH 2274
Cdd:COG1132 504 TSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
2092-2299 |
3.52e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.90 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2092 SRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTG--------GEAFVNGHSVLK-ELLQVQQSLGY 2162
Cdd:PRK13547 10 ARRHRAIL--RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAiDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2163 CPQCDALFDELTAREHLQL----YTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIAL------- 2231
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2232 --IGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECEALCTRLAIMVNGRLRCLGS 2299
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1038-1235 |
3.72e-05 |
|
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: 49.56 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMcpQHNVLFDRLTVEEHlw 1117
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSL--RENILFGKALNEKY-- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1118 FYSRLKSMAqeeirremdkMIEDLEL--SNKRHSLVQ---TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1192
Cdd:TIGR00957 730 YQQVLEACA----------LLPDLEIlpSGDRTEIGEkgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 1193 WDLILKYK---PGRTILLSTHHMDEADLLgDRIAIISHGKLKCCGS 1235
Cdd:TIGR00957 800 FEHVIGPEgvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1037-1230 |
4.42e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.70 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1037 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIRKNLGMCPQ--HNVLFDRL 1110
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1111 TVEEHLWFYSRLKSMAQ-EEIRREMDKMIEDLELSnKRHSL--VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1187
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLL-PEHAWryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 47078218 1188 ARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKL 1230
Cdd:PRK10261 498 IRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2108-2248 |
4.82e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTsTF-KMLTGDESTTGGEafvnghsVLKELlqvqqSLGYCPQcdalfdELTAREHLQLYTRLR 2186
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKT-TFaKLLAGVLKPDEGE-------VDPEL-----KISYKPQ------YIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2187 GIS-------WKDEarvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALiGYPAFIF-LDEPTTGMD 2248
Cdd:PRK13409 423 SITddlgssyYKSE------IIKPLQLERLLDKNVKDLSGGELQRVAIAACL-SRDADLYlLDEPSAHLD 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2081-2248 |
4.95e-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: 48.63 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKigriLAVDRlclG-VRPGECFGLLGVNGAGKTsTF-KMLTGDESTTGGEafvnghsvlkelLQVQQ 2158
Cdd:COG1245 342 VEYPDLTKSYGGFS----LEVEG---GeIREGEVLGIVGPNGIGKT-TFaKILAGVLKPDEGE------------VDEDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2159 SLGYCPQCDALFDELTAREHL--QLYTRLRGISWKDEarvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALiGYPA 2236
Cdd:COG1245 402 KISYKPQYISPDYDGTVEEFLrsANTDDFGSSYYKTE------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACL-SRDA 474
|
170
....*....|...
gi 47078218 2237 FIF-LDEPTTGMD 2248
Cdd:COG1245 475 DLYlLDEPSAHLD 487
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2081-2278 |
7.30e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.95 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT------GDESTTGGEAFVNGHSVLKEL- 2153
Cdd:PRK14258 8 IKVNNLSFYYDTQKI-----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNIYERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2154 ---LQVQQSLGYcPQCDaLFdELTAREHLQLYTRLrgISWKDEAR---VVKWALEKLEL----TKYADKPAGTYSGGNKR 2223
Cdd:PRK14258 83 lnrLRRQVSMVH-PKPN-LF-PMSVYDNVAYGVKI--VGWRPKLEiddIVESALKDADLwdeiKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEE 2278
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2090-2278 |
8.06e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2090 YKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESttggEAFVNgHSVL--------KELLQVQQSLG 2161
Cdd:PRK10938 270 YNDRPI-----LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP----QGYSN-DLTLfgrrrgsgETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2162 YcpqcdalfdeLTAREHL--QLYTRLR-----------GI----SWKDEARVVKWaLEKLELTKY-ADKPAGTYSGGNKR 2223
Cdd:PRK10938 340 Y----------VSSSLHLdyRVSTSVRnvilsgffdsiGIyqavSDRQQKLAQQW-LDILGIDKRtADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVL-TSHSMEE 2278
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAED 464
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1038-1230 |
8.73e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1038 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTG--LFPPTSGSATIYGHDIRTEMDEIRKNLG--MCPQH--------NV 1105
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGifLAFQYpieipgvsNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1106 LFDRLTveehlwFYSRLKSMAQEEIrremdKMIEDLELSNKRHSLV------------QTLSGGMKRK---LSVAIAfvg 1170
Cdd:CHL00131 103 DFLRLA------YNSKRKFQGLPEL-----DPLEFLEIINEKLKLVgmdpsflsrnvnEGFSGGEKKRneiLQMALL--- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 1171 GSRAIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEAD-LLGDRIAIISHGKL 1230
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDyIKPDYVHVMQNGKI 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1033-1185 |
9.41e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 9.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1033 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPpTSGSATIYGHDI----RTEMDEIRKNLGMCPQ--HNVL 1106
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1107 FDRLTV----EEHLWFYSRLKSMAQEEIR--REMDKMIEDLELsnkRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1180
Cdd:PRK15134 376 NPRLNVlqiiEEGLRVHQPTLSAAQREQQviAVMEEVGLDPET---RHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
....*
gi 47078218 1181 TAGVD 1185
Cdd:PRK15134 453 TSSLD 457
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2109-2274 |
9.62e-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: 47.86 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2109 RPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHS---VLK-----ELLQVQQSL-------GYCPQ-CDALFDE 2172
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGD-YDEEPSwdeVLKrfrgtELQDYFKKLangeikvAHKPQyVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2173 L--TAREHLQLYtrlrgiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2250
Cdd:COG1245 176 FkgTVRELLEKV---------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....
gi 47078218 2251 ARRFLWNLILDLIKTGRSVVLTSH 2274
Cdd:COG1245 247 QRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2111-2386 |
1.04e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2111 GECFGLLGVNGAGKTSTFKMLT---------------------GDeSTTGGEAFVNGHSVLKELLQVQQSL--------- 2160
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvGD-DTTALQCVLNTDIERTQLLEEEAQLvaqqrelef 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2161 ------GYCPQCDALFDELTAREHLQLYTRLRGI-SWKDEARVVKwALEKLELT-KYADKPAGTYSGGNKRKLSTAIALI 2232
Cdd:PLN03073 282 etetgkGKGANKDGVDKDAVSQRLEEIYKRLELIdAYTAEARAAS-ILAGLSFTpEMQVKATKTFSGGWRMRIALARALF 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2233 GYPAFIFLDEPTTGMDPKArrFLWnLILDLIKTGRSVVLTSHSMEECEALCTrlaimvngrlrclgSIQHLKNR----FG 2308
Cdd:PLN03073 361 IEPDLLLLDEPTNHLDLHA--VLW-LETYLLKWPKTFIVVSHAREFLNTVVT--------------DILHLHGQklvtYK 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2309 DGYMITVRTKSSQsVKDVVRFFnrnfpEAMLKERHHTKV---QYQLKSEHISLAQ----VFSKMEQVSGVLGIEDYSVSQ 2381
Cdd:PLN03073 424 GDYDTFERTREEQ-LKNQQKAF-----ESNERSRSHMQAfidKFRYNAKRASLVQsrikALDRLGHVDAVVNDPDYKFEF 497
|
....*
gi 47078218 2382 TTLDN 2386
Cdd:PLN03073 498 PTPDD 502
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1019-1081 |
1.30e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 1.30e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 1019 LVVCVDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI 1081
Cdd:PRK11819 323 KVIEAENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2235-2339 |
1.46e-04 |
|
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: 46.53 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEecealctrLAIMVNgrlrcLGSIQHLKNRFGDGYMIT 2314
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH--------LLSEVP-----LENIRRLRRDSGGTTSTK 254
|
90 100
....*....|....*....|....*
gi 47078218 2315 VRTKSSQSVKDVVRFFNRNFPEAML 2339
Cdd:COG3593 255 LIDLDDEDLRKLLRYLGVTRSELLF 279
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2081-2274 |
1.68e-04 |
|
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: 45.68 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQS 2159
Cdd:cd03251 1 VEFKNVTFRYPGDGP---PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFDElTAREHLqLYTRLRGiswkDEARVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTA 2228
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENI-AYGRPGA----TREEVEE-AARAANAHEFIMElPEGydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 2229 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSH 2274
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2081-2277 |
1.93e-04 |
|
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: 44.45 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2081 VKIENLTkvYKSRKiGRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTGgeafvnghsvlkellqvqqS 2159
Cdd:cd03223 1 IELENLS--LATPD-GRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSG-------------------R 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2160 LGYCPQCDALFdeLTAREHLQLYTrLRGIS---WKDEarvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPA 2236
Cdd:cd03223 58 IGMPEGEDLLF--LPQRPYLPLGT-LREQLiypWDDV-----------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 47078218 2237 FIFLDEPTTGMDPKARRFLWNLILD----LIKTGRSVVLTS-HSME 2277
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKElgitVISVGHRPSLWKfHDRV 157
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2096-2303 |
2.39e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.55 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2096 GRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkELLQVQQS------LGYCPQCDAL 2169
Cdd:PRK10575 23 GRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-----QPLESWSSkafarkVAYLPQQLPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2170 FDELTAREHLQL-----YTRLRGISWKDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPT 2244
Cdd:PRK10575 97 AEGMTVRELVAIgrypwHGALGRFGAADREKVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2245 TGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2303
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1041-1210 |
2.55e-04 |
|
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: 46.33 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1041 LSLNLYENQVVsFL-GHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRknlgmcpQH-------NVLFDRLT 1111
Cdd:COG4615 351 IDLTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYR-------QLfsavfsdFHLFDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1112 VEEhlwfysrlksmaQEEIRREMDKMIEDLELSNK------RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:COG4615 423 GLD------------GEADPARARELLERLELDHKvsvedgRFSTTD-LSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180 190
....*....|....*....|....*....|
gi 47078218 1186 PYARRAIWDLILkykP-----GRTILLSTH 1210
Cdd:COG4615 490 PEFRRVFYTELL---PelkarGKTVIAISH 516
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2211-2275 |
3.33e-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: 3.33e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47078218 2211 DKPAGTYSGGNKR--KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHS 2275
Cdd:cd03238 82 GQKLSTLSGGELQrvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2101-2305 |
4.74e-04 |
|
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: 44.46 E-value: 4.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2101 VDRLCLGVRPGECFGLLGVNGAGKTSTF----KMLtgdesTTGGEAFVNGHSVLKELLQV-QQSLGYCPQCDALFDElTA 2175
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLsaflRLL-----NTEGDIQIDGVSWNSVPLQKwRKAFGVIPQKVFIFSG-TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2176 REHLQLYTRlrgisWKDEA--RVVKWALEKLELTKYADK-----PAGTY--SGGNKRKLSTAIALIGYPAFIFLDEPTTG 2246
Cdd:cd03289 94 RKNLDPYGK-----WSDEEiwKVAEEVGLKSVIEQFPGQldfvlVDGGCvlSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 47078218 2247 MDPKARRFLwNLILDLIKTGRSVVLTSHSMeecEAL--CTRLAIMVNGRLRCLGSIQHLKN 2305
Cdd:cd03289 169 LDPITYQVI-RKTLKQAFADCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLLN 225
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1051-1240 |
4.76e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1051 VSFLGHNGAGKTTTMSILTGLFPPTSGSATIyghdirtemdeIRKNLGMCPQHNVLFDRlTVEEHLWFYSRLKSmaqEEI 1130
Cdd:PLN03130 646 VAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TVRDNILFGSPFDP---ERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1131 RREMD--KMIEDLELSnKRHSLVQ------TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYK-P 1201
Cdd:PLN03130 711 ERAIDvtALQHDLDLL-PGGDLTEigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElR 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 47078218 1202 GRTILLST---HHMDEAdllgDRIAIISHGKLK--------CCGSPLFLK 1240
Cdd:PLN03130 790 GKTRVLVTnqlHFLSQV----DRIILVHEGMIKeegtyeelSNNGPLFQK 835
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1054-1185 |
5.00e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.87 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1054 LGHNGAGKTTTMSILTGL---FPPTSGSATIY-GHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMA--- 1126
Cdd:TIGR00956 93 LGRPGSGCSTLLKTIASNtdgFHIGVEGVITYdGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQnrp 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1127 -----QEEIRREMDKMIEDLELSNKRHS-----LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1185
Cdd:TIGR00956 173 dgvsrEEYAKHIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2104-2317 |
5.79e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2104 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALF--------DELT 2174
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFsgtvrfniDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2175 AREHLQLYTRLRGISWKDEARVVKWALEKlELTKYADkpagTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2254
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDVIDRNPFGLDA-EVSEGGE----NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47078218 2255 LWNLILDLIKTGrSVVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRT 2317
Cdd:PLN03232 1410 IQRTIREEFKSC-TMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
2218-2274 |
6.13e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 6.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 47078218 2218 SGGNKRKLSTAIAL-----IGYPaFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2274
Cdd:cd03227 79 SGGEKELSALALILalaslKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2080-2274 |
6.14e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.10 E-value: 6.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2080 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELLQ 2155
Cdd:PRK10535 4 LLELKDIRRSYPSGE-EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2156 VQ-QSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2234
Cdd:PRK10535 83 LRrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 47078218 2235 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2274
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2076-2261 |
6.84e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.80 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2076 ADNDMVKIENLTkVYKSRkiGRILaVDRLCLGVRPGEcfGLL--GVNGAGKTSTFKMLTG-DESTTGgeafvnghsvlke 2152
Cdd:COG4178 358 SEDGALALEDLT-LRTPD--GRPL-LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGlWPYGSG------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2153 llqvqqSLGYCPQCDALFdeLTAREHLQLYTrLRGI--------SWKDEArvVKWALEKLELTKYADKP------AGTYS 2218
Cdd:COG4178 419 ------RIARPAGARVLF--LPQRPYLPLGT-LREAllypataeAFSDAE--LREALEAVGLGHLAERLdeeadwDQVLS 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 47078218 2219 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2261
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
2116-2300 |
8.10e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2116 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQV-----QQSLGYCPQcDA-LFDELTAREHLQlYtrlrGIS 2189
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQ-DArLFPHYKVRGNLR-Y----GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2190 WKDEA---RVVKW-ALEKLeLTKYadkPAgTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD-PKARR---FLWNLILD 2261
Cdd:PRK11144 103 KSMVAqfdKIVALlGIEPL-LDRY---PG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKREllpYLERLARE 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 47078218 2262 lIKTgrSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2300
Cdd:PRK11144 178 -INI--PILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2108-2274 |
1.72e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2108 VRPGECFGLLGVNGAGKTSTFKMLTG--------DESTTGGEAFVN---G---HSVLKELLQVQQSLGYCPQ-CDALFDE 2172
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLKrfrGtelQNYFKKLYNGEIKVVHKPQyVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2173 L--TAREHLQLYtrlrgiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2250
Cdd:PRK13409 176 FkgKVRELLKKV---------DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180
....*....|....*....|....
gi 47078218 2251 ARRFLWNLILDLIKtGRSVVLTSH 2274
Cdd:PRK13409 247 QRLNVARLIRELAE-GKYVLVVEH 269
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
2114-2289 |
2.55e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2114 FGLLGVNGAGKTSTFKMLT----GDesTTGGEAFVNGHSVLKellqvqqslgycPQCDALFDELTAREHLQLY--TRLRG 2187
Cdd:cd03279 31 FLICGPTGAGKSTILDAITyalyGK--TPRYGRQENLRSVFA------------PGEDTAEVSFTFQLGGKKYrvERSRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2188 ISWKDEARVVkwALEKLELTKYADKPAGTYSGGNKRKLSTAIAL---------IGYP-AFIFLDEPTTGMDPKARRFLWN 2257
Cdd:cd03279 97 LDYDQFTRIV--LLPQGEFDRFLARPVSTLSGGETFLASLSLALalsevlqnrGGARlEALFIDEGFGTLDPEALEAVAT 174
|
170 180 190
....*....|....*....|....*....|...
gi 47078218 2258 lILDLIKT-GRSVVLTSHSMEECEALCTRLAIM 2289
Cdd:cd03279 175 -ALELIRTeNRMVGVISHVEELKERIPQRLEVI 206
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2104-2274 |
2.65e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 41.84 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2104 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGdeSTTG-GEAFVNGHSvLKELLQVQQSL--GY-CPQCDALFdELTAREHL 2179
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG--LLPGsGSIQFAGQP-LEAWSAAELARhrAYlSQQQTPPF-AMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2180 QLYtRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGN-KRKLSTAIALIGYPA------FIFLDEPTTGMDPKAR 2252
Cdd:PRK03695 91 TLH-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEwQRVRLAAVVLQVWPDinpagqLLLLDEPMNSLDVAQQ 169
|
170 180
....*....|....*....|..
gi 47078218 2253 RFLWNLILDLIKTGRSVVLTSH 2274
Cdd:PRK03695 170 AALDRLLSELCQQGIAVVMSSH 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1076-1212 |
2.68e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 1076 SGSATIYGHDI-RTEMDEIRKNLGMCPQHNVLFDrLTVEEHLWFYSrlKSMAQEEIRR-----EMDKMIEdlELSNKRHS 1149
Cdd:PTZ00265 1276 SGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFGK--EDATREDVKRackfaAIDEFIE--SLPNKYDT 1350
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47078218 1150 LV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHM 1212
Cdd:PTZ00265 1351 NVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRI 1419
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2224-2306 |
7.38e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.04 E-value: 7.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 2224 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2302
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 47078218 2303 LKNR 2306
Cdd:COG4170 246 ILKS 249
|
|
| MelB |
COG2211 |
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]; |
737-862 |
7.55e-03 |
|
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
Pssm-ID: 441813 [Multi-domain] Cd Length: 447 Bit Score: 41.43 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47078218 737 MMPLCMVISWVYSVAMTIQHIVAEKEH-RLKEVMKTMgLNNAVHWVAWFITGFVQLSISVTAlTAILKYGQVLMHSHVVI 815
Cdd:COG2211 188 IFAVLGLLAFLLTFFGTKERPVPEEEKvSLKESLKAL-LKNRPFLLLLLAYLLFFLALALVA-ALLLYYFKYVLGLSAAL 265
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 47078218 816 IWLFLAVYAVATIMFCFLVSVL---YSKAKLASAcGGIIYFLSYVPYMYV 862
Cdd:COG2211 266 VGLLLALYFLAALLGAPLWPRLakrFGKKKAFII-GLLLAALGLLLLFFL 314
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1003-1078 |
8.12e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 8.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 47078218 1003 RFEETRGMEEepthlpLVVCVDKLTKVYkDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGS 1078
Cdd:PRK15064 308 RFEQDKKLHR------NALEVENLTKGF-DNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
|
| |
