|
Name |
Accession |
Description |
Interval |
E-value |
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-1480 |
0e+00 |
|
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: 2869.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELAS-KKNPKLINALRRCFFW 79
Cdd:TIGR01271 1 MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASaKKNPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 80 RFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSL 159
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 160 IYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAG 239
Cdd:TIGR01271 161 IYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 240 LGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVF 319
Cdd:TIGR01271 241 LGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 320 LSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTA 399
Cdd:TIGR01271 321 LSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 400 FWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSE 479
Cdd:TIGR01271 401 SWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 480 GKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLA 559
Cdd:TIGR01271 481 GKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 560 RAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPD 639
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 640 FSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPV-SWTETKKQSFKQTG-EFGEKRKNS-ILNPINSIRKFSIVQK 716
Cdd:TIGR01271 641 FSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDSTVfSGPETIKQSFKQPPpEFAEKRKQSiILNPIASARKFSFVQM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 717 TPLQMNGIEED--SDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSvNQGQNIHRKTTASTRKV 794
Cdd:TIGR01271 721 GPQKAQATTIEdaVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHS-NRGENRREQLQTSFRKK 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 795 SLAPQAN--LTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLA 872
Cdd:TIGR01271 800 SSITQQNelASELDIYSRRLSKDSVYEISEEINEEDLKECFADERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLA 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 873 EVAASLVVLWLLGNTP---LQDKGNSTHSRN--NSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKI 947
Cdd:TIGR01271 880 EVAASLLGLWLITDNPsapNYVDQQHANASSpdVQKPVIITPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKR 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 948 LHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFI 1027
Cdd:TIGR01271 960 LHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFI 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1028 MLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIF 1107
Cdd:TIGR01271 1040 MLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIF 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1108 VIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEG-KPTKSTKPYkngQ 1186
Cdd:TIGR01271 1120 VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEpRPSGGGGKY---Q 1196
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1187 LSKVMIIENSHVKKddIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGE 1266
Cdd:TIGR01271 1197 LSTVLVIENPHAQK--CWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE 1274
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1267 IQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVL 1346
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVL 1354
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1427 IQKLLNERSLFRQAISPSDRVKLFP--HRNSSKCKSKPQIAALKEETEEEVQDTRL 1480
Cdd:TIGR01271 1435 IQKLLNETSLFKQAMSAADRLKLFPlhRRNSSKRKPQPKITALREEAEEEVQNTRL 1490
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
844-1167 |
0e+00 |
|
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350044 [Multi-domain] Cd Length: 324 Bit Score: 610.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 844 TTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVA 923
Cdd:cd18600 1 TTWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 924 DTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIG 1003
Cdd:cd18600 81 DSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1004 AIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALN 1083
Cdd:cd18600 161 AITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1084 LHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18600 241 LHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
....
gi 90421313 1164 FKFI 1167
Cdd:cd18600 321 FKFI 324
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
389-670 |
0e+00 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 586.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 389 TTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLL 468
Cdd:cd03291 1 TTGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 469 MVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITL 548
Cdd:cd03291 81 MLILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 628
Cdd:cd03291 161 SGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 90421313 629 TFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFS 670
Cdd:cd03291 241 TFSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1208-1480 |
0e+00 |
|
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: 559.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFG 1287
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 1367
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1368 LLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRV 1447
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
|
250 260 270
....*....|....*....|....*....|....*
gi 90421313 1448 KLFPHRNSSKCKSK--PQIAALKEETEEEVQDTRL 1480
Cdd:cd03289 241 KLFPRRNSSKSKRKprPQIQALQEETEEEVQDTRL 275
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-1437 |
5.72e-174 |
|
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: 561.87 E-value: 5.72e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 5 PLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELAS--------------------- 63
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKtrkqpvsavygkkdpskpkgs 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 64 -------------------KKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDpdNKEERSIAIYLG 124
Cdd:TIGR00957 283 sqldaneevealivksphkPRKPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVN--DPMAPDWQGYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 125 IGLclLFI---VRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFV 201
Cdd:TIGR00957 361 TGL--LFVcacLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 202 WIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAM 281
Cdd:TIGR00957 439 WSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 282 EKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALI-KGIIL--RKIFTTISFCIVLRMAVTrQFPWAV 358
Cdd:TIGR00957 519 LDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdENNILdaEKAFVSLALFNILRFPLN-ILPMVI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 359 QTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTE------VVMENVTAFWEEGFgelfekakqnnnnrktsngddslffsn 432
Cdd:TIGR00957 598 SSIVQASVSLKRLRIFLSHEELEPDSIERRTIKpgegnsITVHNATFTWARDL--------------------------- 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 fsllgTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSY 512
Cdd:TIGR00957 651 -----PPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKAL 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 513 DEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVC 592
Cdd:TIGR00957 726 NEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 593 K--LMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELqnLQPDfssklmgcDSFDQFsaeRRNSILTETlhrfs 670
Cdd:TIGR00957 806 PegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQEL--LQRD--------GAFAEF---LRTYAPDEQ----- 867
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 671 lEGDAPVSWTetkkqsfkqTGEFGEKRKNSILNpiNSIRKFSIVQKTplqmngieedsdepLERRLSlvpdseqgeailp 750
Cdd:TIGR00957 868 -QGHLEDSWT---------ALVSGEGKEAKLIE--NGMLVTDVVGKQ--------------LQRQLS------------- 908
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 751 risvistgptlqarrrqsvlNLMTHSVNQGQniHRKTTASTRKVSLAPQA-NLTELDiysrrlSQETG-LEISeeineed 828
Cdd:TIGR00957 909 --------------------ASSSDSGDQSR--HHGSSAELQKAEAKEETwKLMEAD------KAQTGqVELS------- 953
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 829 lkeCFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWclviflaevaaslVVLWLlgNTPLQDkgnsthSRNNSYAVIIt 908
Cdd:TIGR00957 954 ---VYWDYMKAIGLFITFLSIFLFVCNHVSALASNYW-------------LSLWT--DDPMVN------GTQNNTSLRL- 1008
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 909 stSSYYVFYIYVGVADTLLAMGFFRGLplvhtlITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLP 988
Cdd:TIGR00957 1009 --SVYGALGILQGFAVFGYSMAVSIGG------IQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIP 1080
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 989 LTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAF 1068
Cdd:TIGR00957 1081 PVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAF 1160
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1069 GRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMI--FVIFFIAVtFISILTTGEGEGRVGIILTLAMNIMSTLQWA 1146
Cdd:TIGR00957 1161 EEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVgnCIVLFAAL-FAVISRHSLSAGLVGLSVSYSLQVTFYLNWL 1239
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1147 VNSSIDVDSLMRSVSRVFKFIDMPTEGkptkstkPYkngqlskvmIIENShvKKDDIWPSGGQMTVKDLTAKYTEGGNAI 1226
Cdd:TIGR00957 1240 VRMSSEMETNIVAVERLKEYSETEKEA-------PW---------QIQET--APPSGWPPRGRVEFRNYCLRYREDLDLV 1301
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLD 1305
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLD 1381
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1306 PYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIR 1385
Cdd:TIGR00957 1382 PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1386 RTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLF 1437
Cdd:TIGR00957 1462 STIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-1437 |
4.77e-162 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 528.78 E-value: 4.77e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 5 PLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRElASKKNPKLINALRRCFFWRFMFY 84
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCWTEE-SRRPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 85 GIFLYLGEVTKAVQPLLLGRIIASYDPDNKE----ERSIAIYLGIGLCLLFIVRTLLlhpaifGLHHIGMQMRIAMFSLI 160
Cdd:PLN03232 307 GIFKIGHDLSQFVGPVILSHLLQSMQEGDPAwvgyVYAFLIFFGVTFGVLCESQYFQ------NVGRVGFRLRSTLVAAI 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGL 240
Cdd:PLN03232 381 FHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 241 GRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFL 320
Cdd:PLN03232 461 VRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLV 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 321 SVLPYALIKG-IILRKIFTTISFCIVLRMAVTrQFPWAVQTWYDSLGAINKIQDFLQKQEyKTLEYNLT----TTEVVME 395
Cdd:PLN03232 541 SFGVFVLLGGdLTPARAFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEE-RILAQNPPlqpgAPAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 396 NVTAFWEEgfgelfekakqnnnnrKTSNgddslffsnfsllgtPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGEL 475
Cdd:PLN03232 619 NGYFSWDS----------------KTSK---------------PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 476 EPSE-GKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRA 554
Cdd:PLN03232 668 SHAEtSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQ 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 555 RISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQ 634
Cdd:PLN03232 748 RVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 635 nlqpdfssklmgcdsfdqfsaerRNSILTETLhrfslegdapvswtetkkqsFKQTGEFGEKRKnsilnpinsirkfsiv 714
Cdd:PLN03232 828 -----------------------KSGSLFKKL--------------------MENAGKMDATQE---------------- 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 715 qktplqmngiEEDSDEPLerrlslvpdSEQGEAILPRISVISTGPTLQARRRQSVLnlmthsVNQGQnihrkttastrkv 794
Cdd:PLN03232 849 ----------VNTNDENI---------LKLGPTVTIDVSERNLGSTKQGKRGRSVL------VKQEE------------- 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 795 slapqanlteldiysrrlsQETGleiseeineedlkecffddmesipaVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEV 874
Cdd:PLN03232 891 -------------------RETG-------------------------IISWNVLMRYNKAVGGLWVVMILLVCYLTTEV 926
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 875 AASLVVLWLLGNTplqdkgnsTHSRNNSYaviitsTSSYYVFyIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLH 954
Cdd:PLN03232 927 LRVSSSTWLSIWT--------DQSTPKSY------SPGFYIV-VYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLN 991
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 955 SVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFL 1034
Cdd:PLN03232 992 SILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQ 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1035 QTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIF-VIFFIA 1113
Cdd:PLN03232 1072 STSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGgVMIWLT 1151
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1114 VTFiSILTTGEGEGRV------GIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPtkstkpykngql 1187
Cdd:PLN03232 1152 ATF-AVLRNGNAENQAgfastmGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATA------------ 1218
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1188 skvmIIENShvKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GE 1266
Cdd:PLN03232 1219 ----IIENN--RPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGR 1292
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1267 IQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVL 1346
Cdd:PLN03232 1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENF 1372
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:PLN03232 1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDS 1452
|
1450
....*....|..
gi 90421313 1427 IQKLL-NERSLF 1437
Cdd:PLN03232 1453 PQELLsRDTSAF 1464
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-1437 |
2.20e-146 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 488.09 E-value: 2.20e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 5 PLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELaSKKNPKLINALRRCFFWRFMFY 84
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWDEEL-KKPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 85 GIFLYLGEVTKAVQPLLLGRIIASYDPDNKEER----SIAIYLGIGLCLLF-------IVRTlllhpaifglhhiGMQMR 153
Cdd:PLN03130 307 GFFKIGNDLSQFVGPLLLNLLLESMQNGEPAWIgyiyAFSIFVGVVLGVLCeaqyfqnVMRV-------------GFRLR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 154 IAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVL 233
Cdd:PLN03130 374 STLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLM 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 234 ALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFS 313
Cdd:PLN03130 454 FPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSI 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 314 GFFVVFLSVLPYALIKGIIL-RKIFTTISFCIVLRMAVTrQFPWAVQTWYDSLGAINKIQDFLQKQEY-----KTLEYNL 387
Cdd:PLN03130 534 PVLVTVVSFGVFTLLGGDLTpARAFTSLSLFAVLRFPLF-MLPNLITQAVNANVSLKRLEELLLAEERvllpnPPLEPGL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 388 TTteVVMENVTAFWEEgfgelfeKAKQnnnnrktsngddslffsnfsllgtPVLKDINFKIERGQLLAVAGSTGAGKTSL 467
Cdd:PLN03130 613 PA--ISIKNGYFSWDS-------KAER------------------------PTLSNINLDVPVGSLVAIVGSTGEGKTSL 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 468 LMVIMGELEP-SEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGI 546
Cdd:PLN03130 660 ISAMLGELPPrSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGV 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 547 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYF 626
Cdd:PLN03130 740 NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKE 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 627 YGTFSELQNLQPDFSsKLMgcdsfdqfsaerrnsiltetlhrfslegdapvswtetkkqsfKQTGefgekrknsilnpin 706
Cdd:PLN03130 820 EGTYEELSNNGPLFQ-KLM------------------------------------------ENAG--------------- 841
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 707 sirkfsivqktplQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRisviSTGPTLQARRRQSVLnlmthsvnqgqnihrk 786
Cdd:PLN03130 842 -------------KMEEYVEENGEEEDDQTSSKPVANGNANNLKK----DSSSKKKSKEGKSVL---------------- 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 787 ttastrkvslapqanlteldiySRRLSQETGleiseeineedlkecffddmesipaVTTWNTYLRYITVHKSLIFVLIWC 866
Cdd:PLN03130 889 ----------------------IKQEERETG-------------------------VVSWKVLERYKNALGGAWVVMILF 921
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 867 LVIFLAEVAASLVVLWLLGNTplqDKGNS-THS---RNNSYA------VIITSTSSYYvfyiyvgvadtllamgffrglp 936
Cdd:PLN03130 922 LCYVLTEVFRVSSSTWLSEWT---DQGTPkTHGplfYNLIYAllsfgqVLVTLLNSYW---------------------- 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 937 LVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFI----QLL--LIVIGAIAVVAV 1010
Cdd:PLN03130 977 LIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqifQLLstFVLIGIVSTISL 1056
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1011 LqpyifvATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWF 1090
Cdd:PLN03130 1057 W------AIMPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTL 1130
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1091 LYLSTLRWFQMRIEMI--FVIFFIAvTFiSILTTGEGEGRV------GIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSR 1162
Cdd:PLN03130 1131 VNMSSNRWLAIRLETLggLMIWLTA-SF-AVMQNGRAENQAafastmGLLLSYALNITSLLTAVLRLASLAENSLNAVER 1208
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1163 VFKFIDMPTEGKPtkstkpykngqlskvmIIENShvKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGL 1242
Cdd:PLN03130 1209 VGTYIDLPSEAPL----------------VIENN--RPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGI 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1243 LGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADE 1321
Cdd:PLN03130 1271 VGRTGAGKSSMLNALFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLER 1350
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1322 VGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCE 1401
Cdd:PLN03130 1351 AHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIA 1430
|
1450 1460 1470
....*....|....*....|....*....|....*..
gi 90421313 1402 HRIEAMLECQQFLVIEENKVRQYDSIQKLL-NERSLF 1437
Cdd:PLN03130 1431 HRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSAF 1467
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
83-372 |
1.34e-130 |
|
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; This group represents the six-transmembrane domain 1 (TMD1) of the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), which belongs to the ABCC subfamily. CFTR functions as a chloride channel, in contrast to other ABC transporters, and controls ion and water secretion and absorption in epithelial tissues. ABC proteins are formed from two homologous halves each containing a transmembrane domain (TMD) and a cytosolic nucleotide binding domain (NBD). In CFTR, these two TMD-NBD halves are linked by the unique regulatory (R) domain, which is not present in other ABC transporters. The ion channel only opens when its R-domain is phosphorylated by cyclic AMP-dependent protein kinase (PKA) and ATP is bound at the NBDs. Mutations in CFTR cause cystic fibrosis, the most common lethal genetic disorder in populations of Northern European descent.
Pssm-ID: 350038 [Multi-domain] Cd Length: 291 Bit Score: 405.86 E-value: 1.34e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 83 FYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYK 162
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 163 KTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGR 242
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 243 MMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSV 322
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 323 LPYALIKGII-LRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQ 372
Cdd:cd18594 241 VPYVLTGNTLtARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
69-1438 |
6.37e-126 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 429.58 E-value: 6.37e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 69 LINALRRCFFWRFMFygifLYLGEVTKAVQPLLLGRIIASYDPDNKeersiAIYLGIGLCLLFIVRTLLLHPAIFGLHHI 148
Cdd:PTZ00243 238 LFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDADNA-----TWGRGLGLVLTLFLTQLIQSVCLHRFYYI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 149 ----GMQMRIAMFSLIYKKTLKLSSRVLDK--ISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQAS 222
Cdd:PTZ00243 309 sircGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWC 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 223 AFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYV 302
Cdd:PTZ00243 389 ALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 303 RYFNSSAFFFSGFFVVFLSVLPYALIkGIILRK--IFTTISFCIVLRMAVtRQFPWAVQTWYDSLGAINKIQDFLQ---- 376
Cdd:PTZ00243 469 RVATSFVNNATPTLMIAVVFTVYYLL-GHELTPevVFPTIALLGVLRMPF-FMIPWVFTTVLQFLVSIKRISTFLEcdna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 377 -------KQEYKTLEYNLTTT---EVVMEN--VTAFW------------------------------------------- 401
Cdd:PTZ00243 547 tcstvqdMEEYWREQREHSTAcqlAAVLENvdVTAFVpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedt 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 402 -------------EEGFGELFEKAKQNNNNRKTSNGDDSLFFSnfsLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLL 468
Cdd:PTZ00243 627 dygspssasrhivEGGTGGGHEATPTSERSAKTPKMKTDDFFE---LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 469 MVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITL 548
Cdd:PTZ00243 704 QSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 628
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 629 TFSelqnlqpDFssklMGCDSFDQFSAErrnsiLTETLHRFSLEGDAPVSWTETKKqsfkqtgefgekrknsilnpinsi 708
Cdd:PTZ00243 864 SSA-------DF----MRTSLYATLAAE-----LKENKDSKEGDADAEVAEVDAAP------------------------ 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 709 rkfsivqktplqmnGIEEDSDEPLERRLSLvpdSEQGEAilprisviSTGPTLQARrrqsvlnLMThsvnqgqnihrktt 788
Cdd:PTZ00243 904 --------------GGAVDHEPPVAKQEGN---AEGGDG--------AALDAAAGR-------LMT-------------- 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 789 astrkvslapqanlteldiysrRLSQETGleiseeineedlkecffddmeSIPavttWNTYLRYITVHKSLIFVLIWCLV 868
Cdd:PTZ00243 938 ----------------------REEKASG---------------------SVP----WSTYVAYLRFCGGLHAAGFVLAT 970
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 869 IFLAEVAASLVVLWLlgntplqdkgnsthSRNNSYAVIITSTSSYYVfYIYVGVADTLlamgffrGLPL-----VHTLIT 943
Cdd:PTZ00243 971 FAVTELVTVSSGVWL--------------SMWSTRSFKLSAATYLYV-YLGIVLLGTF-------SVPLrfflsYEAMRR 1028
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 944 VSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVI 1023
Cdd:PTZ00243 1029 GSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCG 1108
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1024 VAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQpyfETLFHKALN----LHTANwFLYLSTLRWF 1099
Cdd:PTZ00243 1109 YLYYRLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKA---HLVMQEALRrldvVYSCS-YLENVANRWL 1184
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1100 QMRIEMIFVIFFIAVTFISILTTGEGEGR--VGII---LTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFID------ 1168
Cdd:PTZ00243 1185 GVRVEFLSNIVVTVIALIGVIGTMLRATSqeIGLVslsLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDevphed 1264
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1169 MPtEGKPTKSTKPYKNGQLSKV---MIIENSHVKKDDIWP-SGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLG 1244
Cdd:PTZ00243 1265 MP-ELDEEVDALERRTGMAADVtgtVVIEPASPTSAAPHPvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVG 1343
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1245 RTGSGKSTLLSAFLRLLNT-EGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVG 1323
Cdd:PTZ00243 1344 RTGSGKSTLLLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVG 1423
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1324 LRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK-AKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEH 1402
Cdd:PTZ00243 1424 LRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAH 1503
|
1450 1460 1470
....*....|....*....|....*....|....*..
gi 90421313 1403 RIEAMLECQQFLVIEENKVRQYDSIQKL-LNERSLFR 1438
Cdd:PTZ00243 1504 RLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFH 1540
|
|
| CFTR_R |
pfam14396 |
Cystic fibrosis TM conductance regulator (CFTR), regulator domain; |
639-849 |
4.94e-122 |
|
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
Pssm-ID: 464164 Cd Length: 213 Bit Score: 379.46 E-value: 4.94e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 639 DFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNS-ILNPINSIRKFSIVQKT 717
Cdd:pfam14396 1 DFSSLLMGLEAFDNFSAERRNSILTETLRRFSVDEDAGGSRNEPKKQSFKQTDDFNEKRKNSvILNPLAASRKFSIIQKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 718 PLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLA 797
Cdd:pfam14396 81 QLQMNGIEEGLSELPERRLSLVPESEQGEAALPRSNVLNTGPTLQGQRRQSVLALMTNTVAQGQGRREKGQSSFRKMSVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 798 PQANL-TELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTY 849
Cdd:pfam14396 161 PQSNLaSELDIYARRLSKDSVLDITEEINEEDLKECFADDIENVFETTTWNTY 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
392-623 |
1.10e-94 |
|
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: 303.62 E-value: 1.10e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 392 VVMENVTAFWEEGFGElfekakqnnnnrktsngddslffsnfsllGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVI 471
Cdd:cd03250 1 ISVEDASFTWDSGEQE-----------------------------TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 472 MGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGG 551
Cdd:cd03250 52 LGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 552 QRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCK-LMANKTRILVTSKMEHLKKADKILILHEGS 623
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGlLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1208-1426 |
2.81e-92 |
|
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: 297.48 E-value: 2.81e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVeLSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 1366
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1367 LLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
858-1163 |
3.44e-84 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 278.44 E-value: 3.44e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 858 SLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRN---NSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRG 934
Cdd:cd18601 1 GVFVFILLVLLNIAAQVLYVLSDWWLSYWANLEEKLNDTTDRVqgeNSTNVDIEDLDRDFNLGIYAGLTAATFVFGFLRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 935 LPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPY 1014
Cdd:cd18601 81 LLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVVNPW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1015 IFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLS 1094
Cdd:cd18601 161 VLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFLFLA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1095 TLRWFQMRIEMIFVIFFIAVTFISI-LTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18601 241 TSRWLAVRLDALCALFVTVVAFGSLfLAESLDAGLVGLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
845-1439 |
1.67e-83 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 285.91 E-value: 1.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 845 TWNTYLRYITVHKSLIFVLIwclVIFLAEVAASLVVLWLLGntPLQDKGNSTHSRNNSYAVIItstssyyvfyIYVGVAD 924
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILAL---LLLLLSALLELLLPLLLG--RIIDALLAGGDLSALLLLLL----------LLLGLAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 925 TLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGA 1004
Cdd:COG1132 73 LRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1005 IAVVAVLQPY---IFVATVPVIVAFIMlraYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKA 1081
Cdd:COG1132 153 LVVLFVIDWRlalIVLLVLPLLLLVLR---LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1082 LNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGE---GRVGIILTLAMNIMSTLQWAVNSSIDVDSLMR 1158
Cdd:COG1132 230 NEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSltvGDLVAFILYLLRLFGPLRQLANVLNQLQRALA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1159 SVSRVFKFIDMPTEGKPTKSTKPYKngqlskvmiienshvkkddiwPSGGQMTVKDLTAKYtEGGNAILENISFSISPGQ 1238
Cdd:COG1132 310 SAERIFELLDEPPEIPDPPGAVPLP---------------------PVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1239 RVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL---DPYEqwSDQE 1314
Cdd:COG1132 368 TVALVGPSGSGKSTLVNLLLRFYDpTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDA--TDEE 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1315 IWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD 1394
Cdd:COG1132 446 VEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKG 525
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 90421313 1395 CTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:COG1132 526 RTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYAR 570
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
859-1167 |
1.71e-78 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 261.28 E-value: 1.71e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 859 LIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDkgnsthsrnnsyaviiTSTSSYYVFYIYVGVADTLLAMGFFRGLPLV 938
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSP----------------NSSSGYYLGVYAALLVLASVLLVLLRWLLFV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 939 HTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVA 1018
Cdd:cd18580 65 LAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1019 TVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRW 1098
Cdd:cd18580 145 LPPLLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1099 FQMRIEMIFVIFFIAVTFISILTTGE-GEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFI 1167
Cdd:cd18580 225 LGLRLDLLGALLALVVALLAVLLRSSiSAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
927-1439 |
1.90e-70 |
|
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: 251.68 E-value: 1.90e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 927 LAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSkDIAILDDLLPLTIFDFIQLLLIVIGAIA 1006
Cdd:COG2274 210 GLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1007 VVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYF----ETLFHKAL 1082
Cdd:COG2274 289 VLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFrrrwENLLAKYL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1083 NL-----HTANWFLYLSTLrwfqmriemIFVIFFIAVTFISILTTGEGEGRVG------IILTLAMNIMSTLqwaVNSSI 1151
Cdd:COG2274 369 NArfklrRLSNLLSTLSGL---------LQQLATVALLWLGAYLVIDGQLTLGqliafnILSGRFLAPVAQL---IGLLQ 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1152 DVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQlskvmiienshvkkddiwpsgGQMTVKDLTAKYTEGGNAILENIS 1231
Cdd:COG2274 437 RFQDAKIALERLDDILDLPPEREEGRSKLSLPRLK---------------------GDIELENVSFRYPGDSPPVLDNIS 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1232 FSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL---DPY 1307
Cdd:COG2274 496 LTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENItlgDPD 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1308 EqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRT 1387
Cdd:COG2274 576 A--TDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN 653
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1388 LKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:COG2274 654 LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAE 705
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
964-1440 |
1.47e-68 |
|
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: 242.36 E-value: 1.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 964 LNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYI-FVATVPVIVAFIMLRAYFLQTSQQLKQ 1042
Cdd:COG4987 106 LARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALaLVLALGLLLAGLLLPLLAARLGRRAGR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1043 LESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFEtlfhKALNLHTANWFLYLSTLRWFQMRIE--MIFVIFFIAVTFISIL 1120
Cdd:COG4987 186 RLAAARAALRARLTDLLQGAAELAAYGALDRAL----ARLDAAEARLAAAQRRLARLSALAQalLQLAAGLAVVAVLWLA 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1121 TTGEGEGRVGIILtLAMNIMSTLqwavnSSIDV-----------DSLMRSVSRVFKFIDM-PTEGKPTKSTKPykngqls 1188
Cdd:COG4987 262 APLVAAGALSGPL-LALLVLAAL-----ALFEAlaplpaaaqhlGRVRAAARRLNELLDApPAVTEPAEPAPA------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1189 kvmiienshvkkddiwPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEI 1267
Cdd:COG4987 329 ----------------PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDpQSGSI 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1268 QIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGC 1344
Cdd:COG4987 393 TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGR 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1345 VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQY 1424
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
|
490
....*....|....*.
gi 90421313 1425 DSIQKLLNERSLFRQA 1440
Cdd:COG4987 551 GTHEELLAQNGRYRQL 566
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
85-371 |
2.07e-67 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 229.29 E-value: 2.07e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 85 GIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKT 164
Cdd:cd18579 3 GLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 165 LKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMM 244
Cdd:cd18579 83 LRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 245 MKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLP 324
Cdd:cd18579 163 SKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFAT 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 90421313 325 YALIKGII-LRKIFTTISFCIVLRMaVTRQFPWAVQTWYDSLGAINKI 371
Cdd:cd18579 243 YVLLGNPLtAAKVFTALSLFNLLRF-PLLMLPQAISSLIEALVSLKRI 289
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
83-371 |
6.85e-66 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350037 [Multi-domain] Cd Length: 291 Bit Score: 225.18 E-value: 6.85e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 83 FYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKE-ERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIY 161
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSiSLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 162 KKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLG 241
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 242 RMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLS 321
Cdd:cd18593 161 KLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 322 VLPYALIKGIIL-RKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKI 371
Cdd:cd18593 241 FLAYILLGNILTaERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
63-622 |
1.17e-58 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 213.49 E-value: 1.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 63 SKKNPKLINALRRCF--FWRFMFYGIFLYLGE-VTKAVQPLLLGRIIASYDpdNKEERSIAIYLGIGLCLLFIVRTLLLH 139
Cdd:COG1132 2 SKSPRKLLRRLLRYLrpYRGLLILALLLLLLSaLLELLLPLLLGRIIDALL--AGGDLSALLLLLLLLLGLALLRALLSY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 140 PAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLA-LAHFVWIAPLQVALLMGLI--- 215
Cdd:COG1132 80 LQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAhGLPQLVRSVVTLIGALVVLfvi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 216 -WELlqasAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAM----EKMIENLRQ 290
Cdd:COG1132 160 dWRL----ALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERElerfREANEELRR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 291 TELKLTRKAAyvryfnssaffFSGFFVVFLSVLPYALIKGIILRKIF-------TTISFCIVLRMAVT--RQFPWAVQTW 361
Cdd:COG1132 236 ANLRAARLSA-----------LFFPLMELLGNLGLALVLLVGGLLVLsgsltvgDLVAFILYLLRLFGplRQLANVLNQL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 362 YDSLGAINKIQDFLQ-----KQEYKTLEYNLTTTEVVMENVTaFweeGFGElfekakqnnnnrktsngddslffsnfsll 436
Cdd:COG1132 305 QRALASAERIFELLDeppeiPDPPGAVPLPPVRGEIEFENVS-F---SYPG----------------------------- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIK 503
Cdd:COG1132 352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIR 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFGV-SYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:COG1132 432 ENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTET 511
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 90421313 583 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:COG1132 512 EALIQEA-LERLMKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1204-1426 |
2.72e-58 |
|
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: 199.95 E-value: 2.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1204 WPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQW 1282
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1283 RKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVadevgLRsvieqfpgkldfvLVDGGCVLSHGHKQLMCLARSVLS 1362
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGA-----LR-------------VSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1363 KAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDS 1426
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
997-1433 |
1.20e-57 |
|
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: 210.00 E-value: 1.20e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 997 LLLIVIGAIAVVAVLqpyIFVATVPVIVAFIMLRAYFLQTSQQlKQLESEGR-SpifTHLVTSLKGLWTLRAFGRQP-YF 1074
Cdd:COG4988 148 LILVAVFPLDWLSGL---ILLVTAPLIPLFMILVGKGAAKASR-RQWRALARlS---GHFLDRLRGLTTLKLFGRAKaEA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1075 ETLFHKALNLHTAnwflylsTLRwfQMRI--------EMIFV--IFFIAVTFISILTTGEGEGRVGI-ILTLA------M 1137
Cdd:COG4988 221 ERIAEASEDFRKR-------TMK--VLRVaflssavlEFFASlsIALVAVYIGFRLLGGSLTLFAALfVLLLApefflpL 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1138 NIMSTlQW-----AVNSSidvdslmrsvSRVFKFIDMPTEGKPTKSTKPykngqlskvmiienshvkkddIWPSGGQMTV 1212
Cdd:COG4988 292 RDLGS-FYharanGIAAA----------EKIFALLDAPEPAAPAGTAPL---------------------PAAGPPSIEL 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQWRKAFGVIPQ 1291
Cdd:COG4988 340 EDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILINGVDLSDLDPASWRRQIAWVPQ 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1292 KVFIFSGTFRKNLDPYE-QWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 1370
Cdd:COG4988 419 NPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLD 498
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1371 EPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNE 1433
Cdd:COG4988 499 EPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1210-1420 |
1.78e-53 |
|
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: 184.51 E-value: 1.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYdPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSGTFRKNLdpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1369 LDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENK 1420
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
864-1163 |
7.22e-53 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 187.67 E-value: 7.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 864 IWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSyaviitsTSSYYVfYIYVGVADTLLAMGFFRGLPLVHTLIT 943
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSALPPSEV-------SVLYYL-GIYALISLLSVLLGTLRYLLFFFGSLR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 944 VSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVI 1023
Cdd:cd18604 74 ASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1024 VAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRI 1103
Cdd:cd18604 154 ALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRAFGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1104 EMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18604 234 DLLGALFSFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLVRSYNELELDMNSVERI 293
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
909-1163 |
1.51e-51 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 183.83 E-value: 1.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 909 STSSYYVFYIYVGVADTLLAMGFFrgLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLP 988
Cdd:cd18606 33 SQGFYIGIYAGLGVLQAIFLFLFG--LLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 989 LTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAF 1068
Cdd:cd18606 111 DSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1069 GRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMI--FVIFFIAVtFISILTTGEGEGRVGIILTLAMNIMSTLQWA 1146
Cdd:cd18606 191 GAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLgsLLVLIVAL-LCVTRRFSISPSSTGLVLSYVLQITQVLSWL 269
|
250
....*....|....*..
gi 90421313 1147 VNSSIDVDSLMRSVSRV 1163
Cdd:cd18606 270 VRQFAEVENNMNSVERL 286
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
859-1163 |
2.48e-51 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 183.45 E-value: 2.48e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 859 LIFVLIWCLVIFLAEVAASLvvlWL--LGNTPLQDKGNSTHSRNN---SYAVIITSTSsyyvfyIYVGVADTLLAMGFfr 933
Cdd:cd18603 1 SLLILLLYLLSQAFSVGSNI---WLseWSDDPALNGTQDTEQRDYrlgVYGALGLGQA------IFVFLGSLALALGC-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 934 glplvhtlITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQP 1013
Cdd:cd18603 70 --------VRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1014 YIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYL 1093
Cdd:cd18603 142 IFLVVIIPLAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSI 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1094 STLRWFQMRIEMI--FVIFF---IAVTFISILTTGEgegrVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18603 222 VSNRWLAVRLEFLgnLIVLFaalFAVLSRDSLSPGL----VGLSISYALQITQTLNWLVRMTSELETNIVSVERI 292
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1207-1437 |
1.87e-50 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 179.33 E-value: 1.87e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1207 GGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEIQIDGVSWDSITLQQWRKA 1285
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1365
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1366 ILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLL-NERSLF 1437
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVF 249
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
862-1147 |
1.95e-49 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 177.06 E-value: 1.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 862 VLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNnsyaviitsTSSYYVFYIYVGVADTLLAMGFFRGLplVHTL 941
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQA---------LNVYSLALLLLGLAQFILSFLQSYLL--NHTG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 942 ITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVP 1021
Cdd:pfam00664 70 ERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1022 VIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQM 1101
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 90421313 1102 RIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMnIMSTLQWAV 1147
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLS-LFAQLFGPL 274
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
865-1163 |
2.10e-49 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 178.18 E-value: 2.10e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 865 WCLVIFLAEVAASLVV---LWLlgnTPLQDKGNSTHSRNNSYAVIITSTSSY-YVFYIYVGVADTLLAMGFFRGLPLVHT 940
Cdd:cd18602 1 VALVLALALLKQGLRVatdFWL---ADWTEANHDVASVVFNITSSSLEDDEVsYYISVYAGLSLGAVILSLVTNLAGELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 941 LITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATV 1020
Cdd:cd18602 78 GLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYFLIALI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1021 PVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQ 1100
Cdd:cd18602 158 PIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAFRQQARFTQQMLELIDRNNTAFLFLNTANRWLG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1101 MRIEMI-FVIFFIAvTFISILTTGEGE---GRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRV 1163
Cdd:cd18602 238 IRLDYLgAVIVFLA-ALSSLTAALAGYispSLVGLAITYALLVPIYLNWVVRNLADVEMQMNSVERV 303
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
860-1167 |
5.48e-47 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 171.59 E-value: 5.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 860 IFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSThSRNNSYAVIITSTSSYYVFYIYVGV-ADTLLAM---GFFRGL 935
Cdd:cd18599 2 YVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTT-NNVDNSTVDSGNISDNPDLNFYQLVyGGSILVIlllSLIRGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 936 PLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYI 1015
Cdd:cd18599 81 VFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPWF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1016 FVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLST 1095
Cdd:cd18599 161 LIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNCA 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1096 LRWFQMRIEMIFVIFFIAVTFISILTTGE-GEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFI 1167
Cdd:cd18599 241 MRWLAVRLDILAVLITLITALLVVLLKGSiSPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
123-640 |
6.15e-47 |
|
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: 181.19 E-value: 6.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 123 LGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLS--NNLNKFDEGLALAhf 200
Cdd:COG2274 198 LAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRdvESIREFLTGSLLT-- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 201 VWIAPLQVALLMGLI----WELlqasAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYC 276
Cdd:COG2274 276 ALLDLLFVLIFLIVLffysPPL----ALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALG 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 277 WEEAMekmienLRQTElKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGI----ILRKIFTT---ISFCIVLRMA 349
Cdd:COG2274 352 AESRF------RRRWE-NLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLgaylVIDGQLTLgqlIAFNILSGRF 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 350 VTR--QFPWAVQTWYDSLGAINKIQDFLQK-----QEYKTLEYNLTTTEVVMENVTafweegfgelfekakqnnnnrkts 422
Cdd:COG2274 425 LAPvaQLIGLLQRFQDAKIALERLDDILDLppereEGRSKLSLPRLKGDIELENVS------------------------ 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 423 ngddslfFSnFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RIS 489
Cdd:COG2274 481 -------FR-YPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidpaslrrQIG 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 490 FCSQFSWIMPGTIKENIIFG---VSYDEyryrsVIKACQ---LEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVY 563
Cdd:COG2274 553 VVLQDVFLFSGTIRENITLGdpdATDEE-----IIEAARlagLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALL 627
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 564 KDADLYLLDSPFGYLDVLTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDF 640
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLY 703
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
437-623 |
8.12e-44 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 159.03 E-value: 8.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI-----------------KHSGRISFCSQFSWIMP 499
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 90421313 580 VLTEKEIFESCVCKLMAN--KTRILVTSKMEHLKKADKILILHEGS 623
Cdd:cd03290 173 IHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
437-622 |
9.74e-44 |
|
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: 156.77 E-value: 9.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIK 503
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIifgvsydeyryrsvikacqleediskfaekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03228 94 ENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 90421313 584 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03228 133 ALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
967-1403 |
1.05e-43 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 167.92 E-value: 1.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 967 LKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQ-PYIFVATVPVIVAFIMLRAYFLQTSQQLKQLES 1045
Cdd:TIGR02868 107 LRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSvPAALILAAGLLLAGFVAPLVSLRAARAAEQALA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1046 EGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKA-LNLHTAN----WFLYLSTlrwfqmriemIFVIFFIAVTFISIL 1120
Cdd:TIGR02868 187 RLRGELAAQLTDALDGAAELVASGALPAALAQVEEAdRELTRAErraaAATALGA----------ALTLLAAGLAVLGAL 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1121 TTGEG---EGRVG-------IILTLAM-NIMSTLQWAVNSsidVDSLMRSVSRVFKFIDMPTEGKptkstkpykngqlsk 1189
Cdd:TIGR02868 257 WAGGPavaDGRLApvtlavlVLLPLAAfEAFAALPAAAQQ---LTRVRAAAERIVEVLDAAGPVA--------------- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1190 vmiiENSHVKKDDIWPSGGQMTVKDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEIQ 1268
Cdd:TIGR02868 319 ----EGSAPAAGAVGLGKPTLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPlQGEVT 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1269 IDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLS 1347
Cdd:TIGR02868 394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRlARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1348 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHR 1403
Cdd:TIGR02868 474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1221-1431 |
4.32e-43 |
|
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: 157.00 E-value: 4.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1221 EGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGT 1299
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1300 FRKNL---DPYEQwsDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 1376
Cdd:cd03254 93 IMENIrlgRPNAT--DEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1377 DPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLL 1431
Cdd:cd03254 171 DTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
410-638 |
1.36e-42 |
|
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: 165.32 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 410 EKAKQNNNNRKTSNGDDSLFFSNFSLL---GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG 486
Cdd:COG4988 319 EPAAPAGTAPLPAAGPPSIELEDVSFSypgGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 487 -------------RISFCSQFSWIMPGTIKENIIFG-VSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQ 552
Cdd:COG4988 399 vdlsdldpaswrrQIAWVPQNPYLFAGTIRENLRLGrPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 553 RARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSE 632
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEE 557
|
....*.
gi 90421313 633 LQNLQP 638
Cdd:COG4988 558 LLAKNG 563
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
862-1167 |
6.89e-42 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 156.15 E-value: 6.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 862 VLIWCLVIFLAEVAASLVVLWLlgntplqdKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAmgFFRGLPLVHTL 941
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWL--------SYWVSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFT--LLRAFLFAYGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 942 ITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVP 1021
Cdd:cd18605 71 LRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1022 VIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQM 1101
Cdd:cd18605 151 LAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1102 RIEMIFVIFFIAVTFISILTTGEGE----GRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFI 1167
Cdd:cd18605 231 RLQLLGVLIVTFVALTAVVQHFFGLsidaGLIGLALSYALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
85-371 |
1.32e-41 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350041 [Multi-domain] Cd Length: 293 Bit Score: 155.30 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 85 GIFLYLGEVTKAVQPLLLGRII----ASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLI 160
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLInfveDAYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMG-LIWeLLQASAFCGLGFLIVLALFQAG 239
Cdd:cd18597 83 YRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIAlLIV-NLGPSALVGIGVLILSIPLQGF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 240 LGRMMMKYRdQRAGKIS-ERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVV 318
Cdd:cd18597 162 LMKKLFKLR-KKANKITdKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLAS 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 319 FLSVLPYALIKGiILR--KIFTTISFCIVLRMAVTrQFPWAVQTWYDSLGAINKI 371
Cdd:cd18597 241 MLSFITYYATGH-TLDpaNIFSSLALFNVLRMPLM-FLPLALSSLADALVALKRI 293
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
996-1416 |
1.74e-40 |
|
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: 158.22 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 996 QLLLIVIGAIAVVAVLQPY------IFVATVPVIVAFIMLRAYFLQTSQQlKQLESEGRspIFTHLVTSLKGLWTLRAFG 1069
Cdd:TIGR02857 124 QLVLAVIVPLAILAAVFPQdwisglILLLTAPLIPIFMILIGWAAQAAAR-KQWAALSR--LSGHFLDRLRGLPTLKLFG 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1070 RQ-PYFETLFHKALNLHTANwflyLSTLRwfqMRIEMIFVI-FF----IAVTFISI---LTTGEGEGRVGI-ILTLAMNI 1139
Cdd:TIGR02857 201 RAkAQAAAIRRSSEEYRERT----MRVLR---IAFLSSAVLeLFatlsVALVAVYIgfrLLAGDLDLATGLfVLLLAPEF 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1140 MSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTegKPTkstkpykngqlskvmiiensHVKKDDIWPSGGQMTVKDLTAKY 1219
Cdd:TIGR02857 274 YLPLRQLGAQYHARADGVAAAEALFAVLDAAP--RPL--------------------AGKAPVTAAPASSLEFSGVSVAY 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1220 tEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSG 1298
Cdd:TIGR02857 332 -PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1299 TFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAH 1375
Cdd:TIGR02857 411 TIAENIrlaRPDA--SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 90421313 1376 LDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVI 1416
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1211-1439 |
2.28e-39 |
|
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: 146.61 E-value: 2.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVI 1289
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKI 1366
Cdd:cd03251 82 SQDVFLFNDTVAENIaygRPGA--TREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1367 LLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1208-1421 |
2.71e-39 |
|
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: 145.81 E-value: 2.71e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK 1363
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLA--DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1364 AKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIeAMLE-CQQFLVIEENKV 1421
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDlVDRIIVMDSGRI 216
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1227-1374 |
4.15e-39 |
|
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: 142.79 E-value: 4.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSG-TFRKNL 1304
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1305 -------DPYEQWSDQEIWKVADEVGLrsvieqfPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSA 1374
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1205-1439 |
4.87e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 154.98 E-value: 4.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1205 PSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSaflrLLN-----TEGEIQIDGVSWDSITL 1279
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQ----LLTrawdpQQGEILLNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1280 QQWRKAFGVIPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGkLDFVLVDGGCVLSHGHKQLMCL 1356
Cdd:PRK11160 410 AALRQAISVVSQRVHLFSATLRDNLllaAP--NASDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSL 1436
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGR 566
|
...
gi 90421313 1437 FRQ 1439
Cdd:PRK11160 567 YYQ 569
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1213-1439 |
1.49e-38 |
|
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: 144.30 E-value: 1.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQ 1291
Cdd:cd03253 4 ENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDvSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1292 KVFIFSGTFRKNLDpYEQW--SDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd03253 83 DTVLFNDTIGYNIR-YGRPdaTDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1370 DEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAE 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
437-633 |
1.26e-37 |
|
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: 141.59 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIK 503
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdisrkslrsMIGVVLQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFGVSY--DEyryrSVIKAC---QLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:cd03254 95 ENIRLGRPNatDE----EVIEAAkeaGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 579 DVLTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03254 171 DTETEKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
76-303 |
2.50e-37 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350039 [Multi-domain] Cd Length: 290 Bit Score: 142.61 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 76 CFFWRFmFYGIFLYlgevtkaVQPLLLGRIIaSYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIA 155
Cdd:cd18595 2 AALLKL-LSDILLF-------ASPQLLKLLI-NFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 156 MFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVL-- 233
Cdd:cd18595 73 LTSAIYRKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLip 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 234 -----ALFQAGLGRMMMKYRDqragkisERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVR 303
Cdd:cd18595 153 lnavlARKIKKLQVKQMKLKD-------ERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLN 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
437-640 |
4.29e-37 |
|
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: 148.76 E-value: 4.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIK 503
Cdd:COG4987 347 GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlrrRIAVVPQRPHLFDTTLR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFG---VSyDEyRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:COG4987 427 ENLRLArpdAT-DE-ELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDA 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 581 LTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDF 640
Cdd:COG4987 505 ATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
81-303 |
1.08e-36 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 140.47 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 81 FMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLI 160
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 161 YKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVAL-LMGLIWELLQASAFCGLGFLIVLALFQAG 239
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVgGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 240 LGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVR 303
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVAN 224
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
437-633 |
8.62e-36 |
|
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: 136.21 E-value: 8.62e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-------------ISFCSQFSWIMPGTIK 503
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFGVS-YDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03251 94 ENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 583 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03251 174 ERLVQAA-LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1223-1439 |
4.11e-35 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 143.06 E-value: 4.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1223 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRK 1302
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1303 NL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPV 1379
Cdd:PRK11174 442 NVllgNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1380 TYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFAT 579
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1212-1420 |
2.26e-33 |
|
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: 128.74 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIP 1290
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 Q--KVFIFSGTFR-------KNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLArSVL 1361
Cdd:cd03225 82 QnpDDQFFGPTVEeevafglENLGLPEEEIEERVEEALELVGLEGLRDRSPFT-----------LSGGQKQRVAIA-GVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1362 S-KAKILLLDEPSAHLDPVTYQIIRRTLKQaFADC--TVILCEHRIEAMLE-CQQFLVIEENK 1420
Cdd:cd03225 150 AmDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEgkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
951-1441 |
2.88e-33 |
|
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: 138.72 E-value: 2.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 951 KMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIaVVAVLQPYIFVATVPVIVAFIMLR 1030
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGL-FLVRQNMLLFLLSLLSIPVYAVII 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1031 AYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQpyfETLFHKalnlhtanwflylstlrwfqmrIEMIFVIF 1110
Cdd:TIGR01193 313 ILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSE---AERYSK----------------------IDSEFGDY 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1111 FIAVTFISILTTGEGEGRVGIILTLAMNIMST-LQWAVNSSIDVDSLMRSVSRVFKFIDmPTEG----KPTKSTKPYKNG 1185
Cdd:TIGR01193 368 LNKSFKYQKADQGQQAIKAVTKLILNVVILWTgAYLVMRGKLTLGQLITFNALLSYFLT-PLENiinlQPKLQAARVANN 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1186 QLSKVMIIENSHVKKDDIWPS---GGQMTVKDLTAKYTEGGNaILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN 1262
Cdd:TIGR01193 447 RLNEVYLVDSEFINKKKRTELnnlNGDIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQ 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1263 -TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNL--DPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVL 1339
Cdd:TIGR01193 526 aRSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTEL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1340 VDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQ-IIRRTLKqaFADCTVILCEHRIEAMLECQQFLVIEE 1418
Cdd:TIGR01193 606 SEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKkIVNNLLN--LQDKTIIFVAHRLSVAKQSDKIIVLDH 683
|
490 500
....*....|....*....|...
gi 90421313 1419 NKVRQYDSIQKLLNERSLFRQAI 1441
Cdd:TIGR01193 684 GKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1211-1439 |
3.47e-33 |
|
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: 128.81 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKY-TEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:cd03249 2 EFKNVSFRYpSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSGTFRKNL---DPYEqwSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1365
Cdd:cd03249 82 VSQEPVLFDGTIAENIrygKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1366 ILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
427-619 |
6.01e-33 |
|
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: 135.49 E-value: 6.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 427 SLFFSNFSLL---GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISF 490
Cdd:TIGR02857 321 SLEFSGVSVAypgRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 491 CSQFSWIMPGTIKENIIFGVSY-DEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLY 569
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90421313 570 LLDSPFGYLDVLTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILIL 619
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
441-575 |
6.44e-33 |
|
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: 125.07 E-value: 6.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK-------------HSGRISFCSQFSWIMPG-TIKENI 506
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 507 IFGVsyDEYRYRSVIKACQLEEDISKFAEKD--NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1212-1439 |
7.29e-33 |
|
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: 127.83 E-value: 7.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:COG1122 3 LENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTL----LRLLNgllkpTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVipqkVF------IFSGTFR-------KNLdpyeQWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHG 1349
Cdd:COG1122 78 GL----VFqnpddqLFAPTVEedvafgpENL----GLPREEIRERVEEalelVGLEHLADRPPHE-----------LSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1350 HKQLMCLArSVLS-KAKILLLDEPSAHLDPVTYQIIRRTLKQ-AFADCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDS 1426
Cdd:COG1122 139 QKQRVAIA-GVLAmEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
|
250
....*....|...
gi 90421313 1427 IQKLLNERSLFRQ 1439
Cdd:COG1122 218 PREVFSDYELLEE 230
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1210-1439 |
1.03e-32 |
|
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: 127.60 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1365
Cdd:cd03252 81 VLQENVLFNRSIRDNIalaDP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1366 ILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1211-1420 |
3.31e-32 |
|
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: 123.12 E-value: 3.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVI 1289
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQkvfifsgtfrknldpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd00267 79 PQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1370 DEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRIE-AMLECQQFLVIEENK 1420
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPElAELAADRVIVLKDGK 157
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
437-633 |
1.10e-31 |
|
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: 124.65 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK-----------HSGR--ISFCSQFSWIMPGTIK 503
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevtlDSLRraIGVVPQDTVLFNDTIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFG-VSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03253 93 YNIRYGrPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 583 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03253 173 EREIQAA-LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1212-1421 |
1.35e-31 |
|
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: 121.94 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIP 1290
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSGTFRKNldpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLD 1370
Cdd:cd03246 83 QDDELFSGSIAEN-----------------------------------------ILSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1371 EPSAHLDPVTYQIIRRTLKQA-FADCTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1211-1433 |
1.64e-31 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 124.02 E-value: 1.64e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSiTLQQWRKAFGVI 1289
Cdd:COG1131 2 EVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQKVFIFSG-TFRKNLD--------PYEQwSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSV 1360
Cdd:COG1131 79 PQEPALYPDlTVRENLRffarlyglPRKE-ARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1361 LSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRI-EAMLECQQFLVIEENKVRQYDSIQKLLNE 1433
Cdd:COG1131 147 LHDPELLILDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLeEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1210-1421 |
2.74e-31 |
|
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: 121.27 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSwDSITLQQWRKAFGV 1288
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKpQQGEITLDGVP-VSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSGTFRKNLdpyeqwsdqeiwkvadevGLRsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:cd03247 80 LNQRPYLFDTTLRNNL------------------GRR--------------------FSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1369 LDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1211-1421 |
4.07e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 119.15 E-value: 4.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTakYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQWRKAFGVI 1289
Cdd:COG4619 2 ELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDpPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQKVFIFSGTFRKNLDPYEQWSDQEIwkvaDEVGLRSVIEQFpgKLDFVLVDGGCV-LSHGHKQLMCLARSVLSKAKILL 1368
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRERKF----DRERALELLERL--GLPPDILDKPVErLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1369 LDEPSAHLDPVTYQIIRRTLKQAFADC--TVILCEH-RIEAMLECQQFLVIEENKV 1421
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEgrAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
433-641 |
1.20e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 126.11 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELePSEGKIKHSG-------------RISFCSQFSWIMP 499
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldpeswrkHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIFG-VSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK11174 437 GTLRDNVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 579 DVLTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFS 641
Cdd:PRK11174 517 DAHSEQLVMQA-LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA 578
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
439-622 |
2.11e-29 |
|
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: 117.59 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKEN 505
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIRSN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 I-IFGVSYDEYRYRsVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 584
Cdd:cd03244 98 LdPFGEYSDEELWQ-ALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDA 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 90421313 585 EIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03244 177 LIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKG 213
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
432-619 |
2.27e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 117.25 E-value: 2.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--------RISFCSQ---FSWIMPG 500
Cdd:cd03235 6 TVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQrrsIDRDFPI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKE--------NIIFGVSYDEYRYRSVIKAcqLEE-DISKFAEKDnivLGEggitLSGGQRARISLARAVYKDADLYLL 571
Cdd:cd03235 86 SVRDvvlmglygHKGLFRRLSKADKAKVDEA--LERvGLSELADRQ---IGE----LSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90421313 572 DSPFGYLDVLTEKEIFEsCVCKL-MANKTRILVTSKMEH-LKKADKILIL 619
Cdd:cd03235 157 DEPFAGVDPKTQEDIYE-LLRELrREGMTILVVTHDLGLvLEYFDRVLLL 205
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1208-1439 |
2.86e-29 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 125.13 E-value: 2.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSGTFRKNLdPY---EQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK 1363
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNI-AYartEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRD 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1364 AKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:PRK11176 499 SPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQ 574
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
439-622 |
3.06e-29 |
|
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: 115.39 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFcsqfswimpgtikeniifgvSYDEYRYR 518
Cdd:cd03246 16 PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADIS--------------------QWDPNELG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 519 SVIKAcqLEEDISKFAE--KDNIvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMA 596
Cdd:cd03246 76 DHVGY--LPQDDELFSGsiAENI--------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAA 145
|
170 180
....*....|....*....|....*.
gi 90421313 597 NKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03246 146 GATRIVIAHRPETLASADRILVLEDG 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1211-1435 |
4.32e-29 |
|
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: 117.27 E-value: 4.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQqWRKAFGVI 1289
Cdd:COG4555 3 EVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKpDSGSILIDGEDVRKEPRE-ARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQKVFIFSG-TFRKNLDPY-EQW--SDQEIWKVADEV----GLRSVIEQfpgkldfvLVDGgcvLSHGHKQLMCLARSVL 1361
Cdd:COG4555 80 PDERGLYDRlTVRENIRYFaELYglFDEELKKRIEELiellGLEEFLDR--------RVGE---LSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1362 SKAKILLLDEPSAHLDPVTYQIIRRTLKQAFA-DCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQKLLNERS 1435
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
859-1439 |
6.82e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 124.83 E-value: 6.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 859 LIFVLIWCLVIFLAEVA----ASLVVLWLLgntplQDKGNSTHSRNNSYAVIITSTSSyyvfyiyvgvadtllAMGFFRG 934
Cdd:TIGR00958 163 LISAFVFLTLSSLGEMFipfyTGRVIDTLG-----GDKGPPALASAIFFMCLLSIASS---------------VSAGLRG 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 935 LPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPY 1014
Cdd:TIGR00958 223 GSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1015 I----FVATVPVIVAFIMLRAYFLQTSQQLKqlESEGRSpifTHLV-TSLKGLWTLRAFGRQPYFETLFHKALN-LHTAN 1088
Cdd:TIGR00958 303 LtmvtLINLPLVFLAEKVFGKRYQLLSEELQ--EAVAKA---NQVAeEALSGMRTVRSFAAEEGEASRFKEALEeTLQLN 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1089 W------FLYLSTLRWFQMRIEMIfvIFFIAVTFIsilTTGEGEGrvGIILTLAMNIMSTLQWAVNSSIDVDSLMRSV-- 1160
Cdd:TIGR00958 378 KrkalayAGYLWTTSVLGMLIQVL--VLYYGGQLV---LTGKVSS--GNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVga 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1161 -SRVFKFIDMPTEGKPTKSTKPykngqlskvmiienSHVKkddiwpsgGQMTVKDLTAKY-TEGGNAILENISFSISPGQ 1238
Cdd:TIGR00958 451 sEKVFEYLDRKPNIPLTGTLAP--------------LNLE--------GLIEFQDVSFSYpNRPDVPVLKGLTFTLHPGE 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1239 RVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKN----LDPYEqwsDQ 1313
Cdd:TIGR00958 509 VVALVGPSGSGKSTVAALLQNLYQpTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENiaygLTDTP---DE 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1314 EIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVtyqiIRRTLKQ--A 1391
Cdd:TIGR00958 586 EIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE----CEQLLQEsrS 661
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 90421313 1392 FADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:TIGR00958 662 RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
438-622 |
9.93e-29 |
|
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: 115.38 E-value: 9.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKE 504
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFGVSY-DEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03245 97 NITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 90421313 584 KEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03245 177 ERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1212-1421 |
1.49e-28 |
|
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: 113.26 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLqQWRKAFGVIP 1290
Cdd:cd03230 3 VRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkPDSGEIKVLGKDIKKEPE-EVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSG-TFRKNLDpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd03230 80 EEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1370 DEPSAHLDPVTYQIIRRTLKQ-AFADCTVILCEHRIEAMLE-CQQFLVIEENKV 1421
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1208-1424 |
3.26e-28 |
|
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: 121.39 E-value: 3.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRLL-----NTEGEIQIDGVswdsiTLQQW 1282
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLvgvwpPTAGSVRLDGA-----DLSQW 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1283 RKA-----FGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLA 1357
Cdd:COG4618 400 DREelgrhIGYLPQDVELFDGTIAENIARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLA 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1358 RSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRIEAMLECQQFLVIEENKVRQY 1424
Cdd:COG4618 480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLAAVDKLLVLRDGRVQAF 547
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1201-1439 |
3.32e-28 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 121.75 E-value: 3.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1201 DDIWP-SGGQMTVKDLTAKYTEGgNAILENISFSISPGQRVGLLGRTGSGKSTLLSaflrLLN-----TEGEIQIDGVSW 1274
Cdd:PRK10790 331 NDDRPlQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLAS----LLMgyyplTEGEIRLDGRPL 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1275 DSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLM 1354
Cdd:PRK10790 406 SSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLL 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1355 CLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNER 1434
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
....*
gi 90421313 1435 SLFRQ 1439
Cdd:PRK10790 566 GRYWQ 570
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1211-1421 |
4.02e-28 |
|
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: 112.53 E-value: 4.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVI 1289
Cdd:cd03214 1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQkvfifsgtfrknldpyeqwsdqeiwkVADEVGLRSVIEQFpgkldfvlVDggcVLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd03214 79 PQ--------------------------ALELLGLAHLADRP--------FN---ELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1370 DEPSAHLDPvTYQI----IRRTLKQAFaDCTVILCEHRIE-AMLECQQFLVIEENKV 1421
Cdd:cd03214 122 DEPTSHLDI-AHQIelleLLRRLARER-GKTVVMVLHDLNlAARYADRVILLKDGRI 176
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
85-294 |
4.69e-28 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350042 [Multi-domain] Cd Length: 288 Bit Score: 115.73 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 85 GIFLYLGEVTKAVQPLLLGRIIaSYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKT 164
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLV-EFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 165 LKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQ------- 237
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINkwiakri 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 238 AGLGRMMMKYRDQRAGkiserlvITSEMIENIQSVKAYCWEEAMEKMIENLRQTELK 294
Cdd:cd18598 162 GALSEKMMKHKDARVK-------LMTEILSGIRVIKLLAWERIFKQKIEELRAKELK 211
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1212-1420 |
5.14e-28 |
|
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: 112.95 E-value: 5.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEG---GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGEIQ-IDGVSwdsitlqQWRKAFG 1287
Cdd:cd03250 3 VEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL------GELEkLSGSV-------SVPGSIA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSGTFRKNL---DPYEQwsdQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 1364
Cdd:cd03250 70 YVSQEPWIQNGTIRENIlfgKPFDE---ERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1365 KILLLDEPSAHLDP-VTYQIIRRTLKQAFADC-TVILCEHRIEAMLECQQFLVIEENK 1420
Cdd:cd03250 147 DIYLLDDPLSAVDAhVGRHIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
433-648 |
6.39e-28 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 114.03 E-value: 6.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--------RISFCSQ---FSWIMPGT 501
Cdd:COG1121 14 VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYVPQraeVDWDFPIT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKENIIFGvsydeyRY-------------RSVIKACqLEE-DISKFAEKDnivLGEggitLSGGQRARISLARAVYKDAD 567
Cdd:COG1121 94 VRDVVLMG------RYgrrglfrrpsradREAVDEA-LERvGLEDLADRP---IGE----LSGGQQQRVLLARALAQDPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 568 LYLLDSPFGYLDVLTEKEIFEscvckLMA-----NKTRILVTskmeH-----LKKADKILILHEGsSYFYGTFSELqnLQ 637
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYE-----LLRelrreGKTILVVT----HdlgavREYFDRVLLLNRG-LVAHGPPEEV--LT 227
|
250
....*....|.
gi 90421313 638 PDFSSKLMGCD 648
Cdd:COG1121 228 PENLSRAYGGP 238
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1210-1436 |
8.63e-28 |
|
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: 113.99 E-value: 8.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFI-FSGTFRK--------NLDPYEQWSDQE---IWKVADEVGL-----RSVIEqfpgkldfvlvdggcvLSHGHK 1351
Cdd:COG1120 80 VPQEPPApFGLTVRElvalgrypHLGLFGRPSAEDreaVEEALERTGLehladRPVDE----------------LSGGER 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1352 QLMCLARSVLSKAKILLLDEPSAHLDPvTYQI-IRRTLKQ--AFADCTVILCEHRIE-AMLECQQFLVIEENKVRQYDSI 1427
Cdd:COG1120 144 QRVLIARALAQEPPLLLLDEPTSHLDL-AHQLeVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPP 222
|
....*....
gi 90421313 1428 QKLLNERSL 1436
Cdd:COG1120 223 EEVLTPELL 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
439-633 |
2.00e-27 |
|
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: 112.25 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI-------------KHSGRISFCSQFSWIMPGTIKEN 505
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVSQEPVLFDGTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFG-----VSYDEyryrSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03249 97 IRYGkpdatDEEVE----EAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 581 LTEKEIFESCVcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03249 173 ESEKLVQEALD-RAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
437-604 |
2.11e-27 |
|
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: 118.62 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIK 503
Cdd:TIGR02868 347 APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQDAHLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFG---VSYDEYRyrSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:TIGR02868 427 ENLRLArpdATDEELW--AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....
gi 90421313 581 LTEKEIFEScVCKLMANKTRILVT 604
Cdd:TIGR02868 505 ETADELLED-LLAALSGRTVVLIT 527
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1208-1438 |
3.80e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 118.28 E-value: 3.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:PRK10789 312 GELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSGTFRKNL---DPyeQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK 1363
Cdd:PRK10789 392 AVVSQTPFLFSDTVANNIalgRP--DATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1364 AKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFR 1438
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYR 544
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
432-622 |
3.20e-26 |
|
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: 106.18 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIkhsgrisfcsqfswimpgTIKENIIFGVS 511
Cdd:cd00267 6 SFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI------------------LIDGKDIAKLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 512 YDEYRYRSVIKACqleediskfaekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCV 591
Cdd:cd00267 68 LEELRRRIGYVPQ-----------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180 190
....*....|....*....|....*....|..
gi 90421313 592 CKLMANKTRILVTSKMEHLKKA-DKILILHEG 622
Cdd:cd00267 125 ELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
437-633 |
3.57e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 108.61 E-value: 3.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPG-TIK 503
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENI-----IFGVSYDEY--RYRSVIKACQLEEDISKFAEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:COG1131 92 ENLrffarLYGLPRKEAreRIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 577 YLDVLTEKEIFEsCVCKLMANKTRILVTSkmeHL-----KKADKILILHEGSSYFYGTFSEL 633
Cdd:COG1131 161 GLDPEARRELWE-LLRELAAEGKTVLLST---HYleeaeRLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
85-350 |
1.71e-25 |
|
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 1 (TMD1) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and they belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350035 [Multi-domain] Cd Length: 309 Bit Score: 108.86 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 85 GIFLYLGEVTKAVQPLLLGRII-----ASYDPDNKEERSIAIYL--------GIGLCLLFIVRTLLLHPAIFGLHHI--- 148
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVdyveeNTYSSSNSTDKLSVSYVtveeffsnGYVLAVILFLALLLQATFSQASYHIvir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 149 -GMQMRIAMFSLIYKKTLKLSSRVLD--KISIGQLVSLLS---NNLNKFdegLALAHFVWIAPLQVALLMGLIWELLQAS 222
Cdd:cd18591 83 eGIRLKTALQAMIYEKALRLSSWNLSsgSMTIGQITNHMSedaNNIMFF---FWLIHYLWAIPLKIIVGLILLYLKLGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 223 AFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYV 302
Cdd:cd18591 160 ALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 303 RYFNSSAFFFSGFFVVFLSVLPYALIKGIILR--KIFTTIS-----------FCIVLRMAV 350
Cdd:cd18591 240 WSLMTFLTQASPILVTLVTFGLYPYLEGEPLTaaKAFSSLAlfnqltvplfiFPVVIPILI 300
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1212-1432 |
2.14e-25 |
|
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: 106.43 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSIT---LQQWRKAFG 1287
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpDSGEVLIDGEDISGLSeaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSG-TFRKN----LDPYEQWSDQEIWKVA----DEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1358
Cdd:cd03261 81 MLFQSGALFDSlTVFENvafpLREHTRLSEEEIREIVleklEAVGLRGAEDLYPAE-----------LSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVT-YQIIR--RTLKQAFaDCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQKLLN 1432
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIAsGVIDDliRSLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
437-622 |
2.31e-25 |
|
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: 112.53 E-value: 2.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI----------------KHSG----RISFcsqfsw 496
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVrldgadlsqwdreelgRHIGylpqDVEL------ 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 497 iMPGTIKENII-FGVSYDEyryrSVIKACQL---EEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG4618 418 -FDGTIAENIArFGDADPE----KVVAAAKLagvHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 573 SPFGYLDVLTEKeifescvcKLMA--------NKTRILVTSKMEHLKKADKILILHEG 622
Cdd:COG4618 493 EPNSNLDDEGEA--------ALAAairalkarGATVVVITHRPSLLAAVDKLLVLRDG 542
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1226-1421 |
2.44e-25 |
|
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: 112.99 E-value: 2.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1226 ILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLL-----NTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTF 1300
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTL----ARLLfrfydVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1301 RKNLdPYEQW--SDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 1378
Cdd:COG5265 449 AYNI-AYGRPdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDS 527
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90421313 1379 VTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:COG5265 528 RTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1210-1425 |
5.64e-25 |
|
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: 104.52 E-value: 5.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSITLQqwRK 1284
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAglerpDSGEILIDGRDVTGVPPE--RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQK--------VF--IFSGtFRKNLDPYEQWSDQEIWkVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLM 1354
Cdd:cd03259 73 NIGMVFQDyalfphltVAenIAFG-LKLRGVPKAEIRARVRE-LLELVGLEGLLNRYPHE-----------LSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1355 CLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK--QAFADCTVILCEH-RIEAMLECQQFLVIEENKVRQYD 1425
Cdd:cd03259 140 ALARALAREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQVG 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1211-1421 |
9.42e-25 |
|
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: 110.38 E-value: 9.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL----NTEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggRISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQ---------KVF--IFSGTFRKNLDPYEQWsdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMC 1355
Cdd:COG1123 86 GMVFQdpmtqlnpvTVGdqIAEALENLGLSRAEAR--ARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1356 LARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK--QAFADCTVILCEHRIEAMLE-CQQFLVIEENKV 1421
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRI 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1211-1409 |
1.10e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.40 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSwdsitLQQWRKAFGVI 1289
Cdd:COG1121 8 ELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGKP-----PRRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQKV------------FIFSGTFRKNldPYEQWSDQEIWKVADEVgLRSV-IEQFPGKldfvlvdggCV--LSHGHKQLM 1354
Cdd:COG1121 81 PQRAevdwdfpitvrdVVLMGRYGRR--GLFRRPSRADREAVDEA-LERVgLEDLADR---------PIgeLSGGQQQRV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1355 CLARSVLSKAKILLLDEPSAHLDPVT----YQIIRRtLKQafADCTVILCEHRIEAMLE 1409
Cdd:COG1121 149 LLARALAQDPDLLLLDEPFAGVDAATeealYELLRE-LRR--EGKTILVVTHDLGAVRE 204
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1211-1416 |
1.25e-24 |
|
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: 103.74 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGG--NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSWDSITLQQ---WRK 1284
Cdd:cd03257 3 EVKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkPTSGSIIFDGKDLLKLSRRLrkiRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQKVF-----------IFSGTFRKNLDPYEQWSDQE-IWKVADEVGL-RSVIEQFPGKldfvlvdggcvLSHGHK 1351
Cdd:cd03257 83 EIQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEaVLLLLVGVGLpEEVLNRYPHE-----------LSGGQR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1352 QLMCLARSVLSKAKILLLDEPSAHLDPVT-YQIIR--RTLKQAFaDCTVILCEHRIEAMLE-CQQFLVI 1416
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVM 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
439-633 |
2.61e-24 |
|
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: 103.40 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPG-TIKEN 505
Cdd:COG4555 15 PALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkeprearrQIGVLPDERGLYDRlTVREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 I-----IFGVSYDEYRYR--SVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:COG4555 95 IryfaeLYGLFDEELKKRieELIELLGLEEFLDRRVGE-----------LSTGMKKKVALARALVHDPKVLLLDEPTNGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 579 DVLTeKEIFESCVCKLMANKTRILVTSK-MEHLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:COG4555 164 DVMA-RRLLREILRALKKEGKTVLFSSHiMQEVEAlCDRVVILHKGKVVAQGSLDEL 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
439-638 |
2.61e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.53 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-------------ISFCSQFSWIMPGTIKEN 505
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiadyseaalrqaISVVSQRVHLFSATLRDN 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFGV--SYDEyRYRSVIKACQLEedisKFAEKD---NIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK11160 434 LLLAApnASDE-ALIEVLQQVGLE----KLLEDDkglNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDA 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 581 LTEKEIFESCVcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQP 638
Cdd:PRK11160 509 ETERQILELLA-EHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
437-648 |
2.89e-24 |
|
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: 103.15 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPG-TI 502
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 503 KENI-----IFGVSYDEYRYRsvikACQLEE----DISKFAEKdniVLGEggitLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:cd03295 93 EENIalvpkLLKWPKEKIRER----ADELLAlvglDPAEFADR---YPHE----LSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 574 PFGYLDVLTEKEIFESCV-CKLMANKTRILVTSKM-EHLKKADKILILHEGSSYFYGTFSE-LQNLQPDFSSKLMGCD 648
Cdd:cd03295 162 PFGALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEiLRSPANDFVAEFVGAD 239
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1212-1432 |
2.96e-24 |
|
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: 103.14 E-value: 2.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSIT---LQQWRKAFG 1287
Cdd:COG1127 8 VRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpDSGEILVDGQDITGLSekeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VipqkVF----IFSG-TFRKN----LDPYEQWSDQEIWKVADE----VGLRSVIEQFPGKLdfvlvDGGcvlshghkqlM 1354
Cdd:COG1127 86 M----LFqggaLFDSlTVFENvafpLREHTDLSEAEIRELVLEklelVGLPGAADKMPSEL-----SGG----------M 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1355 C----LARSVLSKAKILLLDEPSAHLDPVT----YQIIRRtLKQAFaDCTVILCEHRIEAMLE-CQQFLVIEENKVRQYD 1425
Cdd:COG1127 147 RkrvaLARALALDPEILLYDEPTAGLDPITsaviDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*..
gi 90421313 1426 SIQKLLN 1432
Cdd:COG1127 225 TPEELLA 231
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-633 |
3.50e-24 |
|
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: 102.95 E-value: 3.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKENI 506
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 IFGvsyDE-YRYRSVIKACQL---EEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03252 97 ALA---DPgMSMERVIEAAKLagaHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 583 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03252 174 EHAIMRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
437-633 |
4.68e-24 |
|
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: 102.41 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFC-----SQFswIM 498
Cdd:COG1122 13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLVfqnpdDQL--FA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 499 PgTIKENIIFG-----VSYDEYRYRsVIKAcqLEE-DISKFAEKDnivlgeggI-TLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG1122 91 P-TVEEDVAFGpenlgLPREEIRER-VEEA--LELvGLEHLADRP--------PhELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 572 DSPFGYLDVLTEKEIFEsCVCKL-MANKTRILVTSKMEHL-KKADKILILHEGSSYFYGTFSEL 633
Cdd:COG1122 159 DEPTAGLDPRGRRELLE-LLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
438-628 |
8.19e-24 |
|
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: 100.08 E-value: 8.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPGTIKEN 505
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGvpvsdlekalssLISVLNQRPYLFDTTLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IifgvsydeyryrsvikacqleediskfaekdnivlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKE 585
Cdd:cd03247 95 L--------------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90421313 586 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYG 628
Cdd:cd03247 137 LLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
115-371 |
1.08e-23 |
|
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350036 [Multi-domain] Cd Length: 287 Bit Score: 103.02 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 115 EERSIAIYLGIGLCLLF----IVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSrvLDKISIGQLVSLLSNNLNK 190
Cdd:cd18592 29 EDSDSSVWYGILLVLGLflteLLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRS--LGDKSVGELINIFSNDGQR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 191 FDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRdQRAGKISERLV-ITSEMIENI 269
Cdd:cd18592 107 LFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFR-RKAIVITDKRVrLMNEILNSI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 270 QSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIIL-RKIFTTISFCIVLRM 348
Cdd:cd18592 186 KLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALGNDLTaAQAFTVIAVFNSMRF 265
|
250 260
....*....|....*....|...
gi 90421313 349 AVtRQFPWAVQTWYDSLGAINKI 371
Cdd:cd18592 266 SL-RMLPYAVKALAEAKVALQRI 287
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
392-1415 |
1.47e-23 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 108.96 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 392 VVMENVTAFWE--EGFGELFEKAK-----QNNNNRKTSNGDDSLFFSNFSL-----LGTPVLKDINFKIERGQLLAVAGS 459
Cdd:PTZ00265 340 IILPNITEYMKslEATNSLYEIINrkplvENNDDGKKLKDIKKIQFKNVRFhydtrKDVEIYKDLNFTLTEGKTYAFVGE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 460 TGAGKTSLLMVIMGELEPSEGKI----KHS----------GRISFCSQFSWIMPGTIKENIIFGV--------------- 510
Cdd:PTZ00265 420 SGCGKSTILKLIERLYDPTEGDIiindSHNlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealsnyyne 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 511 ----SYDEYRYR---------------------------------------SVIKACQLEEDISKFAEKDNIVLGEGGIT 547
Cdd:PTZ00265 500 dgndSQENKNKRnscrakcagdlndmsnttdsneliemrknyqtikdsevvDVSKKVLIHDFVSALPDKYETLVGSNASK 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 548 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKeIFESCVCKLMANKTRI--LVTSKMEHLKKADKILILhegSSY 625
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY-LVQKTINNLKGNENRItiIIAHRLSTIRYANTIFVL---SNR 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 626 FYGTFSELQNLQPDFSSKlmGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSwtetkkqsfKQTGEFGEKRKNSILNPI 705
Cdd:PTZ00265 656 ERGSTVDVDIIGEDPTKD--NKENNNKNNKDDNNNNNNNNNNKINNAGSYIIE---------QGTHDALMKNKNGIYYTM 724
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 706 NSIRKFSIVQKTPlqmNGIEEDSDepleRRLSLVPDSEQGEAilprisvistgptlqarrrqsvlnlmTHSVNqGQNIHR 785
Cdd:PTZ00265 725 INNQKVSSKKSSN---NDNDKDSD----MKSSAYKDSERGYD--------------------------PDEMN-GNSKHE 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 786 KTTASTRKVSLAPQANLTEldiysrrlsqetgleiseeiNEEDLKECFFDDM--ESIPAVTTWNTYLRYITVHKSLIfVL 863
Cdd:PTZ00265 771 NESASNKKSCKMSDENASE--------------------NNAGGKLPFLRNLfkRKPKAPNNLRIVYREIFSYKKDV-TI 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 864 IWCLVIFLAEVAASLVVLWLLGNTPLQDKGNsthsrnnsyaviITSTSSYYVFYIYVgvadtlLAMGFFRGLPL---VHT 940
Cdd:PTZ00265 830 IALSILVAGGLYPVFALLYAKYVSTLFDFAN------------LEANSNKYSLYILV------IAIAMFISETLknyYNN 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 941 LI--TVSKILHHKMLHSVLQAPMSTLNTLK-AGGILN-RFSKDIAILDDLLPLTIFDFIQLLLIVIgaiavVAVLQPYIF 1016
Cdd:PTZ00265 892 VIgeKVEKTMKRRLFENILYQEISFFDQDKhAPGLLSaHINRDVHLLKTGLVNNIVIFTHFIVLFL-----VSMVMSFYF 966
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1017 ---VATVPVIVAFIMLRAYF----LQTSQQLKQLESEGRSPIFTH-------------LVTSLKGLWTLRAFGRQPYFET 1076
Cdd:PTZ00265 967 cpiVAAVLTGTYFIFMRVFAirarLTANKDVEKKEINQPGTVFAYnsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCN 1046
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1077 LFHKALNLhtanwflylstlrwfqmriemifviffiavtfisiltTGEGEGRVGIILTLAMNIMSTLQWAVNS------- 1149
Cdd:PTZ00265 1047 LIEKAIDY-------------------------------------SNKGQKRKTLVNSMLWGFSQSAQLFINSfaywfgs 1089
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1150 ------SIDVDSLMRSVsrvFKFIDMPT-EGKPTKSTKPYKNGQLS----KVMIIENSHV-----------KKDDIwpsG 1207
Cdd:PTZ00265 1090 flirrgTILVDDFMKSL---FTFLFTGSyAGKLMSLKGDSENAKLSfekyYPLIIRKSNIdvrdnggirikNKNDI---K 1163
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNA-ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLR--------------------------- 1259
Cdd:PTZ00265 1164 GKIEIMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfknehtndmtneqdyq 1243
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1260 ----------------------------LLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLD-PYEQW 1310
Cdd:PTZ00265 1244 gdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKEDA 1323
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1311 SDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK- 1389
Cdd:PTZ00265 1324 TREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVd 1403
|
1210 1220
....*....|....*....|....*..
gi 90421313 1390 -QAFADCTVILCEHRIEAMLECQQFLV 1415
Cdd:PTZ00265 1404 iKDKADKTIITIAHRIASIKRSDKIVV 1430
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
437-622 |
1.79e-23 |
|
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: 100.29 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI-----------KHSGRISFCSQFSWIMPG-TIKE 504
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgrdvtgvpPERRNIGMVFQDYALFPHlTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFG-----VSYDEYRYR--SVIKACQLEEDISKFAEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03259 92 NIAFGlklrgVPKAEIRARvrELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPLSA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 578 LDV-LTE------KEIFESCvcklmaNKTRILVTSKM-EHLKKADKILILHEG 622
Cdd:cd03259 161 LDAkLREelreelKELQREL------GITTIYVTHDQeEALALADRIAVMNEG 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1212-1432 |
1.83e-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: 101.03 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEG--GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGvswDSITLQQWRKAFGV 1288
Cdd:COG1124 4 VRNLSVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLErPWSGEVTFDG---RPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IpQKVFifsgtfrknLDPY---------------------EQWSDQEIWKVADEVGL-RSVIEQFPGKldfvlvdggcvL 1346
Cdd:COG1124 81 V-QMVF---------QDPYaslhprhtvdrilaeplrihgLPDREERIAELLEQVGLpPSFLDRYPHQ-----------L 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTY-QIIR--RTLKQAFaDCTVILCEH---RIEAMleCQQFLVIEENK 1420
Cdd:COG1124 140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQaEILNllKDLREER-GLTYLFVSHdlaVVAHL--CDRVAVMQNGR 216
|
250
....*....|..
gi 90421313 1421 VRQYDSIQKLLN 1432
Cdd:COG1124 217 IVEELTVADLLA 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
438-622 |
2.90e-23 |
|
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: 99.46 E-value: 2.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI-------------KHSGRISFC-----SQFswIMP 499
Cdd:cd03225 14 RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVlvdgkdltklslkELRRKVGLVfqnpdDQF--FGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 gTIKENIIFGVsydEYRYRSvikacqlEEDIskfAEKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYL 570
Cdd:cd03225 92 -TVEEEVAFGL---ENLGLP-------EEEI---EERVEEALELVGLeglrdrspfTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90421313 571 LDSPFGYLDVLTEKEIFEScVCKLMA-NKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03225 158 LDEPTAGLDPAGRRELLEL-LKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
437-622 |
3.09e-23 |
|
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: 98.24 E-value: 3.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKhsgrisfcsqfswimpgtikeniIFGVSYDEYR 516
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIK-----------------------VLGKDIKKEP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 517 YRSVIKACQLEEDISKFAE---KDNIvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVcK 593
Cdd:cd03230 69 EEVKRRIGYLPEEPSLYENltvRENL-------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR-E 140
|
170 180 190
....*....|....*....|....*....|.
gi 90421313 594 LMANKTRILVTS-KMEHLKK-ADKILILHEG 622
Cdd:cd03230 141 LKKEGKTILLSShILEEAERlCDRVAILNNG 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1211-1432 |
3.51e-23 |
|
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: 99.96 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGGNAI--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSIT---LQ 1280
Cdd:cd03258 3 ELKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINglerpTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1281 QWRKAFGVIPQKVFIFSG-TFRKNLD-PYE--QWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQ 1352
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVAlPLEiaGVPKAEIEERVLEllelVGLEDKADAYPAQ-----------LSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1353 LMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK--QAFADCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQK 1429
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
...
gi 90421313 1430 LLN 1432
Cdd:cd03258 228 VFA 230
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
432-628 |
3.53e-23 |
|
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: 98.28 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKhsgrisfcsqfswimpgtikeniIFGVS 511
Cdd:cd03214 6 SVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL-----------------------LDGKD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 512 YDEYRYRSVIKAC----Q-LEE-DISKFAEKD-NivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 584
Cdd:cd03214 63 LASLSPKELARKIayvpQaLELlGLAHLADRPfN--------ELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90421313 585 EIFEScVCKLMA--NKTRILVTSKMEH-LKKADKILILHEGSSYFYG 628
Cdd:cd03214 135 ELLEL-LRRLARerGKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
436-646 |
3.64e-23 |
|
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: 100.10 E-value: 3.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 436 LGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-----------RISFCSQFSWIMPG-TIK 503
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFGVsydeyRYRSVIKAcQLEEDISKFAEKDNI--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 581
Cdd:cd03299 90 KNIAYGL-----KKRKVDKK-EIERKVLEIAEMLGIdhLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 582 T-EKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSE-LQNLQPDFSSKLMG 646
Cdd:cd03299 164 TkEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEvFKKPKNEFVAEFLG 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1209-1418 |
5.21e-23 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 98.71 E-value: 5.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1209 QMTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITlQQWRKAFG 1287
Cdd:COG4133 2 MLEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpSAGEVLWNGEPIRDAR-EDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSG-TFRKNLDPY-----EQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVL 1361
Cdd:COG4133 79 YLGHADGLKPElTVRENLRFWaalygLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 1362 SKAKILLLDEPSAHLDP----VTYQIIRRTLKQafaDCTVILCEHrIEAMLECQQFLVIEE 1418
Cdd:COG4133 148 SPAPLWLLDEPFTALDAagvaLLAELIAAHLAR---GGAVLLTTH-QPLELAAARVLDLGD 204
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1212-1402 |
1.23e-22 |
|
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: 98.02 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN------TEGEIQIDG--VSWDSITLQQWR 1283
Cdd:cd03260 3 LRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgapDEGEVLLDGkdIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1284 KAFGVIPQKVFIFSGTFRKNLDpYEQW----SDQEIWKVADEVGLRSVieQFPGKLDFVLVDGGcvLSHGHKQLMCLARS 1359
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVA-YGLRlhgiKLKEELDERVEEALRKA--ALWDEVKDRLHALG--LSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90421313 1360 VLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEH 1402
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH 198
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
438-622 |
1.87e-22 |
|
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: 97.18 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------------ISFCSQFSWIMPG 500
Cdd:cd03255 17 VQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisklsekelaafrrrhIGFVFQSFNLLPD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENI-----IFGVSYDEY--RYRSVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLD 572
Cdd:cd03255 97 lTALENVelpllLAGVPKKERreRAEELLERVGLGDRLNHYPSE-----------LSGGQQQRVAIARALANDPKIILAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 573 SPFGYLDVLTEKEIFEscvckLM------ANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03255 166 EPTGNLDSETGKEVME-----LLrelnkeAGTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
433-622 |
2.37e-22 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 96.81 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMP 499
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIFGVSYDEYRYRsvikacqlEEDISKFAEK---DNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:COG4619 88 GTVRDNLPFPFQLRERKFD--------RERALELLERlglPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 90421313 577 YLDVLTeKEIFESCVCKLMANKTR--ILVTSKMEHLKK-ADKILILHEG 622
Cdd:COG4619 160 ALDPEN-TRRVEELLREYLAEEGRavLWVSHDPEQIERvADRVLTLEAG 207
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
97-298 |
2.58e-22 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 99.49 E-value: 2.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 97 VQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKL--------- 167
Cdd:cd18596 15 APPFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIFEKALRRrdksgssks 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 168 ----------SSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQ 237
Cdd:cd18596 95 seskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWSALVGLAVMVLLLPLN 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 238 AGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRK 298
Cdd:cd18596 175 GYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRK 235
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1211-1402 |
2.71e-22 |
|
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: 102.67 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGGN---AILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSIT---LQQWR 1283
Cdd:COG1123 262 EVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRpTSGSILFDGKDLTKLSrrsLRELR 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1284 KAFGVIPQkvfifsgtfrknlDPYEQ--------------------WSDQEIWKVADE----VGL-RSVIEQFPGKldfv 1338
Cdd:COG1123 342 RRVQMVFQ-------------DPYSSlnprmtvgdiiaeplrlhglLSRAERRERVAEllerVGLpPDLADRYPHE---- 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1339 lvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTY-QIIR--RTLKQAFaDCTVILCEH 1402
Cdd:COG1123 405 -------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQaQILNllRDLQREL-GLTYLFISH 463
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1212-1409 |
2.91e-22 |
|
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: 96.45 E-value: 2.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSwdsitLQQWRKAFGVIP 1290
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKP-----LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKvFIFSGTFRknLDPYE-------------QWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQL 1353
Cdd:cd03235 75 QR-RSIDRDFP--ISVRDvvlmglyghkglfRRLSKADKAKVDEalerVGLSELADRQIGE-----------LSGGQQQR 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1354 MCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRIEAMLE 1409
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLE 197
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
438-633 |
4.34e-22 |
|
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: 96.42 E-value: 4.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPG-TIKE 504
Cdd:cd03263 15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaarqSLGYCPQFDALFDElTVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIF-----GVSYDEYRYRS--VIKACQLEEDISKFAekdnivlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03263 95 HLRFyarlkGLPKSEIKEEVelLLRVLGLTDKANKRA-----------RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSG 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 578 LDVLTEKEIFEsCVCKLMANKTRILVTSKM---EHLkkADKILILHEGSSYFYGTFSEL 633
Cdd:cd03263 164 LDPASRRAIWD-LILEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1210-1420 |
6.22e-22 |
|
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: 94.56 E-value: 6.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWD--SITLQQWRKAF 1286
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLTdlEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSgtfrkNLDpyeqwsdqeiwkVADEVGLRsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKI 1366
Cdd:cd03229 79 GMVFQDFALFP-----HLT------------VLENIALG--------------------LSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1367 LLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVILCEHRI-EAMLECQQFLVIEENK 1420
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLdEAARLADRVVVLRDGK 178
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
437-622 |
6.72e-22 |
|
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: 94.56 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIkhsgrisfcsqfswimpgtikenIIFGVSYDEYR 516
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-----------------------LIDGEDLTDLE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 517 YRSVikacQLEEDISK-FAE---------KDNIVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEI 586
Cdd:cd03229 69 DELP----PLRRRIGMvFQDfalfphltvLENIALG-----LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190
....*....|....*....|....*....|....*....
gi 90421313 587 fESCVCKLMAN--KTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03229 140 -RALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1212-1402 |
7.08e-22 |
|
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: 95.63 E-value: 7.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNA--ILENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGEIQIDGVSWDSITLQQW----R 1283
Cdd:cd03255 3 LKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDrpTSGEVRVDGTDISKLSEKELaafrR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1284 KAFGVIPQK---------------VFIFSGTFRKNldpYEQWSDQeiwkVADEVGLRSVIEQFPGKldfvlvdggcvLSH 1348
Cdd:cd03255 82 RHIGFVFQSfnllpdltalenvelPLLLAGVPKKE---RRERAEE----LLERVGLGDRLNHYPSE-----------LSG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1349 GHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ--AFADCTVILCEH 1402
Cdd:cd03255 144 GQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTH 199
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
439-633 |
7.10e-22 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 7.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKEN 505
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQEPVLFSGSVREN 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFGVSY-DEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 584
Cdd:TIGR00958 575 IAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQ 654
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 90421313 585 EIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:TIGR00958 655 LLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
437-605 |
9.82e-22 |
|
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: 94.85 E-value: 9.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------RISFCSQFSWIMPG-------TIK 503
Cdd:COG4133 14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGHAdglkpelTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIF-----GVSYDEYRYRSVIKACQLEEDISKFAEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:COG4133 94 ENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180
....*....|....*....|....*..
gi 90421313 579 DVLTeKEIFESCVCKLMANKTRILVTS 605
Cdd:COG4133 163 DAAG-VALLAELIAAHLARGGAVLLTT 188
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1208-1437 |
1.13e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 101.19 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKYTEGGNAIlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:PRK13657 333 GAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDpQSGRILIDGTDIRTVTRASLRRNI 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSGTFRKNLD-PYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 1365
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIRvGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1366 ILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLF 1437
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRF 563
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1210-1405 |
1.19e-21 |
|
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: 95.23 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNA--ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSwdsitLQQWRKAF 1286
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERpTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFS-GTFRKN-LDPYEQ--WSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1358
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNvALGLELqgVPKAEARERAEEllelVGLSGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVT--------YQIIRRTLKqafadcTVILCEHRIE 1405
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTreqlqeelLDIWRETGK------TVLLVTHDID 193
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1212-1405 |
2.68e-21 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 94.74 E-value: 2.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTeGGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGEIQIDGVSWDSI---TLQQWR 1283
Cdd:COG3638 5 LRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLL----RCLNglvepTSGEILVDGQDVTALrgrALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1284 KAFGVIPQK--------VF------------IFSGTFRKnldpyeqWSDQEIWKVA---DEVGLrsvieqfpgkLDFVL- 1339
Cdd:COG3638 80 RRIGMIFQQfnlvprlsVLtnvlagrlgrtsTWRSLLGL-------FPPEDRERALealERVGL----------ADKAYq 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1340 -VDGgcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVILCEHRIE 1405
Cdd:COG3638 143 rADQ---LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdgITVVVNLHQVD 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1208-1421 |
3.78e-21 |
|
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: 93.69 E-value: 3.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1208 GQMTVKDLTAKY-TEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKA 1285
Cdd:cd03248 10 GIVKFQNVTFAYpTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQpQGGQVLLDGKPISQYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQKVFIFSGTFRKNLdPY--EQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSK 1363
Cdd:cd03248 90 VSLVGQEPVLFARSLQDNI-AYglQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1364 AKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
437-619 |
5.65e-21 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 94.39 E-value: 5.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--------RISFCSQ----FSWImpgTIKE 504
Cdd:COG1116 23 GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGkpvtgpgpDRGVVFQepalLPWL---TVLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFG-----VSYDEYRYR--SVIKACQLEEDISKF-AEkdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:COG1116 100 NVALGlelrgVPKAERRERarELLELVGLAGFEDAYpHQ------------LSGGMRQRVAIARALANDPEVLLMDEPFG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 577 YLDVLTeKEIFESCVCKLMA--NKTRILVTskmeH-------LkkADKILIL 619
Cdd:COG1116 168 ALDALT-RERLQDELLRLWQetGKTVLFVT----HdvdeavfL--ADRVVVL 212
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1211-1433 |
7.96e-21 |
|
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: 92.88 E-value: 7.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQwRKAFGV- 1288
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRFDGRDITGLPPHE-RARAGIg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 -IPQKVFIFSG-TFRKNLdpyeqwsdqeiwKVADEVGLRS--------VIEQFPGKLDFVLVDGGcVLSHGHKQLMCLAR 1358
Cdd:cd03224 79 yVPEGRRIFPElTVEENL------------LLGAYARRRAkrkarlerVYELFPRLKERRKQLAG-TLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ-AFADCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQKLLNE 1433
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
396-633 |
8.08e-21 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 98.55 E-value: 8.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 396 NVTAFWEEG-------FGELFEKAKQNNNNRKTSNGDDSLFFSN--FSLLG--TPVLKDINFKIERGQLLAVAGSTGAGK 464
Cdd:PRK11176 303 NVNAQFQRGmaacqtlFAILDLEQEKDEGKRVIERAKGDIEFRNvtFTYPGkeVPALRNINFKIPAGKTVALVGRSGSGK 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 465 TSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKENIIFGVSyDEYRYRSVIKACQLE---E 528
Cdd:PRK11176 383 STIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDTIANNIAYART-EQYSREQIEEAARMAyamD 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 529 DISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVTSKME 608
Cdd:PRK11176 462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAI-QAALDELQKNRTSLVIAHRLS 540
|
250 260
....*....|....*....|....*
gi 90421313 609 HLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK11176 541 TIEKADEILVVEDGEIVERGTHAEL 565
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
439-633 |
9.97e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 98.25 E-value: 9.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK-HS------------GRISFCSQFSWIMPGTIKEN 505
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDipltklqldswrSRLAVVSQTPFLFSDTVANN 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFG---VSYDEYRYrsVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:PRK10789 409 IALGrpdATQQEIEH--VARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRT 486
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 583 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK10789 487 EHQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
438-622 |
1.27e-20 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.41 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------------ISFCSQFSWIMPG 500
Cdd:COG1136 21 VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdisslserelarlrrrhIGFVFQFFNLLPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENI-----IFGVSYDEY--RYRSVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG1136 101 lTALENValpllLAGVSRKERreRARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILAD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 573 SPFGYLDVLTEKEIFEscvckLMA------NKTRILVTSKMEHLKKADKILILHEG 622
Cdd:COG1136 170 EPTGNLDSKTGEEVLE-----LLRelnrelGTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
438-619 |
2.08e-20 |
|
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: 91.38 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI--------KHSGRISFCSQ----FSWImpgTIKEN 505
Cdd:cd03293 17 VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepvtGPGPDRGYVFQqdalLPWL---TVLDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFG-----VSYDEYRYR--SVIKACQLEEDISKF-AEkdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03293 94 VALGlelqgVPKAEARERaeELLELVGLSGFENAYpHQ------------LSGGMRQRVALARALAVDPDVLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 90421313 578 LDVLTEKEIFEScvckLMA-----NKTRILVT-SKMEHLKKADKILIL 619
Cdd:cd03293 162 LDALTREQLQEE----LLDiwretGKTVLLVThDIDEAVFLADRVVVL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1211-1432 |
2.40e-20 |
|
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: 91.98 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGV---SWDSITLqqwRKAF 1286
Cdd:cd03295 2 EFENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEIFIDGEdirEQDPVEL---RRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSG-TFRKN--LDP-YEQWSDQEIWKVADE----VGL--RSVIEQFPGKldfvlvdggcvLSHGHKQLMCL 1356
Cdd:cd03295 78 GYVIQQIGLFPHmTVEENiaLVPkLLKWPKEKIRERADEllalVGLdpAEFADRYPHE-----------LSGGQQQRVGV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDPVTyqiiRRTLKQAFADC------TVILCEHRI-EAMLECQQFLVIEENKVRQYDSIQK 1429
Cdd:cd03295 147 ARALAADPPLLLMDEPFGALDPIT----RDQLQEEFKRLqqelgkTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDE 222
|
...
gi 90421313 1430 LLN 1432
Cdd:cd03295 223 ILR 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1205-1419 |
2.66e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 96.80 E-value: 2.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1205 PSGGQMTVKDLTAkYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDgvswdsitlQQWR 1283
Cdd:COG4178 358 SEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPyGSGRIARP---------AGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1284 KAFgvIPQKVFIFSGTFRKNL---DPYEQWSDQEIWKVADEVGLrsviEQFPGKLDFVlVDGGCVLSHGHKQLMCLARSV 1360
Cdd:COG4178 428 VLF--LPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----GHLAERLDEE-ADWDQVLSLGEQQRLAFARLL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1361 LSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEEN 1419
Cdd:COG4178 501 LHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1212-1436 |
4.82e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 91.98 E-value: 4.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKST---LLSAFLRllNTEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLK--PQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 I---PQKVFIFS--------GTFRKNLDPYEQWsdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLA 1357
Cdd:PRK13632 88 IfqnPDNQFIGAtveddiafGLENKKVPPKKMK--DIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1358 rSVLS-KAKILLLDEPSAHLDPV----TYQIIRRTLKQafADCTVILCEHRIEAMLECQQFLVIEENK-VRQYDSIQKLL 1431
Cdd:PRK13632 155 -SVLAlNPEIIIFDESTSMLDPKgkreIKKIMVDLRKT--RKKTLISITHDMDEAILADKVIVFSEGKlIAQGKPKEILN 231
|
....*
gi 90421313 1432 NERSL 1436
Cdd:PRK13632 232 NKEIL 236
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1211-1405 |
9.67e-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: 89.93 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGV---SWDSITLQQWRKAF 1286
Cdd:cd03256 2 EVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTdinKLKGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQK--------VF------------IFSGTFRknldpyeQWSDQEIWKVA---DEVGLRSVIEQFPGKldfvlvdgg 1343
Cdd:cd03256 81 GMIFQQfnlierlsVLenvlsgrlgrrsTWRSLFG-------LFPKEEKQRALaalERVGLLDKAYQRADQ--------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1344 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFA--DCTVILCEHRIE 1405
Cdd:cd03256 145 --LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVD 206
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1218-1385 |
1.52e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.96 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1218 KYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSIT---LQQWRKAFGVIPQkv 1293
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERpTSGQVLVNGQDLSRLKrreIPYLRRRIGVVFQ-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1294 fifsgTFR--KNLDPYE---------QWSDQEIWK----VADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1358
Cdd:COG2884 87 -----DFRllPDRTVYEnvalplrvtGKSRKEIRRrvreVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIAR 150
|
170 180
....*....|....*....|....*...
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVT-YQIIR 1385
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETsWEIME 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1210-1399 |
1.53e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.95 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNA--ILENISFSISPGQRVGLLGRTGSGKSTLL---SAFLRLlnTEGEIQIDGV---SWDSITLQQ 1281
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLnilGGLDRP--TSGEVLIDGQdisSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1282 WR-KAFGVIPQK---------------VFIFSGTFRKNldpyeqwSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcv 1345
Cdd:COG1136 83 LRrRHIGFVFQFfnllpeltalenvalPLLLAGVSRKE-------RRERARELLERVGLGDRLDHRPSQ----------- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1346 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVIL 1399
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVM 200
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
437-619 |
3.50e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.90 E-value: 3.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--RISFCSQFS---WIMPGTIKENIIFGvs 511
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSevpDSLPLTVRDLVAMG-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 512 ydeyRY-------------RSVIKACQLEEDISKFAEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:NF040873 82 ----RWarrglwrrltrddRAAVDDALERVGLADLAGRQ---LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 90421313 579 DVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILIL 619
Cdd:NF040873 151 DAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
432-629 |
4.03e-19 |
|
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: 88.56 E-value: 4.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSwIM 498
Cdd:COG1120 8 SVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslsrrelarRIAYVPQEP-PA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 499 PG--TIKENIIFGvsydeyRY-------------RSVIKACqLEE-DISKFAEKDnivLGEggitLSGGQRARISLARAV 562
Cdd:COG1120 87 PFglTVRELVALG------RYphlglfgrpsaedREAVEEA-LERtGLEHLADRP---VDE----LSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 563 YKDADLYLLDSPFGYLDVLTEKEIFEsCVCKL--MANKTRILVTskmeH-----LKKADKILILHEGSSYFYGT 629
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLE-LLRRLarERGRTVVMVL----HdlnlaARYADRLVLLKDGRIVAQGP 221
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
432-633 |
4.22e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 93.10 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGT-PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWI 497
Cdd:PRK13657 341 SFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvtraslrrNIAVVFQDAGL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 498 MPGTIKENIIFGV--SYDEYRYRSViKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:PRK13657 421 FNRSIEDNIRVGRpdATDEEMRAAA-ERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 576 GYLDVLTEKEIFESCVCkLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13657 500 SALDVETEAKVKAALDE-LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDEL 556
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1211-1422 |
4.27e-19 |
|
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: 87.27 E-value: 4.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSiTLQQWRKAFGVI 1289
Cdd:cd03268 2 KTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKpDSGEITFDGKSYQK-NIEALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQKVFIFSGTFRKNL---DPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKI 1366
Cdd:cd03268 79 EAPGFYPNLTARENLrllARLLGIRKKRIDEVLDVVGLKDSAKKKVKG-----------FSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1367 LLLDEPSAHLDPVTYQIIRRTLkQAFAD--CTVILCEHRIEAM-LECQQFLVIEENKVR 1422
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELI-LSLRDqgITVLISSHLLSEIqKVADRIGIINKGKLI 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1211-1436 |
4.87e-19 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 87.73 E-value: 4.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSwdsIT-LQQWRKA--- 1285
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGED---ITgLPPHRIArlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQKVFIFSG-TFRKNLdpyeqwsdqEI--WKVADEVGLRSVIEQ----FPgkldfVLVD-----GGcVLSHGHKQL 1353
Cdd:COG0410 80 IGYVPEGRRIFPSlTVEENL---------LLgaYARRDRAEVRADLERvyelFP-----RLKErrrqrAG-TLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1354 MCLARSVLSKAKILLLDEPSAHLDPVT----YQIIRRtLKQafADCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQ 1428
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIveeiFEIIRR-LNR--EGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAA 221
|
....*...
gi 90421313 1429 KLLNERSL 1436
Cdd:COG0410 222 ELLADPEV 229
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
437-588 |
6.34e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.22 E-value: 6.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR----------ISFcsQFSWIMP-GTIKEN 505
Cdd:PRK11248 13 GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaergVVF--QNEGLLPwRNVQDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFGV-------SYDEYRYRSVIKACQLEEdiskfAEKDNIvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK11248 91 VAFGLqlagvekMQRLEIAHQMLKKVGLEG-----AEKRYI------WQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170
....*....|
gi 90421313 579 DVLTEKEIFE 588
Cdd:PRK11248 160 DAFTREQMQT 169
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1229-1425 |
7.43e-19 |
|
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: 86.97 E-value: 7.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1229 NISFSIsPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWD----SITLQQWRKAFGVIPQKVFIFSG-TFRK 1302
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKpDGGTIVLNGTVLFdsrkKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1303 NLD-PYEQWSDQEIWKVADEV----GLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:cd03297 95 NLAfGLKRKRNREDRISVDELldllGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 1378 PVTYQIIRRTLKQAFAD--CTVILCEHRI-EAMLECQQFLVIEENKVRQYD 1425
Cdd:cd03297 164 RALRLQLLPELKQIKKNlnIPVIFVTHDLsEAEYLADRIVVMEDGRLQYIG 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
437-635 |
8.08e-19 |
|
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: 87.34 E-value: 8.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG----------------RISFCSQ----FSW 496
Cdd:COG1127 17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelrrRIGMLFQggalFDS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 497 ImpgTIKENIIF------GVSYDEYRYR--SVIKACQLEEDISKF-AEkdnivlgeggitLSGGQRARISLARAVYKDAD 567
Cdd:COG1127 97 L---TVFENVAFplrehtDLSEAEIRELvlEKLELVGLPGAADKMpSE------------LSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 568 LYLLDSPFGYLDVLTEKEIFE---SCVCKLmaNKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQN 635
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDElirELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
430-622 |
9.47e-19 |
|
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: 87.01 E-value: 9.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 430 FSNFsllgtPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQFSWIM 498
Cdd:cd03296 12 FGDF-----VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 499 PG-TIKENIIFGV---------SYDEYRYR--SVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDA 566
Cdd:cd03296 87 RHmTVFDNVAFGLrvkprserpPEAEIRAKvhELLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARALAVEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 567 DLYLLDSPFGYLDVLTEKEIfESCVCKLM--ANKTRILVT-SKMEHLKKADKILILHEG 622
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKEL-RRWLRRLHdeLHVTTVFVThDQEEALEVADRVVVMNKG 213
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1205-1425 |
1.19e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1205 PSGGQM-TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNteGEIQIDG--VSWdSITLQq 1281
Cdd:COG0488 310 RLGKKVlELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLLA--GELEPDSgtVKL-GETVK- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1282 wrkaFGVIPQKvfifSGTFRKNLDPYEqwsdqEIWKVAD---EVGLRSVIEQ--FPGKLDFVLVDggcVLSHGHKQLMCL 1356
Cdd:COG0488 380 ----IGYFDQH----QEELDPDKTVLD-----ELRDGAPggtEQEVRGYLGRflFSGDDAFKPVG---VLSGGEKARLAL 443
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDPVTyqiiRRTLKQAFADC--TVILCEH-R--IEAMleCQQFLVIEENKVRQYD 1425
Cdd:COG0488 444 AKLLLSPPNVLLLDEPTNHLDIET----LEALEEALDDFpgTVLLVSHdRyfLDRV--ATRILEFEDGGVREYP 511
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
439-622 |
1.24e-18 |
|
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: 85.93 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKEN 505
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IifgVSYDEYRYRSVIKACQLEediskfaekdnivlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKE 585
Cdd:cd03369 102 L---DPFDEYSDEEIYGALRVS---------------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 90421313 586 IFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03369 164 IQKT-IREEFTNSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
440-628 |
1.43e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 86.05 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISfcsqfSWIMPG-------TIKENIIF---- 508
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGggfnpelTGRENIYLngrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 509 -GVSYDEYRyrsvikacQLEEDISKFAEkdnivLGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03220 112 lGLSRKEID--------EKIDEIIEFSE-----LGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 90421313 584 KEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYG 628
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
437-622 |
1.85e-18 |
|
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: 84.02 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRisfcsqfswimpgtikeniifgvsydEYR 516
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 517 YRSVIKACQLeediskfaekdnivlgegGIT----LSGGQRARISLARAVYKDADLYLLDSPFGYLDVlTEKEIFESCVC 592
Cdd:cd03216 66 FASPRDARRA------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTP-AEVERLFKVIR 126
|
170 180 190
....*....|....*....|....*....|..
gi 90421313 593 KLMAN-KTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03216 127 RLRAQgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
437-622 |
2.14e-18 |
|
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: 85.38 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQFSWIMPG-TIKE 504
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMVFQNYALYPHmTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFG-----VSYDEY--RYRSVIKACQLEEDISKFAEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03301 92 NIAFGlklrkVPKDEIdeRVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 90421313 578 LDVLTEKEIFESCVcKLMAN--KTRILVT-SKMEHLKKADKILILHEG 622
Cdd:cd03301 161 LDAKLRVQMRAELK-RLQQRlgTTTIYVThDQVEAMTMADRIAVMNDG 207
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
437-588 |
2.66e-18 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 85.49 E-value: 2.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI----KHSGRIS--------------FcsQFSWIM 498
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngQDLSRLKrreipylrrrigvvF--QDFRLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 499 PG-TIKENIIF-----GVSYDEYRYR--SVIKACQLEEDISKFAekdnivlgeggITLSGGQRARISLARAVYKDADLYL 570
Cdd:COG2884 92 PDrTVYENVALplrvtGKSRKEIRRRvrEVLDLVGLSDKAKALP-----------HELSGGEQQRVAIARALVNRPELLL 160
|
170
....*....|....*...
gi 90421313 571 LDSPFGYLDVLTEKEIFE 588
Cdd:COG2884 161 ADEPTGNLDPETSWEIME 178
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
438-582 |
3.07e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 86.07 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR----------ISFcsQFSWIMPG-TIKENI 506
Cdd:COG4525 20 QPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadrgVVF--QKDALLPWlNVLDNV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 IFGVsydeyRYRSVIKACQLEE--------DISKFAEKdNIvlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:COG4525 98 AFGL-----RLRGVPKAERRARaeellalvGLADFARR-RI------WQLSGGMRQRVGIARALAADPRFLLMDEPFGAL 165
|
....
gi 90421313 579 DVLT 582
Cdd:COG4525 166 DALT 169
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
440-629 |
3.21e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRIS--------FCSQFSwimpGtiKENIIF--- 508
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPELT----G--RENIYLngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 509 --GVSYDEYRYRsvikacqlEEDISKFAEkdnivLGEgGI-----TLSGGQRARISLARAVYKDADLYLLDspfgylDVL 581
Cdd:COG1134 115 llGLSRKEIDEK--------FDEIVEFAE-----LGD-FIdqpvkTYSSGMRARLAFAVATAVDPDILLVD------EVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 582 T----------EKEIFEscvckLMAN-KTRILVTSKMEHLKK-ADKILILHEGSSYFYGT 629
Cdd:COG1134 175 AvgdaafqkkcLARIRE-----LRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
433-640 |
3.30e-18 |
|
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: 85.63 E-value: 3.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG----------------RISFCSQFSW 496
Cdd:cd03261 8 KSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGMLFQSGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 497 I---MpgTIKENIIFGVSydEYRYRSvikacqlEEDISKFAEKdniVLGEGGIT---------LSGGQRARISLARAVYK 564
Cdd:cd03261 88 LfdsL--TVFENVAFPLR--EHTRLS-------EEEIREIVLE---KLEAVGLRgaedlypaeLSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 565 DADLYLLDSPFGYLDVLTEKEIFE---SCVCKLmaNKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQNLQPDF 640
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDlirSLKKEL--GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASDDPL 231
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1212-1430 |
5.01e-18 |
|
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: 84.48 E-value: 5.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSiTLQQWRKAFGVIP 1290
Cdd:cd03263 3 IRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRpTSGTAYINGYSIRT-DRKAARQSLGYCP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSG-TFRKNLDPY-------EQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLS 1362
Cdd:cd03263 82 QFDALFDElTVREHLRFYarlkglpKSEIKEEVELLLRVLGLTDKANKRART-----------LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1363 KAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRI-EAMLECQQFLVIEENKVRQYDSIQKL 1430
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMdEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
437-635 |
5.85e-18 |
|
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: 84.93 E-value: 5.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG----------------RISFCSQ-FSWIMP 499
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklkgkalrqlrrQIGMIFQqFNLIER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIFG-VSY--------------DEYRYRSVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYK 564
Cdd:cd03256 93 LSVLENVLSGrLGRrstwrslfglfpkeEKQRALAALERVGLLDKAYQRADQ-----------LSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 565 DADLYLLDSPFGYLDVLTEKEIFEscvckLMA------NKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQN 635
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMD-----LLKrinreeGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAELTD 234
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1223-1437 |
8.37e-18 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 85.29 E-value: 8.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1223 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGEIQIDGvswdsitlqqwRKAFGviPQKVFIFSGTFR 1301
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILgELEPSEGKIKHSG-----------RISFS--SQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1302 KNLD---PYEQWSDQEIWKVADevgLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 1378
Cdd:cd03291 116 ENIIfgvSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1379 VT-YQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLF 1437
Cdd:cd03291 193 FTeKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
430-622 |
8.85e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.74 E-value: 8.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 430 FSNFSLLgtpvlKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFcsqfSWIMPG--------- 500
Cdd:COG1118 12 FGSFTLL-----DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF----TNLPPRerrvgfvfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 --------TIKENIIFGVSyDEYRYRSVIKA---CQLEE-DISKFAEK--DNivlgeggitLSGGQRARISLARAVYKDA 566
Cdd:COG1118 83 hyalfphmTVAENIAFGLR-VRPPSKAEIRArveELLELvQLEGLADRypSQ---------LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 567 DLYLLDSPFGYLDVLTEKEIfEScvcKLMA-----NKTRILVT-SKMEHLKKADKILILHEG 622
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKEL-RR---WLRRlhdelGGTTVFVThDQEEALELADRVVVMNQG 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
437-622 |
1.17e-17 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 86.28 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQfSWI----MpgT 501
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRdvtdlppkdrnIAMVFQ-SYAlyphM--T 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKENIIFGVsydeyRYRSVIKAcQLEEDISKFAEkdniVLGeggIT---------LSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG3839 92 VYENIAFPL-----KLRKVPKA-EIDRRVREAAE----LLG---LEdlldrkpkqLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 573 SPFGYLD----VLTEKEIFescvcKLMA--NKTRILVTskmeH-------LkkADKILILHEG 622
Cdd:COG3839 159 EPLSNLDaklrVEMRAEIK-----RLHRrlGTTTIYVT----HdqveamtL--ADRIAVMNDG 210
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
440-628 |
1.62e-17 |
|
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: 82.71 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR---ISFCSQFSWiMPG--------TIKENIIF 508
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKpldIAARNRIGY-LPEerglypkmKVIDQLVY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 509 -----GVSYDEYRYRSvikacqlEEDISKF--AEKDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV- 580
Cdd:cd03269 94 laqlkGLKKEEARRRI-------DEWLERLelSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPv 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 581 ---LTEKEIFEscvcKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYG 628
Cdd:cd03269 163 nveLLKDVIRE----LARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1212-1409 |
1.96e-17 |
|
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: 83.26 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRLlnTEGEIQIDGVswDSITLQQWRKA--- 1285
Cdd:cd03219 3 VRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLfnlISGFLRP--TSGSVLFDGE--DITGLPPHEIArlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 ----FgvipQKVFIFSG-TFRKNL---------DPYEQW----SDQEIWKVADE----VGLRSVIEQFPGKLdfvlvdgg 1343
Cdd:cd03219 77 igrtF----QIPRLFPElTVLENVmvaaqartgSGLLLArarrEEREARERAEEllerVGLADLADRPAGEL-------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1344 cvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPV-TYQIIRRTLKQAFADCTVILCEHRIEAMLE 1409
Cdd:cd03219 145 ---SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMS 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1212-1389 |
2.18e-17 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 83.12 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTeGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGvswDSIT------LQQWRK 1284
Cdd:TIGR02315 4 VENLSKVYP-NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEpSSGSILLEG---TDITklrgkkLRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQK------------VFI----FSGTFRKNLDPYEQWSDQEIWKVADEVGLrsvieqfpgkLDFVL--VDGgcvL 1346
Cdd:TIGR02315 80 RIGMIFQHynlierltvlenVLHgrlgYKPTWRSLLGRFSEEDKERALSALERVGL----------ADKAYqrADQ---L 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK 1389
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLK 189
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
440-622 |
3.78e-17 |
|
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: 82.23 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLL-----MVIMGELEPSEGKIKHSG---------------RISFCSQFSWIMP 499
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGkdiydldvdvlelrrRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIFGVSYDEYRYRSVIKAcQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKLKEELDE-RVEEALRKAALWDEVKDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 90421313 580 -VLTEKeiFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03260 174 pISTAK--IEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNG 216
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1212-1440 |
3.94e-17 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 83.25 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSI-TLQQWRKA 1285
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTL----AKLLNglllpTSGKVTVDGLDTLDEeNLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVI---PQKVFIfSGTFR---------KNLDPYEQWsdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQL 1353
Cdd:TIGR04520 79 VGMVfqnPDNQFV-GATVEddvafglenLGVPREEMR--KRVDEALKLVGMEDFRDREPHL-----------LSGGQKQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1354 MCLArSVLS-KAKILLLDEPSAHLDPVT----YQIIRRTLKQafADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQ 1428
Cdd:TIGR04520 145 VAIA-GVLAmRPDIIILDEATSMLDPKGrkevLETIRKLNKE--EGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPR 221
|
250
....*....|..
gi 90421313 1429 KLLNERSLFRQA 1440
Cdd:TIGR04520 222 EIFSQVELLKEI 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1212-1424 |
4.21e-17 |
|
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: 81.56 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITlqqwRKAFGVIP 1290
Cdd:cd03269 3 VENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILpDSGEVLFDGKPLDIAA----RNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 -----------QKVFIFSGTFrKNLDPYE--QWSDQEIWKVADEVGLRSVIEQfpgkldfvlvdggcvLSHGHKQLMCLA 1357
Cdd:cd03269 77 eerglypkmkvIDQLVYLAQL-KGLKKEEarRRIDEWLERLELSEYANKRVEE---------------LSKGNQQKVQFI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1358 RSVLSKAKILLLDEPSAHLDPVTYQIIRRTL-KQAFADCTVILCEHRIEAMLE-CQQFLVIEENKVRQY 1424
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLY 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1213-1402 |
4.33e-17 |
|
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: 81.69 E-value: 4.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYTeGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGEIQIDGVSWDSI---TLQQWRKAFGV 1288
Cdd:cd03292 4 INVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLrgrAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSgtfrkNLDPYE---------QWSDQEIWK----VADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMC 1355
Cdd:cd03292 83 VFQDFRLLP-----DRNVYEnvafalevtGVPPREIRKrvpaALELVGLSHKHRALPAEL-----------SGGEQQRVA 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 90421313 1356 LARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQA-FADCTVILCEH 1402
Cdd:cd03292 147 IARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH 194
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1215-1403 |
4.38e-17 |
|
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: 81.06 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1215 LTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAF---LRLLNTEGEIQIDGVswdSITLQQWRKAFGVIPQ 1291
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1292 K-VFIFSGTFRKNLDpyeqwsdqeiwkVAdeVGLRSvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLD 1370
Cdd:cd03213 90 DdILHPTLTVRETLM------------FA--AKLRG-------------------LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190
....*....|....*....|....*....|....
gi 90421313 1371 EPSAHLDPVTYQIIRRTLKQ-AFADCTVILCEHR 1403
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQ 170
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
858-1167 |
7.10e-17 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 83.03 E-value: 7.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 858 SLIFVLIWCLVIFlaevaASLVVLWLLGNTplQDKGNSTHSRNNSYAVIitstssyyvfYIYVGVADTLLAMGFFRGLPL 937
Cdd:cd18559 2 FLLIKLVLCNHVF-----SGPSNLWLLLWF--DDPVNGPQEHGQVYLSV----------LGALAILQGITVFQYSMAVSI 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 938 VHtlITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPyIFV 1017
Cdd:cd18559 65 GG--IFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1018 ATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGrqpyFETLFHKALNLHTANWFLYLST-- 1095
Cdd:cd18559 142 VGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE----WEEAFIRQVDAKRDNELAYLPSiv 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1096 -LRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFI 1167
Cdd:cd18559 218 yLRALAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
438-633 |
9.77e-17 |
|
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: 85.34 E-value: 9.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPS---EGKIKHSG-------------RISFCSQ--FSWIMP 499
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGrdllelsealrgrRIGMVFQdpMTQLNP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIF-----GVSYDEYRYR--SVIKACQLEEDISKFAEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG1123 99 VTVGDQIAEalenlGLSRAEARARvlELLEAVGLERRLDRYPH-----------QLSGGQRQRVAIAMALALDPDLLIAD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 573 SPFGYLDVLTEKEIFEsCVCKLMA--NKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSEL 633
Cdd:COG1123 168 EPTTALDVTTQAEILD-LLRELQRerGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1211-1421 |
1.02e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 82.11 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGG---NAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGEIQIDGV---SWDSITL 1279
Cdd:TIGR04521 2 KLKNVSYIYQPGTpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLI----QHLNgllkpTSGTVTIDGRditAKKKKKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1280 QQWRKAFGVipqkVF------IFSGTFRK-------NLDpyeqWSDQEIWKVADE----VGL-RSVIEQFPGKLdfvlvd 1341
Cdd:TIGR04521 78 KDLRKKVGL----VFqfpehqLFEETVYKdiafgpkNLG----LSEEEAEERVKEalelVGLdEEYLERSPFEL------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1342 ggcvlSHGHKQLMCLArSVLS-KAKILLLDEPSAHLDPVTyqiiRRTLKQAFADC------TVILCEHRIEAMLE-CQQF 1413
Cdd:TIGR04521 144 -----SGGQMRRVAIA-GVLAmEPEVLILDEPTAGLDPKG----RKEILDLFKRLhkekglTVILVTHSMEDVAEyADRV 213
|
....*...
gi 90421313 1414 LVIEENKV 1421
Cdd:TIGR04521 214 IVMHKGKI 221
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1212-1423 |
1.13e-16 |
|
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: 80.31 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQrVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSwDSITLQQWRKAFGVIP 1290
Cdd:cd03264 3 LENLTKRY--GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPpSSGTIRIDGQD-VLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSG-TFRKNLDpYEQW--------SDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVL 1361
Cdd:cd03264 79 QEFGVYPNfTVREFLD-YIAWlkgipskeVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQALV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1362 SKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLE-CQQFLVIEENKVRQ 1423
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVF 209
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
82-356 |
1.15e-16 |
|
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents the 6-transmembrane (6TM) domain of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides.
Pssm-ID: 350003 [Multi-domain] Cd Length: 290 Bit Score: 82.26 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 82 MFYGIFLYlGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLgIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIY 161
Cdd:cd18559 1 SFLLIKLV-LCNHVFSGPSNLWLLLWFDDPVNGPQEHGQVYL-SVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 162 KKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLG 241
Cdd:cd18559 79 HKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 242 RMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLS 321
Cdd:cd18559 159 ASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFAS 238
|
250 260 270
....*....|....*....|....*....|....*...
gi 90421313 322 VLPYALI---KGIILRKIFTTISFCIVLRMAVtRQFPW 356
Cdd:cd18559 239 FFAYVSRhslAGLVALKVFYSLALTTYLNWPL-NMSPE 275
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
387-633 |
1.20e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 85.54 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 387 LTTTEVVMENVTAFWEEGFgELFEKAKQN--NNNRKTSNGD---DSLFFSNFSllGTPVLKDINFKIERGQLLAVAGSTG 461
Cdd:PRK10790 301 LTTQQSMLQQAVVAGERVF-ELMDGPRQQygNDDRPLQSGRidiDNVSFAYRD--DNLVLQNINLSVPSRGFVALVGHTG 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 462 AGKTSLLMVIMGELEPSEGKIKHSGR-------------ISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEE 528
Cdd:PRK10790 378 SGKSTLASLLMGYYPLTEGEIRLDGRplsslshsvlrqgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 529 DISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVTSKME 608
Cdd:PRK10790 458 LARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI-QQALAAVREHTTLVVIAHRLS 536
|
250 260
....*....|....*....|....*
gi 90421313 609 HLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK10790 537 TIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
437-660 |
1.26e-16 |
|
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: 81.82 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMgELEPSEGKIKHSG-----------RISF--CSQFSWIMPGTIK 503
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGvswnsvplqkwRKAFgvIPQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENI-IFGVSYDEYRYRsVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03289 95 KNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 583 EKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNS 660
Cdd:cd03289 174 YQ-VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLFPRRNSSK 250
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
439-622 |
1.28e-16 |
|
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: 80.63 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG----------------RISFCSQ--FSWIMPG 500
Cdd:cd03257 19 KALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdllklsrrlrkirrkEIQMVFQdpMSSLNPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENIIFGVsydeYRYRSVIKACQLEEDISKFAEKdnIVLGEGGIT-----LSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:cd03257 99 mTIGEQIAEPL----RIHGKLSKKEARKEAVLLLLVG--VGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 575 FGYLDVLTEKEIFEscvckLMA------NKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03257 173 TSALDVSVQAQILD-----LLKklqeelGLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
438-622 |
1.37e-16 |
|
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: 80.59 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-------------ISFCSQFSWIMPGTIKE 504
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQEPVLFARSLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFGVSYDEYRyrSVIKACQ---LEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 581
Cdd:cd03248 107 NIAYGLQSCSFE--CVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 90421313 582 TEKEIFESCVCKLmANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03248 185 SEQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
430-628 |
1.57e-16 |
|
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: 80.03 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 430 FSNFSLlgtpvlkDINFKIErGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPG--------- 500
Cdd:cd03297 10 LPDFTL-------KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkiglvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 ---------TIKENIIFGV-----SYDEYRYRSVIKACQLEEdiskfaekdniVLGEGGITLSGGQRARISLARAVYKDA 566
Cdd:cd03297 82 qqyalfphlNVRENLAFGLkrkrnREDRISVDELLDLLGLDH-----------LLNRYPAQLSGGEKQRVALARALAAQP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 567 DLYLLDSPFGYLDVLTeKEIFESCVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEGSSYFYG 628
Cdd:cd03297 151 ELLLLDEPFSALDRAL-RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1213-1436 |
1.64e-16 |
|
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: 80.90 E-value: 1.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSaflrLLNTE------GEIQIDGVSWDSITLQQWRKAF 1286
Cdd:COG1119 7 RNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS----LITGDlpptygNDVRLFGERRGGEDVWELRKRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVI----------PQKVF--IFSGtFRKNLDPYEQWSDQEI---WKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHK 1351
Cdd:COG1119 81 GLVspalqlrfprDETVLdvVLSG-FFDSIGLYREPTDEQReraRELLELLGLAHLADRPFGT-----------LSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1352 QLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVILCEHRIEAMLEC-QQFLVIEENKVRQYDSIQ 1428
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKE 228
|
....*...
gi 90421313 1429 KLLNERSL 1436
Cdd:COG1119 229 EVLTSENL 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1212-1407 |
2.10e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 81.25 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGG---NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVS-WD-SITLQQWRKA 1285
Cdd:PRK13637 5 IENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVDiTDkKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQ--KVFIFSGTFRK-------NLDPYEQWSDQEIWKVADEVGLRsvIEQFPGKLDFvlvdggcVLSHGHKQLMCL 1356
Cdd:PRK13637 85 VGLVFQypEYQLFEETIEKdiafgpiNLGLSEEEIENRVKRAMNIVGLD--YEDYKDKSPF-------ELSGGQKRRVAI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDP-----VTYQIirRTLKQAFaDCTVILCEHRIEAM 1407
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPkgrdeILNKI--KELHKEY-NMTIILVSHSMEDV 208
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1221-1405 |
2.97e-16 |
|
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: 78.62 E-value: 2.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1221 EGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDG--VSWDSITLQQWRKAFGVIPQkvfifs 1297
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRpQSGAVLIDGepLDYSRKGLLERRQRVGLVFQ------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1298 gtfrknlDPYEQWSDQEIWK-VA--------DEVGLRSVIEQFPGKLDFV-LVDGGC-VLSHGHKQLMCLARSVLSKAKI 1366
Cdd:TIGR01166 76 -------DPDDQLFAADVDQdVAfgplnlglSEAEVERRVREALTAVGASgLRERPThCLSGGEKKRVAIAGAVAMRPDV 148
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 90421313 1367 LLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRIE 1405
Cdd:TIGR01166 149 LLLDEPTAGLDPAGREQMLAILRRLRAEgMTVVISTHDVD 188
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1211-1380 |
4.46e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 81.28 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGGNAI--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVswdSIT----- 1278
Cdd:COG1135 3 ELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTL----IRCINllerpTSGSVLVDGV---DLTalser 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1279 -LQQWRKAFGVIPQKvfiF----SGTFRKNLD-PYEQ--WSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvL 1346
Cdd:COG1135 76 eLRAARRKIGMIFQH---FnllsSRTVAENVAlPLEIagVPKAEIRKRVAEllelVGLSDKADAYPSQ-----------L 141
|
170 180 190
....*....|....*....|....*....|....
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVT 1380
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
439-622 |
4.59e-16 |
|
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: 79.30 E-value: 4.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG------------KIKHSGRISFC----SQFSWIMP--- 499
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGevrvaglvpwkrRKKFLRRIGVVfgqkTQLWWDLPvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 --GTIKEniIFGVSYDEYRYRsvikacqleedISKFAEKDNI--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:cd03267 115 sfYLLAA--IYDLPPARFKKR-----------LDELSELLDLeeLLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 576 GYLDVLTEKEI--FESCVCKLmaNKTRILVTSK-MEHLKK-ADKILILHEG 622
Cdd:cd03267 182 IGLDVVAQENIrnFLKEYNRE--RGTTVLLTSHyMKDIEAlARRVLVIDKG 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
438-586 |
4.73e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.67 E-value: 4.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-----------RISFCSQ-FSWIMPGTIKEN 505
Cdd:PRK10851 15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQhYALFRHMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFGVSYDEYRYR---SVI--KACQLEE--DISKFAEKDNivlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK10851 95 IAFGLTVLPRRERpnaAAIkaKVTQLLEmvQLAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
|
....*...
gi 90421313 579 DVLTEKEI 586
Cdd:PRK10851 168 DAQVRKEL 175
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
427-622 |
5.07e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 5.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 427 SLFFSNFSLL---GTPV----LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------- 486
Cdd:PRK13641 2 SIKFENVDYIyspGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 487 ----RISFCSQF--SWIMPGTIKENII-----FGVSYDEYRYRSV--IKACQLEEDiskfaekdniVLGEGGITLSGGQR 553
Cdd:PRK13641 82 klrkKVSLVFQFpeAQLFENTVLKDVEfgpknFGFSEDEAKEKALkwLKKVGLSED----------LISKSPFELSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 554 ARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHG 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
435-622 |
6.37e-16 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 77.47 E-value: 6.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 435 LLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRIsfcsqfswIMPGTIKENIIFGVSY-- 512
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP--------VTRRSPRDAIRAGIAYvp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 513 DEYRYRSVIkacqLEEDIskfaeKDNIVLGeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVC 592
Cdd:cd03215 82 EDRKREGLV----LDLSV-----AENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
170 180 190
....*....|....*....|....*....|.
gi 90421313 593 KLMANKTRILVTSKM-EHLKKADKILILHEG 622
Cdd:cd03215 150 LADAGKAVLLISSELdELLGLCDRILVMYEG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1212-1378 |
6.86e-16 |
|
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: 77.96 E-value: 6.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGEIQIDG--VSWDSITLQQWRK 1284
Cdd:cd03262 3 IKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINlleepDSGTIIIDGlkLTDDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQKVFIFSG-TFRKN--LDPYE--QWSDQEIWKVA----DEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMC 1355
Cdd:cd03262 77 KVGMVFQQFNLFPHlTVLENitLAPIKvkGMSKAEAEERAlellEKVGLADKADAYPAQ-----------LSGGQQQRVA 145
|
170 180
....*....|....*....|...
gi 90421313 1356 LARSVLSKAKILLLDEPSAHLDP 1378
Cdd:cd03262 146 IARALAMNPKVMLFDEPTSALDP 168
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1205-1399 |
8.00e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.98 E-value: 8.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1205 PSGGQMTVKDLTAKYT--EGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSIT--- 1278
Cdd:COG1116 3 AAAPALELRGVSKRFPtgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKpTSGEVLVDGKPVTGPGpdr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1279 ---LQQ-----WRK-----AFGVIPQKVfifsgtfrknldpyeqwSDQEIWKVADE----VGLRSVIEQFPGkldfvlvd 1341
Cdd:COG1116 83 gvvFQEpallpWLTvldnvALGLELRGV-----------------PKAERRERAREllelVGLAGFEDAYPH-------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1342 ggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVT----YQIIRRTLKQafADCTVIL 1399
Cdd:COG1116 138 ---QLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTrerlQDELLRLWQE--TGKTVLF 194
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
437-580 |
9.80e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 9.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--RISFCSQFSWIMPG-TIKENIIFGVS-- 511
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglRIGYLPQEPPLDDDlTVLDTVLDGDAel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 512 ---YDEYRyRSVIKACQLEEDISKFAEKDN---------------IVLGEGGI----------TLSGGQRARISLARAVY 563
Cdd:COG0488 90 ralEAELE-ELEAKLAEPDEDLERLAELQEefealggweaearaeEILSGLGFpeedldrpvsELSGGWRRRVALARALL 168
|
170
....*....|....*..
gi 90421313 564 KDADLYLLDSPFGYLDV 580
Cdd:COG0488 169 SEPDLLLLDEPTNHLDL 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1211-1402 |
1.04e-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: 1.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGEIQIDgvswDSITlqqwrkaFGVI 1289
Cdd:cd03221 2 ELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAgELEPDEGIVTWG----STVK-------IGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQkvfifsgtfrknldpyeqwsdqeiwkvadevglrsvieqfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLL 1369
Cdd:cd03221 69 EQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|...
gi 90421313 1370 DEPSAHLDPVTYQIIRRTLKQaFaDCTVILCEH 1402
Cdd:cd03221 95 DEPTNHLDLESIEALEEALKE-Y-PGTVILVSH 125
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
437-632 |
1.56e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 78.94 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTP----VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG---------------RISFCSQFS-- 495
Cdd:PRK13637 15 GTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkkvklsdirkKVGLVFQYPey 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 496 WIMPGTIKENIIFGVS----YDEYRYRSVIKACQLEE-DISKFAEKDNIvlgeggiTLSGGQRARISLARAVYKDADLYL 570
Cdd:PRK13637 95 QLFEETIEKDIAFGPInlglSEEEIENRVKRAMNIVGlDYEDYKDKSPF-------ELSGGQKRRVAIAGVVAMEPKILI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 571 LDSPFGYLDVLTEKEIFEScVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSE 632
Cdd:PRK13637 168 LDEPTAGLDPKGRDEILNK-IKELHKeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
437-635 |
1.58e-15 |
|
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: 77.47 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR--------------ISFCSQFSWIMPG-T 501
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKENIIFGVSydeYRYRSVIKAcQLEEDISKFAekdniVLGE-----GGiTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:cd03224 92 VEENLLLGAY---ARRRAKRKA-RLERVYELFP-----RLKErrkqlAG-TLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 577 YLDVLTEKEIFEsCVCKLMANKTRILVTSKMEH--LKKADKILILHEGSSYFYGTFSELQN 635
Cdd:cd03224 162 GLAPKIVEEIFE-AIRELRDEGVTILLVEQNARfaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
427-579 |
2.03e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 427 SLFFSNFSLL--GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEP---SEGKIKHSGR-------------I 488
Cdd:COG4136 1 MLSLENLTITlgGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRrltalpaeqrrigI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 489 SFcsQFSWIMPG-TIKENIIFGVSYD---EYRYRSVIKAcqLEE-DISKFAEKDNIvlgeggiTLSGGQRARISLARAVY 563
Cdd:COG4136 81 LF--QDDLLFPHlSVGENLAFALPPTigrAQRRARVEQA--LEEaGLAGFADRDPA-------TLSGGQRARVALLRALL 149
|
170
....*....|....*.
gi 90421313 564 KDADLYLLDSPFGYLD 579
Cdd:COG4136 150 AEPRALLLDEPFSKLD 165
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
432-622 |
2.26e-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: 74.41 E-value: 2.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFC--SQfswimpgtikeniifg 509
Cdd:cd03221 7 SKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGyfEQ---------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 510 vsydeyryrsvikacqleediskfaekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT----EKE 585
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESiealEEA 112
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 90421313 586 I--FESCVcklmanktrILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03221 113 LkeYPGTV---------ILVSHDRYFLDQvATKIIELEDG 143
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
437-588 |
2.28e-15 |
|
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: 76.68 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG----------------RISFCSQFSWIMPG 500
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENIIF-----GVSYDEYRYR--SVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLD 572
Cdd:cd03292 93 rNVYENVAFalevtGVPPREIRKRvpAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIAD 161
|
170
....*....|....*.
gi 90421313 573 SPFGYLDVLTEKEIFE 588
Cdd:cd03292 162 EPTGNLDPDTTWEIMN 177
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
438-622 |
2.42e-15 |
|
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: 78.07 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-----------------RISFCSQFSWIMPG 500
Cdd:cd03294 37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFALLPH 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENIIF-----GVSYDEYRYRS--VIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLD 572
Cdd:cd03294 117 rTVLENVAFglevqGVPRAEREERAaeALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 573 SPFGYLDVLTEKEIFESCVcKLMAN--KTRILVTSKM-EHLKKADKILILHEG 622
Cdd:cd03294 186 EAFSALDPLIRREMQDELL-RLQAElqKTIVFITHDLdEALRLGDRIAIMKDG 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
437-632 |
2.56e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 2.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK--HSGRISFCSQ-----------FSWI---MPG 500
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKlgETVKIGYFDQhqeeldpdktvLDELrdgAPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENII-----FGVSYDeyryrsvikacqleeDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:COG0488 407 GTEQEVRgylgrFLFSGD---------------DAFKPVGV-----------LSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 576 GYLDVLTeKEI-------FESCVcklmanktrILVTskmeH----LKK-ADKILILHEGS-SYFYGTFSE 632
Cdd:COG0488 461 NHLDIET-LEAleealddFPGTV---------LLVS----HdryfLDRvATRILEFEDGGvREYPGGYDD 516
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1211-1434 |
3.15e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 76.72 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYtegGNAILeNISFSISPGQRVGLLGRTGSGKSTLLSA---FLRLlnTEGEIQIDGVSWDSI---------- 1277
Cdd:COG3840 3 RLDDLTYRY---GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLiagFLPP--DSGRILWNGQDLTALppaerpvsml 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1278 ----------TLQQwRKAFGVIPqkvfifsgtfRKNLDPYEQwsdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLS 1347
Cdd:COG3840 77 fqennlfphlTVAQ-NIGLGLRP----------GLKLTAEQR---AQVEQALERVGLAGLLDRLPGQ-----------LS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1348 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPV----TYQIIRRTLKQAFAdcTVILCEHRIE-AMLECQQFLVIEENKVR 1422
Cdd:COG3840 132 GGQRQRVALARCLVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRERGL--TVLMVTHDPEdAARIADRVLLVADGRIA 209
|
250
....*....|..
gi 90421313 1423 QYDSIQKLLNER 1434
Cdd:COG3840 210 ADGPTAALLDGE 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
437-622 |
4.59e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 78.60 E-value: 4.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQ----FswimPG- 500
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRdvtglppekrnVGMVFQdyalF----PHl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENIIFG-----VSYDEYRYR--SVIKACQLEEdiskFAEK--DnivlgeggiTLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG3842 93 TVAENVAFGlrmrgVPKAEIRARvaELLELVGLEG----LADRypH---------QLSGGQQQRVALARALAPEPRVLLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 572 DSPFGYLDV-LTE------KEIFEScvcklmANKTRILVT-SKMEHLKKADKILILHEG 622
Cdd:COG3842 160 DEPLSALDAkLREemreelRRLQRE------LGITFIYVThDQEEALALADRIAVMNDG 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1224-1439 |
5.29e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 80.79 E-value: 5.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1224 NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDgvswdsitlqqWRKAFGVIPQKVFIFSGTFRKN 1303
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1304 LDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-VTYQ 1382
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1383 IIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKK 835
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
437-633 |
6.11e-15 |
|
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: 75.66 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR--------------ISFCSQFSWIMPG-T 501
Cdd:cd03218 12 KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKENI-----IFGVSYDEYRYRsvikacqLEEDISKFaekdNI--VLGEGGITLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:cd03218 92 VEENIlavleIRGLSKKEREEK-------LEELLEEF----HIthLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 575 FGYLDVLTEKEIfESCVCKLMANKTRILVTSK--MEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03218 161 FAGVDPIAVQDI-QKIIKILKDRGIGVLITDHnvRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1210-1402 |
6.38e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 76.23 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGEIQIDGV-----SWDSIT 1278
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgARVEGEILLDGEdiydpDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1279 LqqwRKAFGVIPQKVFIFSGTFRKN----------LDPYE-----QWS--DQEIWkvaDEVGlrsvieqfpGKLDfvlvD 1341
Cdd:COG1117 90 L---RRRVGMVFQKPNPFPKSIYDNvayglrlhgiKSKSEldeivEESlrKAALW---DEVK---------DRLK----K 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1342 GGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPV-TYQI---IRRtLKQafaDCTVILCEH 1402
Cdd:COG1117 151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIsTAKIeelILE-LKK---DYTIVIVTH 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1210-1422 |
6.83e-15 |
|
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: 75.48 E-value: 6.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKY--TEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSwdsiTLQQWRKA- 1285
Cdd:cd03266 2 ITADALTKRFrdVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEpDAGFATVDGFD----VVKEPAEAr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 --FGVIPQKVFIFSG-TFRKNLDPY-------EQWSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMC 1355
Cdd:cd03266 78 rrLGFVSDSTGLYDRlTARENLEYFaglyglkGDELTARLEELADRLGMEELLDRRVGGF-----------STGMRQKVA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1356 LARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRI-EAMLECQQFLVIEENKVR 1422
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgKCILFSTHIMqEVERLCDRVVVLHRGRVV 215
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1212-1441 |
6.91e-15 |
|
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: 75.51 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLqqwrKAFGVIp 1290
Cdd:TIGR03740 3 TKNLSKRF--GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRpTSGEIIFDGHPWTRKDL----HKIGSL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 qkvfIFSGTFRKNLDPYEQW---------SDQEIWKVADEVGLRsVIEQFPGKlDFvlvdggcvlSHGHKQLMCLARSVL 1361
Cdd:TIGR03740 76 ----IESPPLYENLTARENLkvhttllglPDSRIDEVLNIVDLT-NTGKKKAK-QF---------SLGMKQRLGIAIALL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1362 SKAKILLLDEPSAHLDPVTYQIIRRtLKQAFAD--CTVILCEHrieAMLECQQFL----VIEENKVRQYDSIQKLLNERS 1435
Cdd:TIGR03740 141 NHPKLLILDEPTNGLDPIGIQELRE-LIRSFPEqgITVILSSH---ILSEVQQLAdhigIISEGVLGYQGKINKSENLEK 216
|
....*.
gi 90421313 1436 LFRQAI 1441
Cdd:TIGR03740 217 LFVEVV 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1227-1434 |
1.09e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.41 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGvswDSITLQQWRKAFGVIPQKV---FIFSGT--F 1300
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAG---YHITPETGNKNLKKLRKKVslvFQFPEAqlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1301 R-----------KNLDPYEQWSDQEIWKVADEVGLR-SVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:PRK13641 100 EntvlkdvefgpKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFE-----------LSGGQMRRVAIAGVMAYEPEILC 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1369 LDEPSAHLDPVTyqiiRRTLKQAFADC-----TVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQKLLNER 1434
Cdd:PRK13641 169 LDEPAAGLDPEG----RKEMMQLFKDYqkaghTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1212-1416 |
1.10e-14 |
|
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: 73.23 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRLlnTEGEIQIDGvswdsitlqqwrkafgv 1288
Cdd:cd03216 3 LRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLmkiLSGLYKP--DSGEILVDG----------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 ipqkvfifsgtfrknlDPYEQWSDQEiwkvADEVGLRsVIEQfpgkldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:cd03216 62 ----------------KEVSFASPRD----ARRAGIA-MVYQ---------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1369 LDEPSAHLDPVT----YQIIRRtLKQafADCTVILCEHRIEAMLE-CQQFLVI 1416
Cdd:cd03216 106 LDEPTAALTPAEverlFKVIRR-LRA--QGVAVIFISHRLDEVFEiADRVTVL 155
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1218-1390 |
1.14e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.59 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1218 KYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSwdsitLQQW-RKAfgVIP-----Q 1291
Cdd:PRK15134 293 KRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQP-----LHNLnRRQ--LLPvrhriQ 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1292 KVF----------------IFSG--TFRKNLDPYEQwsDQEIWKVADEVGLRSVIEQ-FPGKldfvlvdggcvLSHGHKQ 1352
Cdd:PRK15134 366 VVFqdpnsslnprlnvlqiIEEGlrVHQPTLSAAQR--EQQVIAVMEEVGLDPETRHrYPAE-----------FSGGQRQ 432
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 90421313 1353 LMCLARSVLSKAKILLLDEPSAHLD-PVTYQIIR--RTLKQ 1390
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDkTVQAQILAllKSLQQ 473
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
436-588 |
1.38e-14 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 74.85 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 436 LGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-----------------RISFCSQFSWIM 498
Cdd:PRK11629 20 VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 499 PG-TIKENI-----IFGVSYDEY--RYRSVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYL 570
Cdd:PRK11629 100 PDfTALENVampllIGKKKPAEInsRALEMLAAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVL 168
|
170
....*....|....*...
gi 90421313 571 LDSPFGYLDVLTEKEIFE 588
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQ 186
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1210-1403 |
1.73e-14 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 72.57 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAkYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGEIQIdgvswdsitLQQWRK 1284
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF----RALAglwpwGSGRIGM---------PEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFgvIPQKVFIFSGTFRknldpyEQ----WSDqeiwkvadevglrsvieqfpgkldfvlvdggcVLSHGHKQLMCLARSV 1360
Cdd:cd03223 67 LF--LPQRPYLPLGTLR------EQliypWDD--------------------------------VLSGGEQQRLAFARLL 106
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90421313 1361 LSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAdcTVILCEHR 1403
Cdd:cd03223 107 LHKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1212-1399 |
1.85e-14 |
|
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: 76.25 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKY-TEGGNA-ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL----NTEGEIQIDGVSWDSITLQQWRKA 1285
Cdd:COG0444 4 VRNLKVYFpTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppgITSGEILFDGEDLLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 ----FGVIPQkvfifsgtfrknlDPY----------EQ----------WSDQEIWKVADE----VGL---RSVIEQFPGK 1334
Cdd:COG0444 84 rgreIQMIFQ-------------DPMtslnpvmtvgDQiaeplrihggLSKAEARERAIEllerVGLpdpERRLDRYPHE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1335 ldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDpVT--YQIIR--RTLKQAFaDCTVIL 1399
Cdd:COG0444 151 -----------LSGGMRQRVMIARALALEPKLLIADEPTTALD-VTiqAQILNllKDLQREL-GLAILF 206
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
437-633 |
2.15e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 75.44 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTP----VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI--------------------KHSGrISFcs 492
Cdd:PRK13634 15 KTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagkknkklkplrKKVG-IVF-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 493 QF--SWIMPGTIKENIIFG-----VSYDE--YRYRSVIKACQLEEDI---SKFAekdnivlgeggitLSGGQRARISLAR 560
Cdd:PRK13634 92 QFpeHQLFEETVEKDICFGpmnfgVSEEDakQKAREMIELVGLPEELlarSPFE-------------LSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 561 AVYKDADLYLLDSPFGYLDVLTEKEIFEscvcklM-------ANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSE 632
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMME------MfyklhkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232
|
.
gi 90421313 633 L 633
Cdd:PRK13634 233 I 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1227-1382 |
2.19e-14 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 77.80 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSIT---LQQWRKAFGVIPQkvfifsgtfrkn 1303
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQ------------ 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1304 lDPY---------------------EQWSDQE----IWKVADEVGL-RSVIEQFPGKldfvlvdggcvLSHGHKQLMCLA 1357
Cdd:COG4172 370 -DPFgslsprmtvgqiiaeglrvhgPGLSAAErrarVAEALEEVGLdPAARHRYPHE-----------FSGGQRQRIAIA 437
|
170 180
....*....|....*....|....*.
gi 90421313 1358 RSVLSKAKILLLDEP-SAhLDpVTYQ 1382
Cdd:COG4172 438 RALILEPKLLVLDEPtSA-LD-VSVQ 461
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
448-609 |
2.81e-14 |
|
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: 74.37 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 448 IERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-RISFCSQF-SWIMPGTIKE---NIIFGVSYDEYRYRSVIK 522
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYiKADYEGTVRDllsSITKDFYTHPYFKTEIAK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 523 ACQLEEDIskfaekDNIVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVltEKEIFESCVCK---LMANKT 599
Cdd:cd03237 102 PLQIEQIL------DREVP-----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV--EQRLMASKVIRrfaENNEKT 168
|
170
....*....|
gi 90421313 600 RILVtskmEH 609
Cdd:cd03237 169 AFVV----EH 174
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
441-622 |
3.40e-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: 73.65 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR----------ISF--CSQFSWImpgTIKENIIF 508
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrmVVFqnYSLLPWL---TVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 509 GVSydeyryrsvikacQLEEDISKfAEKDNIV--------LGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:TIGR01184 78 AVD-------------RVLPDLSK-SERRAIVeehialvgLTEAAdkrpGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 577 YLDVLTEKEIFEscvcKLM-----ANKTRILVTSKM-EHLKKADKILILHEG 622
Cdd:TIGR01184 144 ALDALTRGNLQE----ELMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1212-1430 |
3.91e-14 |
|
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: 73.17 E-value: 3.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDG--VSWDSITLqqwRKAFGV 1288
Cdd:cd03265 3 VENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGhdVVREPREV---RRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVFIFSG-TFRKNLD--------PYEQWsDQEIWKVADEVGLrsvieqfpgkLDFV--LVdggCVLSHGHKQLMCLA 1357
Cdd:cd03265 78 VFQDLSVDDElTGWENLYiharlygvPGAER-RERIDELLDFVGL----------LEAAdrLV---KTYSGGMRRRLEIA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1358 RSVLSKAKILLLDEPSAHLDPVT----YQIIrRTLKQAFaDCTVILCEHRI-EAMLECQQFLVIEENKVRQYDSIQKL 1430
Cdd:cd03265 144 RSLVHRPEVLFLDEPTIGLDPQTrahvWEYI-EKLKEEF-GMTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
437-622 |
4.37e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 75.25 E-value: 4.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPG-TIK 503
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 EN-IIFGvsydeyRYRSvIKACQLEEDISKFAE------KDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK13536 133 ENlLVFG------RYFG-MSTREIEAVIPSLLEfarlesKADARVSD----LSGGMKRRLTLARALINDPQLLILDEPTT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90421313 577 YLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAG 248
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
440-628 |
4.79e-14 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 73.07 E-value: 4.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEpsEGKIKhSGRI----------------SFCSQFSWIMPG-TI 502
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTT-SGQIlfngqprkpdqfqkcvAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 503 KENIIFGVsydeyryRSVIKACQLEEDISKFAEkdNIVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDS 573
Cdd:cd03234 99 RETLTYTA-------ILRLPRKSSDAIRKKRVE--DVLLRDLALTriggnlvkgISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 574 PFGYLDVLTEKEIFEscVCKLMANKTRILVTS----KMEHLKKADKILILHEGSSYFYG 628
Cdd:cd03234 170 PTSGLDSFTALNLVS--TLSQLARRNRIVILTihqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1209-1421 |
4.88e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 73.89 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1209 QMTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSWDSITLQQWRKAFG 1287
Cdd:PRK11231 2 TLRTENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSGTFRKNL-----DPY-EQW-----SDQEIWKVADEvglRSVIEQFPGKLdfvLVDggcvLSHGHKQLMCL 1356
Cdd:PRK11231 80 LLPQHHLTPEGITVRELvaygrSPWlSLWgrlsaEDNARVNQAME---QTRINHLADRR---LTD----LSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDpVTYQI----IRRTLKQAFAdcTVILCEHRI-EAMLECQQFLVIEENKV 1421
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD-INHQVelmrLMRELNTQGK--TVVTVLHDLnQASRYCDHLVVLANGHV 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1212-1377 |
5.20e-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: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNteGEIQIDGvswDSITLQQ-WRkaFGVIP 1290
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKILA--GELEPDS---GEVSIPKgLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSGT------------FRKNLDPYEQ------WSDQEIWKVA------DEVG---LRSVIEQFPGKLDFVLVDGG 1343
Cdd:COG0488 68 QEPPLDDDLtvldtvldgdaeLRALEAELEEleaklaEPDEDLERLAelqeefEALGgweAEARAEEILSGLGFPEEDLD 147
|
170 180 190
....*....|....*....|....*....|....*..
gi 90421313 1344 C---VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:COG0488 148 RpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1222-1432 |
5.36e-14 |
|
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: 73.14 E-value: 5.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVswDSITLQQWRKAFGVIPQKVFIFSGT- 1299
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDsGKILLNGK--DITNLPPEKRDISYVPQNYALFPHMt 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1300 --------FRKNLDPYEQwSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDE 1371
Cdd:cd03299 88 vykniaygLKKRKVDKKE-IERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1372 PSAHLDPVTYQIIRRTLKQAF--ADCTVILCEHR-IEAMLECQQFLVIEENKVRQYDSIQKLLN 1432
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
437-635 |
5.93e-14 |
|
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: 72.85 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-I---------------SFcsQFSWIMPG 500
Cdd:cd03219 12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEdItglppheiarlgigrTF--QIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKdniVLGEGGI---------TLSGGQRARISLARAVYKDADLYL 570
Cdd:cd03219 90 lTVLENVMVAAQARTGSGLLLARARREEREARERAEE---LLERVGLadladrpagELSYGQQRRLEIARALATDPKLLL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 571 LDSPFGYLDvLTEKEIFESCVCKLMANKTRILVTskmEH-----LKKADKILILHEGSSYFYGTFSELQN 635
Cdd:cd03219 167 LDEPAAGLN-PEETEELAELIRELRERGITVLLV---EHdmdvvMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
440-648 |
6.20e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.46 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPG-TIKENI 506
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQFDNLDPDfTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 I-----FGVSYDEYRYR--SVIKACQLEEdiskfaeKDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13537 102 LvfgryFGLSAAAARALvpPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 580 VLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQNLQpdfssklMGCD 648
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESE-------IGCD 233
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
437-623 |
7.56e-14 |
|
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: 72.65 E-value: 7.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQFSWIMPG-TIKE 504
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFG-----VSYDEYRYR--SVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03300 92 NIAFGlrlkkLPKAEIKERvaEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKVLLLDEPLGA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 90421313 578 LDV-LTEKEIFESCVCKLMANKTRILVT-SKMEHLKKADKILILHEGS 623
Cdd:cd03300 161 LDLkLRKDMQLELKRLQKELGITFVFVThDQEEALTMSDRIAVMNKGK 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1222-1417 |
1.19e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 74.10 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSiTLQQWRKAFGVIPQkvfiFSG-- 1298
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPA-RARLARARIGVVPQ----FDNld 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1299 ---TFRKNLDPYEQW---SDQEIwkvadEVGLRSVIE--QFPGKLDFVLVDggcvLSHGHKQLMCLARSVLSKAKILLLD 1370
Cdd:PRK13536 127 lefTVRENLLVFGRYfgmSTREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 90421313 1371 EPSAHLDPVTYQIIRRTLKQAFADC-TVILCEHRI-EAMLECQQFLVIE 1417
Cdd:PRK13536 198 EPTTGLDPHARHLIWERLRSLLARGkTILLTTHFMeEAERLCDRLCVLE 246
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1210-1405 |
1.43e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.12 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL--LNTE----GEIQIDGVSW-----DSIT 1278
Cdd:PRK14239 6 LQVSDLSVYY--NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtitGSIVYNGHNIysprtDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1279 LqqwRKAFGVIPQKVFIFSGTFRKNLdPY----EQWSDQEIWKVADEVGLR--SVIEQFPGKLDfvlvDGGCVLSHGHKQ 1352
Cdd:PRK14239 84 L---RKEIGMVFQQPNPFPMSIYENV-VYglrlKGIKDKQVLDEAVEKSLKgaSIWDEVKDRLH----DSALGLSGGQQQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1353 LMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIE 1405
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQ 208
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
440-628 |
1.58e-13 |
|
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: 71.24 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPG-TIKENI 506
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 IF-----GVSYDEYRYRsvikacqLEEDISKFAEKDNIVLGEGGitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 581
Cdd:cd03266 100 EYfaglyGLKGDELTAR-------LEELADRLGMEELLDRRVGG--FSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVM 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 90421313 582 TEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYG 628
Cdd:cd03266 171 ATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1211-1390 |
1.70e-13 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 73.59 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSA---FLRLlnTEGEIQIDGVSWDsitlqqwrkafG 1287
Cdd:COG3842 7 ELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMiagFETP--DSGRILLDGRDVT-----------G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQK-----VF--------------I-FSGTFRKnldpyeqWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdgg 1343
Cdd:COG3842 72 LPPEKrnvgmVFqdyalfphltvaenVaFGLRMRG-------VPKAEIRARVAEllelVGLEGLADRYPHQ--------- 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90421313 1344 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ 1390
Cdd:COG3842 136 --LSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRR 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1211-1437 |
2.44e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.26 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSITLQQWRK- 1284
Cdd:COG1118 4 EVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTL----LRIIAgletpDSGRIVLNGRDLFTNLPPRERRv 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 -------------------AFG--VIPqkvfifsgtfrknldpyeqWSDQEIWKVADE----VGLRSVIEQFPGKldfvl 1339
Cdd:COG1118 78 gfvfqhyalfphmtvaeniAFGlrVRP-------------------PSKAEIRARVEEllelVQLEGLADRYPSQ----- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1340 vdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-VTYQiIRRTLKQAFAD--CTVILCEH-RIEAMLECQQFLV 1415
Cdd:COG1118 134 ------LSGGQRQRVALARALAVEPEVLLLDEPFGALDAkVRKE-LRRWLRRLHDElgGTTVFVTHdQEEALELADRVVV 206
|
250 260
....*....|....*....|...
gi 90421313 1416 IEENKVRQYDSIQKLLNE-RSLF 1437
Cdd:COG1118 207 MNQGRIEQVGTPDEVYDRpATPF 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
437-622 |
2.69e-13 |
|
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: 74.17 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI----------------KHSGRISFCSQ--FSWIM 498
Cdd:COG1123 277 GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklsrrslrELRRRVQMVFQdpYSSLN 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 499 PG-TIKENIIFGVsydeyRYRSVIKACQLEEDISKFAEKdniV-LGEGGI-----TLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG1123 357 PRmTVGDIIAEPL-----RLHGLLSRAERRERVAELLER---VgLPPDLAdryphELSGGQRQRVAIARALALEPKLLIL 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 572 DSPFGYLDVLTEKEIFEscvckLMA------NKTRILVT---SKMEHLkkADKILILHEG 622
Cdd:COG1123 429 DEPTSALDVSVQAQILN-----LLRdlqrelGLTYLFIShdlAVVRYI--ADRVAVMYDG 481
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
439-622 |
2.80e-13 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 71.48 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPGTIKEN 505
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKe 585
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATEN- 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 90421313 586 IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRG 230
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1227-1439 |
2.87e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.16 E-value: 2.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLrllnteGEIQidGVSWDSITLqqwRKAFGVIPQKVFIFSGTFRKNL-- 1304
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAML------GELP--PRSDASVVI---RGTVAYVPQVSWIFNATVRDNIlf 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1305 -DPYEQwsdQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP-VTYQ 1382
Cdd:PLN03130 702 gSPFDP---ERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQ 778
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1383 IIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQ 1439
Cdd:PLN03130 779 VFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK 835
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
448-580 |
3.01e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 74.46 E-value: 3.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 448 IERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFswIMP---GTIKENI-----IFGVSYdeyrYRS 519
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQY--IKPdydGTVEDLLrsitdDLGSSY----YKS 435
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 520 -VIKACQLEedisKFAEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK13409 436 eIIKPLQLE----RLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1210-1440 |
3.42e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 71.80 E-value: 3.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDG--VSWDSITLQQWRKAF 1286
Cdd:PRK13636 6 LKVEELNYNYSDGTHA-LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGkpIDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKV--FIFSGTFRKNLD--PYE-QWSDQEIWKVADEVGLRSVIEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVL 1361
Cdd:PRK13636 85 GMVFQDPdnQLFSASVYQDVSfgAVNlKLPEDEVRKRVDNALKRTGIEHLKDKPTH-------CLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1362 SKAKILLLDEPSAHLDPVTYQIIRRTLKQAFA--DCTVILCEHRIEAM-LECQQFLVIEENKVRQYDSIQKLLNERSLFR 1438
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
..
gi 90421313 1439 QA 1440
Cdd:PRK13636 238 KV 239
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
437-623 |
3.47e-13 |
|
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: 70.99 E-value: 3.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRI-------SFCSQFSWIM--------PG- 500
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPvtrrrrkAFRRRVQMVFqdpyaslhPRh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENI-----IFGVSYDEYRYRSVIKACQLEEDI-SKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:COG1124 97 TVDRILaeplrIHGLPDREERIAELLEQVGLPPSFlDRYPHQ-----------LSGGQRQRVAIARALILEPELLLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90421313 575 FGYLDVLTEKEIFEsCVCKLMA--NKTRILVT---SKMEHLkkADKILILHEGS 623
Cdd:COG1124 166 TSALDVSVQAEILN-LLKDLREerGLTYLFVShdlAVVAHL--CDRVAVMQNGR 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
437-662 |
3.83e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.95 E-value: 3.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQFSWIMPG-TIKE 504
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFGVSYDEYRyRSVIKAcQLEEDIS-----KFAEKDNIvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK11607 111 NIAFGLKQDKLP-KAEIAS-RVNEMLGlvhmqEFAKRKPH-------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 580 vlteKEIFESCVCKLMANKTRILVTSKM------EHLKKADKILILHEGSSYFYGTFSEL-QNLQPDFSSKLMG-CDSFD 651
Cdd:PRK11607 182 ----KKLRDRMQLEVVDILERVGVTCVMvthdqeEAMTMAGRIAIMNRGKFVQIGEPEEIyEHPTTRYSAEFIGsVNVFE 257
|
250
....*....|.
gi 90421313 652 QFSAERRNSIL 662
Cdd:PRK11607 258 GVLKERQEDGL 268
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1222-1402 |
4.56e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN------TEGEIQIDGVSWDSITLQ--QWRKAFGVipqkV 1293
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYSPDVDpiEVRREVGM----V 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1294 FIFSGTF---------------------RKNLDPYEQWSDQE--IWkvaDEVGLRsvIEQFPGKLdfvlvdggcvlSHGH 1350
Cdd:PRK14267 91 FQYPNPFphltiydnvaigvklnglvksKKELDERVEWALKKaaLW---DEVKDR--LNDYPSNL-----------SGGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1351 KQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEH 1402
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1231-1432 |
4.68e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 70.38 E-value: 4.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1231 SFSISPGQRVGLLGRTGSGKSTLLS---AFLRllNTEGEIQIDGVswDSITLQQWRKAFGVIPQKVFIFSG-TFRKN--- 1303
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNliaGFLT--PASGSLTLNGQ--DHTTTPPSRRPVSMLFQENNLFSHlTVAQNigl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1304 -------LDPYEQWSDQEIwkvADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 1376
Cdd:PRK10771 95 glnpglkLNAAQREKLHAI---ARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1377 DPVTYQIIRRTLKQAFAD--CTVILCEHRIE-AMLECQQFLVIEENKVrQYD-SIQKLLN 1432
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQErqLTLLMVSHSLEdAARIAPRSLVVADGRI-AWDgPTDELLS 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1210-1422 |
5.71e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 5.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:PRK09536 4 IDVSDLSVEF--GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKV---FIFSG--TFRKNLDPYEQWSDQeiWKVADEVGLRSVIEQfPGKLDFV--LVDGgcvLSHGHKQLMCLARSVL 1361
Cdd:PRK09536 82 VPQDTslsFEFDVrqVVEMGRTPHRSRFDT--WTETDRAAVERAMER-TGVAQFAdrPVTS---LSGGERQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1362 SKAKILLLDEPSAHLDpVTYQIirRTLK--QAFADC--TVILCEHRIE-AMLECQQFLVIEENKVR 1422
Cdd:PRK09536 156 QATPVLLLDEPTASLD-INHQV--RTLElvRRLVDDgkTAVAAIHDLDlAARYCDELVLLADGRVR 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1211-1390 |
5.94e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTakYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDG---VSWDSITLQQW 1282
Cdd:PRK13548 4 EARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALSgelspDSGEVRLNGrplADWSPAELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1283 RkafGVIPQKVfifSGTFrknldPyeqwsdqeiWKVADEVGL-RSVIEQFPGKLDfVLVDG-----GCV---------LS 1347
Cdd:PRK13548 78 R---AVLPQHS---SLSF-----P---------FTVEEVVAMgRAPHGLSRAEDD-ALVAAalaqvDLAhlagrdypqLS 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90421313 1348 HGHKQLMCLARsVL-------SKAKILLLDEPSAHLDPVTYQIIRRTLKQ 1390
Cdd:PRK13548 137 GGEQQRVQLAR-VLaqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQ 185
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1211-1390 |
6.36e-13 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 71.76 E-value: 6.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYTEGGNAI--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGV---SWDSITLQ 1280
Cdd:PRK11153 3 ELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINllerpTSGRVLVDGQdltALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1281 QWRKAFGVIPQKVFIFSG-TFRKNLD-PYE--QWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQ 1352
Cdd:PRK11153 79 KARRQIGMIFQHFNLLSSrTVFDNVAlPLElaGTPKAEIKARVTEllelVGLSDKADRYPAQ-----------LSGGQKQ 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 90421313 1353 LMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ 1390
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKD 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
432-614 |
6.46e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.21 E-value: 6.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMP 499
Cdd:PRK13540 8 DFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdlctyqkQLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 G-TIKENIIFGVSYDEyryrsviKACQLEEDISKFAEKDNIVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK13540 88 YlTLRENCLYDIHFSP-------GAVGITELCRLFSLEHLIDYPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 90421313 579 DVLTekeiFESCVCKLMANKTR---ILVTSKME-HLKKAD 614
Cdd:PRK13540 159 DELS----LLTIITKIQEHRAKggaVLLTSHQDlPLNKAD 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1226-1402 |
6.56e-13 |
|
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: 69.61 E-value: 6.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1226 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL----NTEGEIQIDGVswdSITLQQWRKAFGVIPQkvfifSGTFR 1301
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegggTTSGQILFNGQ---PRKPDQFQKCVAYVRQ-----DDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1302 KNLDPYEQW------------SDQEIWKVADEVGLRSV-IEQFPGKldfvLVDGgcvLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:cd03234 94 PGLTVRETLtytailrlprksSDAIRKKRVEDVLLRDLaLTRIGGN----LVKG---ISGGERRRVSIAVQLLWDPKVLI 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 90421313 1369 LDEPSAHLDPVT-YQIIrRTLKQ-AFADCTVILCEH 1402
Cdd:cd03234 167 LDEPTSGLDSFTaLNLV-STLSQlARRNRIVILTIH 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
437-635 |
6.87e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 72.91 E-value: 6.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMG--ELEPSEGKIKHsgRISFCSQFSWIMP------------GTI 502
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIY--HVALCEKCGYVERpskvgepcpvcgGTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 503 KENIIFGVSYDEYRYRSVIK--ACQLEEDISKFAEK---DNIV--LGEGG----------------------IT-----L 548
Cdd:TIGR03269 90 EPEEVDFWNLSDKLRRRIRKriAIMLQRTFALYGDDtvlDNVLeaLEEIGyegkeavgravdliemvqlshrIThiardL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSK----MEHLkkADKILILHEGSS 624
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpevIEDL--SDKAIWLENGEI 247
|
250
....*....|.
gi 90421313 625 YFYGTFSELQN 635
Cdd:TIGR03269 248 KEEGTPDEVVA 258
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
437-604 |
7.35e-13 |
|
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: 70.11 E-value: 7.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGK----------------IKHsgRISFCSQF--SWIM 498
Cdd:COG1119 15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrlfgerrggedvweLRK--RIGLVSPAlqLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 499 PGTIKENII----FGVS--YDEYRYRSVIKACQ-LEE-DISKFAEKDnivLGeggiTLSGGQRARISLARAVYKDADLYL 570
Cdd:COG1119 93 RDETVLDVVlsgfFDSIglYREPTDEQRERARElLELlGLAHLADRP---FG----TLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 90421313 571 LDSPFGYLDvLTEKEIFESCVCKLMAN--KTRILVT 604
Cdd:COG1119 166 LDEPTAGLD-LGARELLLALLDKLAAEgaPTLVLVT 200
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
437-646 |
8.34e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 70.40 E-value: 8.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGrISFCSqFSwIMPGTIK-ENIIFGVSYDEY 515
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-IDTGD-FS-KLQGIRKlVGIVFQNPETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 516 RYRSVikacqlEEDIS-----------KFAEKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:PRK13644 91 VGRTV------EEDLAfgpenlclppiEIRKRVDRALAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 576 GYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGtfsELQNLQPDFSSKLMG 646
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEG---EPENVLSDVSLQTLG 232
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1205-1421 |
8.84e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.09 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1205 PSGGQMTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLL-----NTEGEIQIDGVSWDSIT- 1278
Cdd:PRK11247 8 NQGTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTL----LRLLagletPSAGELLAGTAPLAEARe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1279 ----------LQQWRKafgVIPQKVFIFSGtfrknldpyeQWSDQEIwKVADEVGLRSVIEQFPGkldfvlvdggcVLSH 1348
Cdd:PRK11247 82 dtrlmfqdarLLPWKK---VIDNVGLGLKG----------QWRDAAL-QALAAVGLADRANEWPA-----------ALSG 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1349 GHKQLMCLARSVLSKAKILLLDEPSAHLDPVT----YQIIRRT-LKQAFadcTVILCEHRI-EAMLECQQFLVIEENKV 1421
Cdd:PRK11247 137 GQKQRVALARALIHRPGLLLLDEPLGALDALTriemQDLIESLwQQHGF---TVLLVTHDVsEAVAMADRVLLIEEGKI 212
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1210-1433 |
9.86e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 69.52 E-value: 9.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGEIQIDG---VSWDsiTLQQWRKA 1285
Cdd:PRK11614 6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgDPRATSGRIVFDGkdiTDWQ--TAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQKVFIFSG-TFRKNLDPYEQWSDQEIWKVAdevgLRSVIEQFPGKLDFVLVDGGcVLSHGHKQLMCLARSVLSKA 1364
Cdd:PRK11614 82 VAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQER----IKWVYELFPRLHERRIQRAG-TMSGGEQQMLAIGRALMSQP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1365 KILLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRI-EAMLECQQFLVIEENKVRQYDSIQKLL-NE 1433
Cdd:PRK11614 157 RLLLLDEPSLGLAPIIIQQIFDTIEQLREQgMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALLaNE 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
437-622 |
1.05e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.11 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTP----VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-ISFCSQF---SWI-------MPGT 501
Cdd:COG1101 14 GTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEYkraKYIgrvfqdpMMGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 -----IKENII------------FGVSYDEY-RYRSVIKACQ--LEEDIskfaeKDNIVLgeggitLSGGQRARISLARA 561
Cdd:COG1101 94 apsmtIEENLAlayrrgkrrglrRGLTKKRReLFRELLATLGlgLENRL-----DTKVGL------LSGGQRQALSLLMA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 562 VYKDADLYLLDSPFGYLD------V--LTEKEIFESCVCKLManktrilVTSKMEH-LKKADKILILHEG 622
Cdd:COG1101 163 TLTKPKLLLLDEHTAALDpktaalVleLTEKIVEENNLTTLM-------VTHNMEQaLDYGNRLIMMHEG 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1211-1390 |
1.24e-12 |
|
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: 69.11 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSwdsITL----QQWRKA 1285
Cdd:cd03218 2 RAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKpDSGKILLDGQD---ITKlpmhKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQKVFIFSG-TFRKNL--------DPYEQWSDqEIWKVADEVGLRSVIEQFpgkldfvlvdgGCVLSHGHKQLMCL 1356
Cdd:cd03218 77 IGYLPQEASIFRKlTVEENIlavleirgLSKKEREE-KLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEI 144
|
170 180 190
....*....|....*....|....*....|....
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ 1390
Cdd:cd03218 145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
431-636 |
1.36e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.59 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 431 SNFSLLGTPVL-KDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--RISFCSQFSwiMPG-TIKENI 506
Cdd:PLN03073 514 ASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAkvRMAVFSQHH--VDGlDLSSNP 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 IFgvsYDEYRYRSVIKAcQLEEDISKFAEKDNIVLgEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVltekEI 586
Cdd:PLN03073 592 LL---YMMRCFPGVPEQ-KLRAHLGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL----DA 662
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 587 FESCVCKLMANKTRILVTSKMEHL--KKADKILILHEGS-SYFYGTFSELQNL 636
Cdd:PLN03073 663 VEALIQGLVLFQGGVLMVSHDEHLisGSVDELWVVSEGKvTPFHGTFHDYKKT 715
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
437-628 |
1.46e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.06 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPS---EGKI------------KHSGRISFCSQFSWIMPG- 500
Cdd:cd03233 19 KIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIhyngipykefaeKYPGEIIYVSEEDVHFPTl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENIIFGVSydeyryrsvikaCQleediskfaeKDNIVLGeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03233 99 TVRETLDFALR------------CK----------GNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90421313 581 LTEKEIFeSCVcKLMANKTR------ILVTSKmEHLKKADKILILHEGSSYFYG 628
Cdd:cd03233 152 STALEIL-KCI-RTMADVLKtttfvsLYQASD-EIYDLFDKVLVLYEGRQIYYG 202
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1210-1456 |
1.56e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 69.72 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGG-------NAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLL-----NTEGEIQIDGVSWDSI 1277
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLvglesPSQGNVSWRGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1278 TLQQWRkAFGVIPQKVF---------------IFSGTFRK--NLDPYEQwsDQEIWKVADEVGLR-SVIEQFPGKldfvl 1339
Cdd:PRK10419 80 NRAQRK-AFRRDIQMVFqdsisavnprktvreIIREPLRHllSLDKAER--LARASEMLRAVDLDdSVLDKRPPQ----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1340 vdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPV-TYQIIR--RTLKQAFaDCTVILCEHRIEaMLE--CQQFL 1414
Cdd:PRK10419 152 ------LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVlQAGVIRllKKLQQQF-GTACLFITHDLR-LVErfCQRVM 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 90421313 1415 VIEENKVRQYDSIQKLLNERS----LFRQAISPSdrvklFPHRNSS 1456
Cdd:PRK10419 224 VMDNGQIVETQPVGDKLTFSSpagrVLQNAVLPA-----FPVRRRT 264
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
440-622 |
1.62e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG----------KIKHSGRISFcsQFSWIMP-GTIKENIIF 508
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGellagtaplaEAREDTRLMF--QDARLLPwKKVIDNVGL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 509 GVSYD-EYRYRSVIKACQLEEDIskfaekdnivlGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIf 587
Cdd:PRK11247 105 GLKGQwRDAALQALAAVGLADRA-----------NEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEM- 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 90421313 588 ESCVCKLMANK--TRILVTSKM-EHLKKADKILILHEG 622
Cdd:PRK11247 173 QDLIESLWQQHgfTVLLVTHDVsEAVAMADRVLLIEEG 210
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
443-580 |
2.00e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 443 DINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK------HSGRISFCSQFSWI--MPGtIK------ENIIF 508
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLLYLghQPG-IKteltalENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 509 gvsydeyryrsvikACQLEEDISKFAEKDniVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13538 98 --------------YQRLHGPGDDEALWE--ALAQVGLagfedvpvrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
.
gi 90421313 580 V 580
Cdd:PRK13538 162 K 162
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1227-1426 |
2.19e-12 |
|
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: 68.51 E-value: 2.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDG-VSWDSitLQQWRKAFGVI-PQKvfifsGTFRKN 1303
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGlVPWKR--RKKFLRRIGVVfGQK-----TQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1304 LDPYEQWS-DQEIWKVaDEVGLRSVIEQFPGKLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVT 1380
Cdd:cd03267 110 LPVIDSFYlLAAIYDL-PPARFKKRLDELSELLDLEELLDTPVrqLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 1381 YQIIRRTLKQAFAD--CTVILCEHR---IEAMleCQQFLVIEENKVrQYDS 1426
Cdd:cd03267 189 QENIRNFLKEYNRErgTTVLLTSHYmkdIEAL--ARRVLVIDKGRL-LYDG 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1212-1440 |
2.20e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 69.38 E-value: 2.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGEIQIDGVSWDSITLQQWRKAFGVIP 1290
Cdd:PRK13647 7 VEDLHFRYKDGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKV--FIFSGTFRKNL--DPYEQWSDQEIWKVADEVGLRSV-IEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVLSKAK 1365
Cdd:PRK13647 86 QDPddQVFSSTVWDDVafGPVNMGLDKDEVERRVEEALKAVrMWDFRDKPPY-------HLSYGQKKRVAIAGVLAMDPD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1366 ILLLDEPSAHLDP----VTYQIIRRTLKQAfadCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSiQKLLNERSLFRQA 1440
Cdd:PRK13647 159 VIVLDEPMAYLDPrgqeTLMEILDRLHNQG---KTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDEDIVEQA 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1210-1378 |
2.21e-12 |
|
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: 67.38 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTakYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIqidgvSWDSITLQQWRK 1284
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTL----LRILAgllrpDSGEV-----RWNGTPLAEQRD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 afgvIPQKVFIFSG---------TFRKNLD---PYEQWSDQEIWKVADEVGLRSvIEQFPGKldfvlvdggcVLSHGHKQ 1352
Cdd:TIGR01189 70 ----EPHENILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPAA----------QLSAGQQR 134
|
170 180
....*....|....*....|....*.
gi 90421313 1353 LMCLARSVLSKAKILLLDEPSAHLDP 1378
Cdd:TIGR01189 135 RLALARLWLSRRPLWILDEPTTALDK 160
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
441-634 |
2.47e-12 |
|
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: 67.78 E-value: 2.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQFSWIMPG-TIKENI- 506
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvreprevrrRIGIVFQDLSVDDElTGWENLy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 ----IFGVSYDEYRYR--SVIKACQLEEdiskfaEKDNIVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03265 96 iharLYGVPGAERRERidELLDFVGLLE------AADRLVK-----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 581 LTEKEIFEScVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQ 634
Cdd:cd03265 165 QTRAHVWEY-IEKLKEefGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
440-628 |
2.62e-12 |
|
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: 67.60 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGqLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG------------RISFCSQ-FSWIMPGTIKE-- 504
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqpqklrrRIGYLPQeFGVYPNFTVREfl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 ---NIIFGVSYDEYRYR--SVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03264 94 dyiAWLKGIPSKEVKARvdEVLELVNLGDRAKKKIGS-----------LSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90421313 580 VlTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYG 628
Cdd:cd03264 163 P-EERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
447-580 |
2.64e-12 |
|
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: 71.35 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 447 KIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQF-SWIMPGTIKENI------IFGVSYdeyrYRS 519
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQYiSPDYDGTVEEFLrsantdDFGSSY----YKT 437
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 520 -VIKACQLEedisKFAEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:COG1245 438 eIIKPLGLE----KLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1209-1402 |
2.69e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.40 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1209 QMTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN------TEGEIQIDGVSWDSITLQQW 1282
Cdd:PRK14247 3 KIEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1283 RKAFGVIPQ------KVFIFSGTF-----------RKNLDPYEQWS--DQEIWkvaDEVGLRsvIEQFPGKLdfvlvdgg 1343
Cdd:PRK14247 81 RRRVQMVFQipnpipNLSIFENVAlglklnrlvksKKELQERVRWAleKAQLW---DEVKDR--LDAPAGKL-------- 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1344 cvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEH 1402
Cdd:PRK14247 148 ---SGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
438-633 |
2.73e-12 |
|
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: 67.99 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGeLE-PSEGKIKHSG----------------RISFCSQ-FSWIMP 499
Cdd:cd03258 18 VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LErPTSGSVLVDGtdltllsgkelrkarrRIGMIFQhFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENI-----IFGVSyDEYRYRSV---IKACQLEEDISKFAEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLL 571
Cdd:cd03258 97 RTVFENValpleIAGVP-KAEIEERVlelLELVGLEDKADAYPA-----------QLSGGQKQRVGIARALANNPKVLLC 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 572 DSPFGYLDVLTEKEIFE---SCVCKLmaNKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:cd03258 165 DEATSALDPETTQSILAllrDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
435-622 |
3.50e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 70.82 E-value: 3.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 435 LLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR--------------ISFCS----QFSW 496
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvrirsprdairagIAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 497 IMPGTIKENIIFgVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLgeGGI-----TLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG1129 342 VLDLSIRENITL-ASLDRLSRGGLLDRRRERALAEEYIKRLRIKT--PSPeqpvgNLSGGNQQKVVLAKWLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 572 DSPF-GyLDVLTEKEIFescvcKLMANKTR-----ILVTSKM-EHLKKADKILILHEG 622
Cdd:COG1129 419 DEPTrG-IDVGAKAEIY-----RLIRELAAegkavIVISSELpELLGLSDRILVMREG 470
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
437-628 |
3.65e-12 |
|
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: 66.81 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSegkikhsgrisfcsqfswIMPGTIKENiifGVSYDEYR 516
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGL------------------GVSGEVLIN---GRPLDKRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 517 YRSvikacqleedISKFAEKDNIVLGEggIT-------------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03213 80 FRK----------IIGYVPQDDILHPT--LTvretlmfaaklrgLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 584 KEIFEScvckLMA----NKTRILVT----SKMEHLkkADKILILHEGSSYFYG 628
Cdd:cd03213 148 LQVMSL----LRRladtGRTIICSIhqpsSEIFEL--FDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1212-1421 |
4.02e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.50 E-value: 4.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSITLQQWRKAF 1286
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTL----AKLLNglllpEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVI---PQKVFIfsGT---------FRKNLDPYEQWSDQEIWKVaDEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLM 1354
Cdd:PRK13635 84 GMVfqnPDNQFV--GAtvqddvafgLENIGVPREEMVERVDQAL-RQVGMEDFLNREPHR-----------LSGGQKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 1355 CLARSVLSKAKILLLDEPSAHLDPVTYQ----IIRRTLKQafADCTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRRevleTVRQLKEQ--KGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1212-1380 |
4.58e-12 |
|
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: 67.46 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNA--ILENISFSISPGQRVGLLGRTGSGKSTLLS--AFLrLLNTEGEIQIDGVSWDSIT---LQQWRk 1284
Cdd:COG4181 11 LRGLTKTVGTGAGEltILKGISLEVEAGESVAIVGASGSGKSTLLGllAGL-DRPTSGTVRLAGQDLFALDedaRARLR- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 afgviPQKV-FIF-------SGTFRKN-LDPYEQWSDQEIWKVA----DEVGLRSVIEQFPGkldfvlvdggcVLSHGHK 1351
Cdd:COG4181 89 -----ARHVgFVFqsfqllpTLTALENvMLPLELAGRRDARARArallERVGLGHRLDHYPA-----------QLSGGEQ 152
|
170 180
....*....|....*....|....*....
gi 90421313 1352 QLMCLARSVLSKAKILLLDEPSAHLDPVT 1380
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAAT 181
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
440-622 |
5.30e-12 |
|
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: 66.78 E-value: 5.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG---------------RISFCSQ-FSWIMPGTIK 503
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkltddkkninelrqKVGMVFQqFNLFPHLTVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIF------GVSYDEY--RYRSVIKACQLEEDISKFAekdnivlgeggITLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:cd03262 95 ENITLapikvkGMSKAEAeeRALELLEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90421313 576 GYLDVLTEKEIFEscVCKLMA--NKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03262 164 SALDPELVGEVLD--VMKDLAeeGMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
437-635 |
5.31e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.22 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWI---------------MPGT 501
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKENIIFG-----VSYDEY--RYRSVIKACQLEEdiskFAEKdnivlgeGGITLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK13647 97 VWDDVAFGpvnmgLDKDEVerRVEEALKAVRMWD----FRDK-------PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 575 FGYLDVLTEKEIFESCVCKLMANKTRILVTSKME-HLKKADKILILHEGSSYFYGTFSELQN 635
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1222-1420 |
8.52e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.91 E-value: 8.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSWDSiTLQQWRKAFGVIPQkvfiFSgtf 1300
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCGEPVPS-RARHARQRVGVVPQ----FD--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1301 rkNLDPyeQWSDQEIWKV-ADEVGLRS--VIEQFPGKLDFVLVDGGC-----VLSHGHKQLMCLARSVLSKAKILLLDEP 1372
Cdd:PRK13537 90 --NLDP--DFTVRENLLVfGRYFGLSAaaARALVPPLLEFAKLENKAdakvgELSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90421313 1373 SAHLDPVTYQIIRRTLKQAFADC-TVILCEHRI-EAMLECQQFLVIEENK 1420
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSLLARGkTILLTTHFMeEAERLCDRLCVIEEGR 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
438-622 |
9.37e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR---------------ISFC---SQFSWImp 499
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGItiskenlkeirkkigIIFQnpdNQFIGA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 gTIKENIIFGVS---YDEYRYRSVIKACQLEEDISKFAEKDNivlgeggITLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK13632 100 -TVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDYLDKEP-------QNLSGGQKQRVAIASVLALNPEIIIFDESTS 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 577 YLDVLTEKEIFescvcKLM------ANKTRILVTSKMEHLKKADKILILHEG 622
Cdd:PRK13632 172 MLDPKGKREIK-----KIMvdlrktRKKTLISITHDMDEAILADKVIVFSEG 218
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1211-1430 |
9.49e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.83 E-value: 9.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGvswDSITLQQwRKAFGVI 1289
Cdd:COG4152 3 ELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILApDSGEVLWDG---EPLDPED-RRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 P--------QKVF---IFSGTfRKNLDPYEqwSDQEIWKVADEVGLRSV----IEQfpgkldfvlvdggcvLSHGHKQLM 1354
Cdd:COG4152 77 PeerglypkMKVGeqlVYLAR-LKGLSKAE--AKRRADEWLERLGLGDRankkVEE---------------LSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1355 CLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK-QAFADCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQKL 1430
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIReLAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEI 216
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
437-635 |
9.79e-12 |
|
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: 66.54 E-value: 9.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR--------------ISFCSQFSWIMPG-T 501
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEditglpphriarlgIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKENIIFGvsydeyRYRSVIKAcQLEEDIskfaekDNI-----VLGE-----GGiTLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG0410 95 VEENLLLG------AYARRDRA-EVRADL------ERVyelfpRLKErrrqrAG-TLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 572 DSPfgyldvlTE-------KEIFEsCVCKLMANKTRILVTskmEH-----LKKADKILILHEGSSYFYGTFSELQN 635
Cdd:COG0410 161 DEP-------SLglaplivEEIFE-IIRRLNREGVTILLV---EQnarfaLEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1219-1377 |
1.09e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1219 YTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFS 1297
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISpTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1298 GTFRKNLD-PYEQWSDQeiwkvADEVGLRSVIEQFpGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 1376
Cdd:PRK10247 95 DTVYDNLIfPWQIRNQQ-----PDPAIFLDDLERF-ALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
.
gi 90421313 1377 D 1377
Cdd:PRK10247 169 D 169
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
437-586 |
1.12e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 1.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR----------ISFCSQ---FSWIMPGTIK 503
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlVAYVPQseeVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFG-------VSYDEYRYRSVIKACQLEEDISKFAEKDnivLGEggitLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170
....*....|
gi 90421313 577 YLDVLTEKEI 586
Cdd:PRK15056 172 GVDVKTEARI 181
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
440-635 |
1.26e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.44 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI---------KHSGRISFcsqfswiMP---G-----TI 502
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVlwdgepldpEDRRRIGY-------LPeerGlypkmKV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 503 KENIIF-----GVSydeyryRSVIKAcQLEEDISKF--AEKDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:COG4152 89 GEQLVYlarlkGLS------KAEAKR-RADEWLERLglGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 576 GYLDV----LTEKEIFEscvckLMAN-KTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQN 635
Cdd:COG4152 158 SGLDPvnveLLKDVIRE-----LAAKgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1222-1450 |
1.37e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 66.27 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSW--DSITLQQWRKAFGVIPQKVF 1294
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTL----LRCINkleeiTSGDLIVDGLKVndPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1295 IFSG-TFRKNL--DPYE--QWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAK 1365
Cdd:PRK09493 88 LFPHlTALENVmfGPLRvrGASKEEAEKQAREllakVGLAERAHHYPSE-----------LSGGQQQRVAIARALAVKPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1366 ILLLDEPSAHLDPVTYQIIRRTLKQ-AFADCTVILCEHRIE-AMLECQQFLVIEENKVRQYDSIQKLLNErslfrqaiSP 1443
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIKN--------PP 228
|
....*..
gi 90421313 1444 SDRVKLF 1450
Cdd:PRK09493 229 SQRLQEF 235
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1210-1440 |
1.52e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 66.75 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL----NTEGEIQIDGVSWDSITLQQWRKA 1285
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddNPNSKITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQkvfifsgtfrknlDPYEQWSDQeiwKVADEV--GL--------------RSVIEQFpGKLDFVLVDGGcVLSHG 1349
Cdd:PRK13640 86 VGIVFQ-------------NPDNQFVGA---TVGDDVafGLenravprpemikivRDVLADV-GMLDYIDSEPA-NLSGG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1350 HKQLMCLARSVLSKAKILLLDEPSAHLDPV----TYQIIRRTLKQafADCTVILCEHRIEAMLECQQFLVIEENKVRQYD 1425
Cdd:PRK13640 148 QKQRVAIAGILAVEPKIIILDESTSMLDPAgkeqILKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225
|
250
....*....|....*
gi 90421313 1426 SIQKLLNERSLFRQA 1440
Cdd:PRK13640 226 SPVEIFSKVEMLKEI 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1210-1438 |
1.55e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.07 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTegGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGvswDSITL----QQWRK 1284
Cdd:PRK10895 4 LTAKNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVpRDAGNIIIDD---EDISLlplhARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQKVFIFSG-----------TFRKNLDPyEQWSDQeiwkvADEVGLRSVIEQFPGKLdfvlvdgGCVLSHGHKQL 1353
Cdd:PRK10895 79 GIGYLPQEASIFRRlsvydnlmavlQIRDDLSA-EQREDR-----ANELMEEFHIEHLRDSM-------GQSLSGGERRR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1354 MCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAF-ADCTVILCEHRIEAMLE-CQQFLVIEENKVRQYDSIQKLL 1431
Cdd:PRK10895 146 VEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEIL 225
|
....*..
gi 90421313 1432 NERSLFR 1438
Cdd:PRK10895 226 QDEHVKR 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
441-608 |
1.64e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 66.34 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVI--MGELEPS---EGKIKHSG---------------RISFCSQFSWIMPG 500
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGknlyapdvdpvevrrRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENIIFGV-------SYDEYRYRSVIKACQLEEdiskfaEKDNivLGEGGITLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK14243 106 SIYDNIAYGAringykgDMDELVERSLRQAALWDE------VKDK--LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*
gi 90421313 574 PFGYLDVLTEKEIfESCVCKLMANKTRILVTSKME 608
Cdd:PRK14243 178 PCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQ 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1212-1426 |
1.68e-11 |
|
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: 65.82 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSITLQQwrKAF 1286
Cdd:cd03296 5 VRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTL----LRLIAglerpDSGTILFGGEDATDVPVQE--RNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSG-TFRKNL-------DPYEQWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLM 1354
Cdd:cd03296 77 GFVFQHYALFRHmTVFDNVafglrvkPRSERPPEAEIRAKVHEllklVQLDWLADRYPAQ-----------LSGGQRQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1355 CLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADC--TVILCEHRIEAMLE-CQQFLVIEENKVRQYDS 1426
Cdd:cd03296 146 ALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGT 220
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
437-580 |
1.81e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.90 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-ISFCSQFSWI--------MPG--TIKEN 505
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdIDDPDVAEAChylghrnaMKPalTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFGVSY---DEYRYRSVIKACQLE--EDIsKFAEkdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK13539 94 LEFWAAFlggEELDIAAALEAVGLAplAHL-PFGY------------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
430-637 |
1.86e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 69.29 E-value: 1.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 430 FSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIM------------------GEL---------------- 475
Cdd:PTZ00265 1173 FRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtNDMtneqdyqgdeeqnvgm 1252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 476 ----------EPSEGK----IKHSGRI-------------------SFCSQFSWIMPGTIKENIIFGvsYDEYRYRSVIK 522
Cdd:PTZ00265 1253 knvnefsltkEGGSGEdstvFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIYENIKFG--KEDATREDVKR 1330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 523 ACQ---LEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCV-CKLMANK 598
Cdd:PTZ00265 1331 ACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdIKDKADK 1410
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 90421313 599 TRILVTSKMEHLKKADKILILH--EGSSYF---YGTFSELQNLQ 637
Cdd:PTZ00265 1411 TIITIAHRIASIKRSDKIVVFNnpDRTGSFvqaHGTHEELLSVQ 1454
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
437-633 |
1.97e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 66.73 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTP----VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-----------------RISFCSQF- 494
Cdd:PRK13646 15 GTPyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 495 -SWIMPGTIKENIIFG-----VSYDEYRYRsvikACQLEEDISkfAEKDniVLGEGGITLSGGQRARISLARAVYKDADL 568
Cdd:PRK13646 95 eSQLFEDTVEREIIFGpknfkMNLDEVKNY----AHRLLMDLG--FSRD--VMSQSPFQMSGGQMRKIAIVSILAMNPDI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 569 YLLDSPFGYLDVLTEKEIFESC-VCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13646 167 IVLDEPTAGLDPQSKRQVMRLLkSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
434-580 |
2.03e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.94 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 434 SLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR----------------------ISFc 491
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaraasrrvasvpqdtsLSF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 492 sQFS---WIMPGTIKENIIFGvSYDEYRYRSVIKACQlEEDISKFAEKDnivlgeggIT-LSGGQRARISLARAVYKDAD 567
Cdd:PRK09536 91 -EFDvrqVVEMGRTPHRSRFD-TWTETDRAAVERAME-RTGVAQFADRP--------VTsLSGGERQRVLLARALAQATP 159
|
170
....*....|...
gi 90421313 568 LYLLDSPFGYLDV 580
Cdd:PRK09536 160 VLLLDEPTASLDI 172
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1202-1404 |
2.04e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.27 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1202 DIWPSGGQMTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT------EGEIQIDGVS-W 1274
Cdd:PRK14271 14 DVDAAAPAMAAVNLTLGF--AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrySGDVLLGGRSiF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1275 DSITLQQWRKAFGVIPQKVFIFSGTFRKNL----DPYEQWSDQEIWKVAD----EVGLRSVIEQfpgkldfVLVDGGCVL 1346
Cdd:PRK14271 92 NYRDVLEFRRRVGMLFQRPNPFPMSIMDNVlagvRAHKLVPRKEFRGVAQarltEVGLWDAVKD-------RLSDSPFRL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRI 1404
Cdd:PRK14271 165 SGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1223-1449 |
2.18e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.16 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1223 GNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRllNTEGEIQIDGV-SWDSITLQQWRKAFGVI---PQKVFI 1295
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLR--PQKGKVLVSGIdTGDFSKLQGIRKLVGIVfqnPETQFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1296 fSGTFRKNLDPYEQ---WSDQEIWKVAD----EVGLRSVIEQFPGkldfvlvdggcVLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:PRK13644 92 -GRTVEEDLAFGPEnlcLPPIEIRKRVDralaEIGLEKYRHRSPK-----------TLSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1369 LDEPSAHLDPVTYQIIRRTLKQAFADC-TVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRV 1447
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKLHEKGkTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGLTPPSLI 239
|
..
gi 90421313 1448 KL 1449
Cdd:PRK13644 240 EL 241
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
411-588 |
4.19e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 4.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 411 KAKQNNNNRKTSNGDDSLFFSNFSLL---GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGeLEPS-EGKIKH-- 484
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTLRtpdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSGRIARpa 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 485 SGRISFCSQFSWIMPGTIKENIIF---GVSYDEYRYRSVIKACQLEEDISKFAEKDNIvlgegGITLSGGQRARISLARA 561
Cdd:COG4178 425 GARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGEQQRLAFARL 499
|
170 180
....*....|....*....|....*..
gi 90421313 562 VYKDADLYLLDSPFGYLDVLTEKEIFE 588
Cdd:COG4178 500 LLHKPDWLFLDEATSALDEENEAALYQ 526
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1226-1274 |
4.20e-11 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 64.72 E-value: 4.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1226 ILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDG-VSW 1274
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTL----LKLIAgilepTSGRVEVNGrVSA 91
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1227-1402 |
4.79e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 64.86 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGV---SWDSITLQQWRkafGVIPQ--------KVFI 1295
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRplsDWSAAELARHR---AYLSQqqsppfamPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1296 FSGTFR-KNLDPYEQwsDQEIWKVADEVGL-----RSViEQfpgkldfvlvdggcvLSHGHKQLMCLARSVL-------S 1362
Cdd:COG4138 89 YLALHQpAGASSEAV--EQLLAQLAEALGLedklsRPL-TQ---------------LSGGEWQRVRLAAVLLqvwptinP 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 90421313 1363 KAKILLLDEPSAHLDpVTYQIIRRTLKQAFADC--TVILCEH 1402
Cdd:COG4138 151 EGQLLLLDEPMNSLD-VAQQAALDRLLRELCQQgiTVVMSSH 191
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
863-1114 |
4.82e-11 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 65.26 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 863 LIWCLVIFLAEVAASLVVLWLLGntplqdkgnsthsrnnsYAV--IITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHT 940
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTK-----------------LLIddVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 941 LITVSKILHH---KMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFV 1017
Cdd:cd07346 64 ARLGQRVVFDlrrDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1018 ATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLR 1097
Cdd:cd07346 144 VALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA 223
|
250
....*....|....*..
gi 90421313 1098 WFQMRIEMIFVIFFIAV 1114
Cdd:cd07346 224 LFSPLIGLLTALGTALV 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
433-635 |
4.96e-11 |
|
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: 68.12 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR------------ISFCSQFSWIMPG 500
Cdd:TIGR01257 938 FEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnldavrqsLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENIIFgvsYDEYRYRSVIKAcQLE-----EDiSKFAEKDNivlgEGGITLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:TIGR01257 1018 lTVAEHILF---YAQLKGRSWEEA-QLEmeamlED-TGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 575 FGYLDVLTEKEIFEsCVCKLMANKTRILVTSKMEHLK-KADKILILHEGSSYFYGTFSELQN 635
Cdd:TIGR01257 1089 TSGVDPYSRRSIWD-LLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFLKN 1149
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
438-637 |
5.12e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.11 E-value: 5.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGK----------------IKHSGRISFCSQFSWIMPGT 501
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKvyvdgldtsdeenlwdIRNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKENIIF-----GVSYDEYRYR--SVIKACQLEEdISKFAEKdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK13633 103 VEEDVAFgpenlGIPPEEIRERvdESLKKVGMYE-YRRHAPH----------LLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 575 FGYLDVLTEKEIFeSCVCKLmaNK----TRILVTSKMEHLKKADKILILHEGSSYFYGT----FSELQNLQ 637
Cdd:PRK13633 172 TAMLDPSGRREVV-NTIKEL--NKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTpkeiFKEVEMMK 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1210-1419 |
5.38e-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: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLL----NTEGEI------------------ 1267
Cdd:TIGR03269 1 IEVKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMdqyePTSGRIiyhvalcekcgyverpsk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1268 ---------------QIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFR------KNLDPYEQWSDQEIWKVADevglrs 1326
Cdd:TIGR03269 78 vgepcpvcggtlepeEVDFWNLSDKLRRRIRKRIAIMLQRTFALYGDDTvldnvlEALEEIGYEGKEAVGRAVD------ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1327 VIEQFpgKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAF--ADCTVILCEHRI 1404
Cdd:TIGR03269 152 LIEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWP 229
|
250
....*....|....*
gi 90421313 1405 EAMLECQQFLVIEEN 1419
Cdd:TIGR03269 230 EVIEDLSDKAIWLEN 244
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1231-1419 |
5.99e-11 |
|
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: 63.67 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1231 SFSISPGQRVGLLGRTGSGKSTLL---SAFLrlLNTEGEIQIDGVswDSITLQQWRKAFGVIPQKVFIFSG-TFRKN--- 1303
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLnliAGFE--TPQSGRVLINGV--DVTAAPPADRPVSMLFQENNLFAHlTVEQNvgl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1304 -------LDPYEQwsdQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 1376
Cdd:cd03298 94 glspglkLTAEDR---QAIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 90421313 1377 DPvtyqIIRRTLKQAFADC------TVILCEHRIEAMLECQQFLVIEEN 1419
Cdd:cd03298 160 DP----ALRAEMLDLVLDLhaetkmTVLMVTHQPEDAKRLAQRVVFLDN 204
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
424-647 |
7.70e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 7.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 424 GDDSLFFSNFSLLGtpvLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRIsfcsqfswIMPGTIK 503
Cdd:PRK10762 254 GEVRLKVDNLSGPG---VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE--------VVTRSPQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFGVSY-DEYRYR-------SVI-------------KACQLEEDISKFAEKDNIVL-------GEGGI-TLSGGQRA 554
Cdd:PRK10762 323 DGLANGIVYiSEDRKRdglvlgmSVKenmsltalryfsrAGGSLKHADEQQAVSDFIRLfniktpsMEQAIgLLSGGNQQ 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 555 RISLARAVYKDADLYLLDSPFGYLDVLTEKEIFEscvcklMANKTR------ILVTSKM-EHLKKADKILILHEGSsyFY 627
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQ------LINQFKaeglsiILVSSEMpEVLGMSDRILVMHEGR--IS 474
|
250 260
....*....|....*....|
gi 90421313 628 GTFSELQNLQpdfsSKLMGC 647
Cdd:PRK10762 475 GEFTREQATQ----EKLMAA 490
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1222-1384 |
9.16e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 63.88 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGEIQIDGVSWD------SITLQQWRKAFGVIP 1290
Cdd:PRK11124 13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLL----RVLNllempRSGTLNIAGNHFDfsktpsDKAIRELRRNVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSG-TFRKNL--DPYE--QWSDQEIWKVADEVGLRSVIEQFPGKldFVLVdggcvLSHGHKQLMCLARSVLSKAK 1365
Cdd:PRK11124 89 QQYNLWPHlTVQQNLieAPCRvlGLSKDQALARAEKLLERLRLKPYADR--FPLH-----LSGGQQQRVAIARALMMEPQ 161
|
170 180
....*....|....*....|
gi 90421313 1366 ILLLDEPSAHLDP-VTYQII 1384
Cdd:PRK11124 162 VLLFDEPTAALDPeITAQIV 181
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1222-1390 |
9.43e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 63.88 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGEIQIDGVSWD------SITLQQWRKAFGVIP 1290
Cdd:COG4161 13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLL----RVLNlletpDSGQLNIAGHQFDfsqkpsEKAIRLLRQKVGMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QKVFIFSG-TFRKNLDPYEQW----SDQEIWKVADEVGLRSVIEQFPGKldFVLVdggcvLSHGHKQLMCLARSVLSKAK 1365
Cdd:COG4161 89 QQYNLWPHlTVMENLIEAPCKvlglSKEQAREKAMKLLARLRLTDKADR--FPLH-----LSGGQQQRVAIARALMMEPQ 161
|
170 180
....*....|....*....|....*...
gi 90421313 1366 ILLLDEPSAHLDP-VTYQI--IRRTLKQ 1390
Cdd:COG4161 162 VLLFDEPTAALDPeITAQVveIIRELSQ 189
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
441-622 |
1.13e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG--------------KIKHSGR----ISFCSQFS--WIMPG 500
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyaipanlkKIKEVKRlrkeIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENIIFGVSY----DEYRYRSV---IKACQLEEDISKfaekdnivlgEGGITLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK13645 107 TIEKDIAFGPVNlgenKQEAYKKVpelLKLVQLPEDYVK----------RSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 574 PFGYLDVLTEKEiFESCVCKLMANKTR--ILVTSKMEH-LKKADKILILHEG 622
Cdd:PRK13645 177 PTGGLDPKGEED-FINLFERLNKEYKKriIMVTHNMDQvLRIADEVIVMHEG 227
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
441-656 |
1.13e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 65.44 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-----------------RISFCSQFSWIMPG-TI 502
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 503 KENIIFG-----VSYDEYRYRSV--IKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:PRK10070 124 LDNTAFGmelagINAEERREKALdaLRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 576 GYLDVLTEKEIFESCVcKLMANKTRILVTSKM---EHLKKADKILILHEGSSYFYGTFSE-LQNLQPDFSSKLM-GCDSF 650
Cdd:PRK10070 193 SALDPLIRTEMQDELV-KLQAKHQRTIVFISHdldEAMRIGDRIAIMQNGEVVQVGTPDEiLNNPANDYVRTFFrGVDIS 271
|
....*.
gi 90421313 651 DQFSAE 656
Cdd:PRK10070 272 QVFSAK 277
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
437-622 |
1.28e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 64.97 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQFSWIMPG-TIKE 504
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrhVNTVFQSYALFPHmTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFG-----VSYDEYRYR--SVIKACQLEEdiskFAEKDNIvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK09452 106 NVAFGlrmqkTPAAEITPRvmEALRMVQLEE----FAQRKPH-------QLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 578 LDVLTEKEifescvcklMANK----------TRILVTSKMEH-LKKADKILILHEG 622
Cdd:PRK09452 175 LDYKLRKQ---------MQNElkalqrklgiTFVFVTHDQEEaLTMSDRIVVMRDG 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
444-579 |
1.38e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 62.85 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 444 INFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQ----FSWImpgTIKENIIF 508
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQdltalppaerpVSMLFQennlFPHL---TVAQNIGL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 509 GVSYDeYRYRSVIKAcQLEEDISKfaekdnivLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:COG3840 95 GLRPG-LKLTAEQRA-QVEQALER--------VGLAGLldrlpgQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1227-1430 |
1.66e-10 |
|
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: 63.95 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGvsWDsITLQ--QWRKAFGVIPQKVFIFSG-TFRK 1302
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAG--YD-VVREprKVRRSIGIVPQYASVDEDlTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1303 NL----DPYEqWSDQEIWKVADEVglrsvIEQFPgkldfvLVDGGCVL----SHGHKQLMCLARSVLSKAKILLLDEPSA 1374
Cdd:TIGR01188 86 NLemmgRLYG-LPKDEAEERAEEL-----LELFE------LGEAADRPvgtySGGMRRRLDIAASLIHQPDVLFLDEPTT 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1375 HLDPVTYQIIR---RTLKQafADCTVILCEHRI-EAMLECQQFLVIEENKVRQYDSIQKL 1430
Cdd:TIGR01188 154 GLDPRTRRAIWdyiRALKE--EGVTILLTTHYMeEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
437-633 |
1.86e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 63.56 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------------ISFCSQFSWIMP 499
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrktvgIVFQNPDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIFG-----VSYDEY--RYRSVIKACQLEedisKFAEKDNivlgeggITLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK13639 94 PTVEEDVAFGplnlgLSKEEVekRVKEALKAVGME----GFENKPP-------HHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 573 SPFGYLDVLTEKEIFescvcKLMA--NK---TRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13639 163 EPTSGLDPMGASQIM-----KLLYdlNKegiTIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEV 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1212-1423 |
2.15e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.13 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEggNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDG--------VSWDSITLQQWR 1283
Cdd:PRK14258 10 VNNLSFYYDT--QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqnIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1284 KAFGVIPQKVFIFSGTFRKNL----------------DPYEQ-WSDQEIWkvaDEVglrsvieqfPGKLDFVLVDggcvL 1346
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVaygvkivgwrpkleidDIVESaLKDADLW---DEI---------KHKIHKSALD----L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAF--ADCTVILCEHRIEAMLECQQFLVI---EENKV 1421
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFfkgNENRI 231
|
..
gi 90421313 1422 RQ 1423
Cdd:PRK14258 232 GQ 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
440-580 |
2.32e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 61.74 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK------HSGRISFCSQFSWI--MPG-----TIKENI 506
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggplDFQRDSIARGLLYLghAPGikttlSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 IFgvsydeyrYRSVIKACQLEEDISKfaekdnivLGEGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03231 95 RF--------WHADHSDEQVEEALAR--------VGLNGFedrpvaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
440-580 |
2.37e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--RISFCSQ--------------FSWIMPGTIK 503
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQklyldttlpltvnrFLRLRPGTKK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 504 ENIIfgvsydeyryrSVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK09544 99 EDIL-----------PALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1212-1390 |
2.61e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 62.79 E-value: 2.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDG--VSWDSITLQQWRKAFGV 1288
Cdd:PRK13639 4 TRDLKYSYPDGTEA-LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGepIKYDKKSLLEVRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKV--FIFSGTFRK-------NLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARS 1359
Cdd:PRK13639 83 VFQNPddQLFAPTVEEdvafgplNLGLSKEEVEKRVKEALKAVGMEGFENKPPHH-----------LSGGQKKRVAIAGI 151
|
170 180 190
....*....|....*....|....*....|.
gi 90421313 1360 VLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ 1390
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYD 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1211-1377 |
2.70e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAkyTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWD------SIT----- 1278
Cdd:PRK13539 4 EGEDLAC--VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPpAAGTIKLDGGDIDdpdvaeACHylghr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1279 ------------LQQWRKAFGvipqkvfifsgtfRKNLDPYEqwsdqeiwkVADEVGLrSVIEQFPGKldfvlvdggcVL 1346
Cdd:PRK13539 82 namkpaltvaenLEFWAAFLG-------------GEELDIAA---------ALEAVGL-APLAHLPFG----------YL 128
|
170 180 190
....*....|....*....|....*....|.
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:PRK13539 129 SAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
433-560 |
2.81e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.04 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMP 499
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFG 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 500 GTIKENIIFgvsydEYRYRSviKACQ---LEEDISKFAEKDNIVlgEGGIT-LSGGQRARISLAR 560
Cdd:PRK10247 95 DTVYDNLIF-----PWQIRN--QQPDpaiFLDDLERFALPDTIL--TKNIAeLSGGEKQRISLIR 150
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
443-622 |
3.53e-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: 61.35 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 443 DINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQFSWIMPG-TIKENIIFGV 510
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 511 S-------YDEYRYRSVIKACQLEEDISKFAEkdnivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03298 96 SpglkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 90421313 584 KEIFEsCVCKLMANK--TRILVTSKMEHLKK-ADKILILHEG 622
Cdd:cd03298 165 AEMLD-LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1222-1390 |
3.53e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.56 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDG--VS------------------------W 1274
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHqTSGHIRFHGtdVSrlhardrkvgfvfqhyalfrhmtvF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1275 DSItlqqwrkAFG--VIPQkvfifsgtfRKNLDPYEqwSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQ 1352
Cdd:PRK10851 93 DNI-------AFGltVLPR---------RERPNAAA--IKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQ 143
|
170 180 190
....*....|....*....|....*....|....*...
gi 90421313 1353 LMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ 1390
Cdd:PRK10851 144 RVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQ 181
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1211-1407 |
3.86e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 63.17 E-value: 3.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGvswdsitlqqwRKA 1285
Cdd:COG3839 5 ELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIAgledpTSGEILIGG-----------RDV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQK-----VF----IF-SGTFRKNL---------DPYEQwsDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvL 1346
Cdd:COG3839 68 TDLPPKDrniamVFqsyaLYpHMTVYENIafplklrkvPKAEI--DRRVREAAELLGLEDLLDRKPKQ-----------L 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVILCEH-RIEAM 1407
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlgTTTIYVTHdQVEAM 198
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
441-637 |
4.06e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.46 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI----------------KHSGrISFCSQFSWIMPGTIKE 504
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklrKHIG-IVFQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFG-----VSYDEYrYRSVIKACqleEDISKFAEKDNivlgeGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13648 104 DVAFGlenhaVPYDEM-HRRVSEAL---KQVDMLERADY-----EPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 580 VLTEKEIFeSCVCKLMANK--TRILVTSKMEHLKKADKILILHEGSSYFYGT----FSELQNLQ 637
Cdd:PRK13648 175 PDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTpteiFDHAEELT 237
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
430-625 |
4.20e-10 |
|
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: 60.25 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 430 FSNFSLL---GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVImGELEPS-EGKIKH--SGRISFCSQFSWIMPGTIK 503
Cdd:cd03223 3 LENLSLAtpdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRAL-AGLWPWgSGRIGMpeGEDLLFLPQRPYLPLGTLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIfgvsydeYRYRSVikacqleediskfaekdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03223 82 EQLI-------YPWDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90421313 584 KEIFESCVCKLMAnktrILVTSKMEHLKK-ADKILILHEGSSY 625
Cdd:cd03223 128 DRLYQLLKELGIT----VISVGHRPSLWKfHDRVLDLDGEGGW 166
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1224-1438 |
4.37e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.95 E-value: 4.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1224 NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN----TEGEIQIDGVSWD-----SITLQQWRKAFGVIPQK-- 1292
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRTVQregrlARDIRKSRANTGYIFQQfn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1293 ----------VFIFS-GT---FRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGkldfvlvdggcVLSHGHKQLMCLAR 1358
Cdd:PRK09984 97 lvnrlsvlenVLIGAlGStpfWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVS-----------TLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVILCEHRIE-AMLECQQFLVIEENKVRQYDSIQKLLNER- 1434
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERf 245
|
....*
gi 90421313 1435 -SLFR 1438
Cdd:PRK09984 246 dHLYR 250
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1229-1386 |
4.66e-10 |
|
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: 62.28 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1229 NISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSIT---LQQWRK--------AFGVIPQKVFIF 1296
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSrkeLRELRRkkismvfqSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1297 SGTFR---KNLDPYEQWSDQEiwKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 1373
Cdd:cd03294 122 NVAFGlevQGVPRAEREERAA--EALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188
|
170
....*....|...
gi 90421313 1374 AHLDPvtyqIIRR 1386
Cdd:cd03294 189 SALDP----LIRR 197
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1213-1440 |
5.50e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 62.13 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYTeGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQ 1291
Cdd:PRK13652 7 RDLCYSYS-GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1292 KV--FIFSGTFRK-------NLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLS 1362
Cdd:PRK13652 86 NPddQIFSPTVEQdiafgpiNLGLDEETVAHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1363 KAKILLLDEPSAHLDPV-TYQIIR--RTLKQAFAdCTVILCEHRIEAMLECQQFL-VIEENKVRQYDSIQKLLNERSLFR 1438
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQgVKELIDflNDLPETYG-MTVIFSTHQLDLVPEMADYIyVMDKGRIVAYGTVEEIFLQPDLLA 233
|
..
gi 90421313 1439 QA 1440
Cdd:PRK13652 234 RV 235
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1225-1402 |
6.43e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.60 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1225 AILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEIQIDG---------VSWDSITLqqwRKAFGVIPQKVF 1294
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGkvlyfgkdiFQIDAIKL---RKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1295 IFS-----GTFRKNLDPYEQWSDQEIWKVADE----VGL-RSVIEQfpgkldfvLVDGGCVLSHGHKQLMCLARSVLSKA 1364
Cdd:PRK14246 101 PFPhlsiyDNIAYPLKSHGIKEKREIKKIVEEclrkVGLwKEVYDR--------LNSPASQLSGGQQQRLTIARALALKP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 90421313 1365 KILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEH 1402
Cdd:PRK14246 173 KVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
440-622 |
6.48e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 61.52 E-value: 6.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG--------------------------RISFCSQ 493
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlkvadknqlrllrtRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 494 -FSWIMPGTIKENI------IFGVSYDEYRYRSVikacqleedisKFAEK---DNIVLGEGGITLSGGQRARISLARAVY 563
Cdd:PRK10619 100 hFNLWSHMTVLENVmeapiqVLGLSKQEARERAV-----------KYLAKvgiDERAQGKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 564 KDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHvSSHVIFLHQG 228
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1223-1377 |
7.00e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 60.81 E-value: 7.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1223 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEIQIDGVSWDSITLQQW----RKAFGVIPQKVFIFS 1297
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTlEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1298 GTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1222-1402 |
7.60e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEiqidgVSWDSITLQQWRKAF---------- 1286
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSL----LRILAglarpDAGE-----VLWQGEPIRRQRDEYhqdllylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 -GVIPQkvfifsgtfrknLDPYE--QW--------SDQEIWKVADEVGLRSViEQFPGKldfvlvdggcVLSHGHKQLMC 1355
Cdd:PRK13538 83 pGIKTE------------LTALEnlRFyqrlhgpgDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90421313 1356 LARSVLSKAKILLLDEPSAHLDpvtyqiirrtlKQAFADCTVILCEH 1402
Cdd:PRK13538 140 LARLWLTRAPLWILDEPFTAID-----------KQGVARLEALLAQH 175
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
432-636 |
8.89e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 8.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVI--MGELEpseGKIKHSGRISFCSQFSW------------- 496
Cdd:PRK14258 14 SFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELE---SEVRVEGRVEFFNQNIYerrvnlnrlrrqv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 497 --------IMPGTIKENIIFGVSYDEYRYR--------SVIKACQLEEDISKFAEKDnivlgegGITLSGGQRARISLAR 560
Cdd:PRK14258 91 smvhpkpnLFPMSVYDNVAYGVKIVGWRPKleiddiveSALKDADLWDEIKHKIHKS-------ALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 561 AVYKDADLYLLDSPFGYLDVLTEKEIfESCV--CKLMANKTRILVTSKMEHLKKadkiliLHEGSSYFYGTFSELQNL 636
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKV-ESLIqsLRLRSELTMVIVSHNLHQVSR------LSDFTAFFKGNENRIGQL 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
444-608 |
9.58e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 444 INFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIkhsgriSFCSQFSWI--------MPGTIKENI-IFGVSYDE 514
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV------NVRVGDEWVdmtkpgpdGRGRAKRYIgILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 515 YRYRSVIKacQLEEDIS-----KFAE-KDNIVLGEGGIT--------------LSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:TIGR03269 377 YPHRTVLD--NLTEAIGlelpdELARmKAVITLKMVGFDeekaeeildkypdeLSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190
....*....|....*....|....*....|....*
gi 90421313 575 FGYLDVLTEKEIFESCV-CKLMANKTRILVTSKME 608
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILkAREEMEQTFIIVSHDMD 489
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1213-1405 |
1.12e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.95 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL------LNTEGEIQIDGVS-WDS-ITLQQWRK 1284
Cdd:PRK14243 14 ENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndlipgFRVEGKVTFHGKNlYAPdVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQKVFIFSGTFRKNL------DPYEQWSDQEIwkvadEVGLRSVI--EQFPGKLDfvlvDGGCVLSHGHKQLMCL 1356
Cdd:PRK14243 92 RIGMVFQKPNPFPKSIYDNIaygariNGYKGDMDELV-----ERSLRQAAlwDEVKDKLK----QSGLSLSGGQQQRLCI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIE 1405
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
433-579 |
1.16e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------RISFCSQFSWiMPG----- 500
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktatrgdRSRFMAYLGH-LPGlkadl 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 501 TIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAekDNIVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13543 98 STLENLHFLCGLHGRRAKQMPGSALAIVGLAGYE--DTLVR-----QLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1210-1279 |
1.21e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 60.48 E-value: 1.21e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDG---VSWDSITL 1279
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPpDSGEVLVDGldvATTPSREL 73
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
441-608 |
1.38e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 60.56 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVI--MGELEPS---EGKIKHSGR---------------ISFCSQFSWIMPG 500
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtvdlrkeIGMVFQQPNPFPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENIIFGVS---------YDEYRYRSVIKACQLEEdiskfaEKDNivLGEGGITLSGGQRARISLARAVYKDADLYLL 571
Cdd:PRK14239 101 SIYENVVYGLRlkgikdkqvLDEAVEKSLKGASIWDE------VKDR--LHDSALGLSGGQQQRVCIARVLATSPKIILL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 90421313 572 DSPFGYLDVLTEKEIfESCVCKLMANKTRILVTSKME 608
Cdd:PRK14239 173 DEPTSALDPISAGKI-EETLLGLKDDYTMLLVTRSMQ 208
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
441-619 |
1.95e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-ISFCS-------------Q-FSWIMPGTIKEN 505
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpVRIRSprdaialgigmvhQhFMLVPNLTVAEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFGVsydEYRYRSVIKACQLEEDISKFAEK-------DNIVlgEggiTLSGGQRARISLARAVYKDADLYLLDSPFGyl 578
Cdd:COG3845 101 IVLGL---EPTKGGRLDRKAARARIRELSERygldvdpDAKV--E---DLSVGEQQRVEILKALYRGARILILDEPTA-- 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90421313 579 dVLTEKEI---FEscVCKLMAN--KTRILVTSKMEHLKK-ADKILIL 619
Cdd:COG3845 171 -VLTPQEAdelFE--ILRRLAAegKSIIFITHKLREVMAiADRVTVL 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
434-633 |
1.99e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.52 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 434 SLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-RISFCSQFSWIMPGTIKENIIFGVSY 512
Cdd:PRK13643 15 SPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKVGVVFQFPE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 513 DEYRYRSVIKACQL--------EEDISKFAEKDNIVLG-------EGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK13643 95 SQLFEETVLKDVAFgpqnfgipKEKAEKIAAEKLEMVGladefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 578 LDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13643 175 LDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
438-623 |
2.17e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.72 E-value: 2.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVI-------MGEL----------EPSEGKIKHSGRISFcSQFSWIMPG 500
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglkvndpKVDERLIRQEAGMVF-QQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENIIFGvsydEYRYRSVIKA---CQLEEDISK--FAEKDNIVLGEggitLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:PRK09493 93 TALENVMFG----PLRVRGASKEeaeKQARELLAKvgLAERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 576 GYLDVLTEKEIFEscVCKLMANK--TRILVTSKMEHLKKA-------DKILILHEGS 623
Cdd:PRK09493 165 SALDPELRHEVLK--VMQDLAEEgmTMVIVTHEIGFAEKVasrlifiDKGRIAEDGD 219
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1210-1409 |
2.26e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.02 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEggNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRllntegeIQIDGVSWDSITLQQWRKAF 1286
Cdd:PRK13638 2 LATSDLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLR-------PQKGAVLWQGKPLDYSKRGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKV-FIFSG----TFRKNLDPYEQWSDQEIWKVADEVGlRSVIEQFpgkldfVLVDGG--------CvLSHGHKQL 1353
Cdd:PRK13638 73 LALRQQVaTVFQDpeqqIFYTDIDSDIAFSLRNLGVPEAEIT-RRVDEAL------TLVDAQhfrhqpiqC-LSHGQKKR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1354 MCLARSVLSKAKILLLDEPSAHLDPV----TYQIIRRTLKQAfadCTVILCEHRIEAMLE 1409
Cdd:PRK13638 145 VAIAGALVLQARYLLLDEPTAGLDPAgrtqMIAIIRRIVAQG---NHVIISSHDIDLIYE 201
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1226-1384 |
2.28e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.81 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1226 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSwdsitLQQWRKAFgvipQKVFIFSGtFRKNL 1304
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQS-----IKKDLCTY----QKQLCFVG-HRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1305 DPYEQWSDQ---EIWKVADEVGLRSVIEQFpgKLDFvLVDGGC-VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVT 1380
Cdd:PRK13540 86 NPYLTLRENclyDIHFSPGAVGITELCRLF--SLEH-LIDYPCgLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
....
gi 90421313 1381 YQII 1384
Cdd:PRK13540 163 LLTI 166
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
440-629 |
2.36e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.63 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEG-------------------------KIKHSGR----ISF 490
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnhelitnpyskKIKNFKElrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 491 CSQFS--WIMPGTIKENIIFG-VSYDEYRYRSVIKAcqleediSKFAEK---DNIVLGEGGITLSGGQRARISLARAVYK 564
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGpVALGVKKSEAKKLA-------KFYLNKmglDDSYLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 565 DADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGT 629
Cdd:PRK13631 194 QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGT 259
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
438-603 |
2.40e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 59.64 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFCSQFSWIMPG-TIK 503
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENIIFGVS-----------YDEYRYRSVIKACQLEEdiskFAEKdniVLGEggitLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK11231 95 ELVAYGRSpwlslwgrlsaEDNARVNQAMEQTRINH----LADR---RLTD----LSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 90421313 573 SPFGYLDVLTEKEIFescvcKLM-----ANKTRILV 603
Cdd:PRK11231 164 EPTTYLDINHQVELM-----RLMrelntQGKTVVTV 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1222-1377 |
2.55e-09 |
|
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: 59.17 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVswDSITLQQWRKAFGVIPQKVFIF 1296
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAgfetpTSGEILLDGK--DITNLPPHKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1297 S----------GTFRKNLDPYEQwsDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKI 1366
Cdd:cd03300 85 PhltvfeniafGLRLKKLPKAEI--KERVAEALDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKV 151
|
170
....*....|.
gi 90421313 1367 LLLDEPSAHLD 1377
Cdd:cd03300 152 LLLDEPLGALD 162
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1213-1437 |
2.99e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.50 E-value: 2.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDG--VSWDSItlQQwrKAFGVI 1289
Cdd:PRK11432 10 KNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGedVTHRSI--QQ--RDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1290 PQKVFIFSgtfrkNLDPYEQ---------WSDQEIWKVADE----VGLRSVIEQFpgkldfvlVDGgcvLSHGHKQLMCL 1356
Cdd:PRK11432 84 FQSYALFP-----HMSLGENvgyglkmlgVPKEERKQRVKEalelVDLAGFEDRY--------VDQ---ISGGQQQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDPVTYQIIR---RTLKQAFaDCTVILCEH-RIEAMLECQQFLVIEENKVRQYDSIQKL-L 1431
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMRekiRELQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELyR 226
|
....*.
gi 90421313 1432 NERSLF 1437
Cdd:PRK11432 227 QPASRF 232
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
445-646 |
3.19e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 58.83 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 445 NFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQ----FSWImpgTIKENIIFG 509
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQennlFSHL---TVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 510 V-------SYDEYRYRSVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:PRK10771 96 LnpglklnAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 583 EKEIFE--SCVCKlMANKTRILVTSKMEH-LKKADKILILHEGSSYFYGTFSELQNLQPDfSSKLMG 646
Cdd:PRK10771 165 RQEMLTlvSQVCQ-ERQLTLLMVSHSLEDaARIAPRSLVVADGRIAWDGPTDELLSGKAS-ASALLG 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
440-646 |
3.60e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.50 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------ISFCSQFSWIMPG-TIKENI- 506
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrsiqqrdICMVFQSYALFPHmSLGENVg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 ----IFGVSYDEYRYRsVIKACQLeEDISKFAEK--DNIvlgeggitlSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK11432 101 yglkMLGVPKEERKQR-VKEALEL-VDLAGFEDRyvDQI---------SGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 581 LTEKEIFEscvcKLMANKTRILVTS------KMEHLKKADKILILHEGSSYFYGTFSELQnLQPD--FSSKLMG 646
Cdd:PRK11432 170 NLRRSMRE----KIRELQQQFNITSlyvthdQSEAFAVSDTVIVMNKGKIMQIGSPQELY-RQPAsrFMASFMG 238
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1210-1378 |
4.22e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.99 E-value: 4.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTegGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAfLRLLNTE-------GEIQIDGvswdSITLQQW 1282
Cdd:PRK11264 4 IEVKNLVKKFH--GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRC-INLLEQPeagtirvGDITIDT----ARSLSQQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1283 RKAFGVIPQKV-FIFSGTfrkNLDPY--------------EQWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdgg 1343
Cdd:PRK11264 77 KGLIRQLRQHVgFVFQNF---NLFPHrtvleniiegpvivKGEPKEEATARAREllakVGLAGKETSYPRR--------- 144
|
170 180 190
....*....|....*....|....*....|....*
gi 90421313 1344 cvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 1378
Cdd:PRK11264 145 --LSGGQQQRVAIARALAMRPEVILFDEPTSALDP 177
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1210-1423 |
5.10e-09 |
|
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: 58.04 E-value: 5.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGV---SWD------ 1275
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTT----LRMIAgleepTSGRIYIGGRdvtDLPpkdrdi 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1276 SITLQQwrkaFGVIPQK-VF--IFSGTFRKNLDPYEqwSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQ 1352
Cdd:cd03301 75 AMVFQN----YALYPHMtVYdnIAFGLKLRKVPKDE--IDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQ 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1353 LMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK--QAFADCTVILCEH-RIEAMLECQQFLVIEENKVRQ 1423
Cdd:cd03301 138 RVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQ 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
437-633 |
5.23e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 59.09 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-----------------ISFCSQFSWIMP 499
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpidysrkglmklresvgMVFQDPDNQLFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIFGVSydeyryrsvikACQLEEDisKFAEKDNIVLGEGGIT---------LSGGQRARISLARAVYKDADLYL 570
Cdd:PRK13636 98 ASVYQDVSFGAV-----------NLKLPED--EVRKRVDNALKRTGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVLV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 571 LDSPFGYLDVLTEKEIFEscVCKLMANK---TRILVTSKMEHLK-KADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMK--LLVEMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
440-644 |
6.49e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI----------KHSG----------------------- 486
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkKKTKekekvleklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 487 ----RISFCSQFS--WIMPGTIKENIIFG-VSYD------EYRYRSVIKACQLEEDI---SKFAekdnivlgeggitLSG 550
Cdd:PRK13651 102 eirrRVGVVFQFAeyQLFEQTIEKDIIFGpVSMGvskeeaKKRAAKYIELVGLDESYlqrSPFE-------------LSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 551 GQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEH-LKKADKILILHEGSSYFYG- 628
Cdd:PRK13651 169 GQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGd 248
|
250 260
....*....|....*....|....*...
gi 90421313 629 TFSELQ--------NLQP----DFSSKL 644
Cdd:PRK13651 249 TYDILSdnkflienNMEPpkllNFVNKL 276
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1210-1405 |
6.72e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.56 E-value: 6.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSWD------SITLQQ- 1281
Cdd:PRK11248 2 LQISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEgpgaerGVVFQNe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1282 ----WRK-----AFGVIPQKVfifsgtfrknldPYEQwSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQ 1352
Cdd:PRK11248 80 gllpWRNvqdnvAFGLQLAGV------------EKMQ-RLEIAHQMLKKVGLEGAEKRYIWQ-----------LSGGQRQ 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 1353 LMCLARSVLSKAKILLLDEPSAHLDPVT--------YQIIRRTLKQafadctVILCEHRIE 1405
Cdd:PRK11248 136 RVGIARALAANPQLLLLDEPFGALDAFTreqmqtllLKLWQETGKQ------VLLITHDIE 190
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
435-622 |
8.10e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 57.58 E-value: 8.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 435 LLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG---------RISFC-SQFSWI------- 497
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrEVPFLrRQIGMIfqdhhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 498 MPGTIKEN-----IIFGVSYDEYRYR--SVIKACQLEEDISKFAekdnivlgeggITLSGGQRARISLARAVYKDADLYL 570
Cdd:PRK10908 92 MDRTVYDNvaiplIIAGASGDDIRRRvsAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 571 LDSPFGYLD-VLTEK--EIFESC----VCKLMANKTRILVTskmehlKKADKILILHEG 622
Cdd:PRK10908 161 ADEPTGNLDdALSEGilRLFEEFnrvgVTVLMATHDIGLIS------RRSYRMLTLSDG 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1227-1438 |
8.72e-09 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.28 E-value: 8.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWR-----------KAFGVIPQKVF 1294
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1295 IFSGTFRKNLDPYEQWSDQEiwKVAD---EVGLRSVIEQFPGKLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDE 1371
Cdd:PRK10070 124 LDNTAFGMELAGINAEERRE--KALDalrQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1372 PSAHLDPVTYQIIRRTLK--QAFADCTVILCEHRI-EAMLECQQFLVIEENKVRQYDSIQKLLNE------RSLFR 1438
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVklQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpandyvRTFFR 266
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
1222-1421 |
8.91e-09 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 57.90 E-value: 8.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVswDSITLQQWRKAfgvipqkvfifsgtf 1300
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpDAGTVDLAGV--DLHGLSRRARA--------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1301 rKNLDPYEQWSDQEI-WKVADEVGL-----RSVIEQFP----GKLDFVLVDGGC---------VLSHGHKQLMCLARSVL 1361
Cdd:TIGR03873 75 -RRVALVEQDSDTAVpLTVRDVVALgriphRSLWAGDSphdaAVVDRALARTELshladrdmsTLSGGERQRVHVARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1362 SKAKILLLDEPSAHLDpVTYQI--IRRTLKQAFADCTVILCEHRIE-AMLECQQFLVIEENKV 1421
Cdd:TIGR03873 154 QEPKLLLLDEPTNHLD-VRAQLetLALVRELAATGVTVVAALHDLNlAASYCDHVVVLDGGRV 215
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-633 |
9.56e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 58.13 E-value: 9.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQ-----------------FSWIMPG-- 500
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifqidaiklrkevgmvFQQPNPFph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENIIFGVSYDEYRYRSVIKACqLEEDISKFAEKDNIV--LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEKREIKKI-VEECLRKVGLWKEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 578 LDVLTEKEIfESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK14246 184 IDIVNSQAI-EKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1205-1274 |
1.01e-08 |
|
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: 57.16 E-value: 1.01e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1205 PSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDG-VSW 1274
Cdd:cd03220 16 GSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTL----LRLLAgiyppDSGTVTVRGrVSS 87
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1218-1377 |
1.13e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.56 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1218 KYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRL---LNTEgeiqIDGVSW--DSITLqqwrkafGVIPQK 1292
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTL----LRImagVDKD----FNGEARpqPGIKV-------GYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1293 ------------VFIFSGTFRKNLDPYEQWS------DQEIWKVADEVG-LRSVIEQFPG-----KLDFVLVDGGC---- 1344
Cdd:TIGR03719 77 pqldptktvrenVEEGVAEIKDALDRFNEISakyaepDADFDKLAAEQAeLQEIIDAADAwdldsQLEIAMDALRCppwd 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 90421313 1345 ----VLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:TIGR03719 157 advtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
432-561 |
1.21e-08 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 57.47 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR----------------------IS 489
Cdd:PRK13548 9 SVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelarrravlpqhssLS 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 490 FcsqfswimPGTIKENIIFGVS---YDEYRYRSVIKACQLEEDISKFAEKDNivlgeggITLSGGQRARISLARA 561
Cdd:PRK13548 89 F--------PFTVEEVVAMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDY-------PQLSGGEQQRVQLARV 148
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
438-633 |
1.22e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.10 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR---------------ISFC---SQFswiMP 499
Cdd:PRK13635 20 TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwdvrrqvgMVFQnpdNQF---VG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIF-----GVSYDEY--RYRSVIKACQLEEdiskFAEKDNivlgeggITLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK13635 97 ATVQDDVAFgleniGVPREEMveRVDQALRQVGMED----FLNREP-------HRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 573 SPFGYLDVLTEKEIFEscVCKLMANKTRILV---TSKMEHLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13635 166 EATSMLDPRGRREVLE--TVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1222-1377 |
1.34e-08 |
|
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: 56.73 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEiqidgVSWDSITLQQWRKAFgvipQKVFIFSG-- 1298
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPpLAGR-----VLLNGGPLDFQRDSI----ARGLLYLGha 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1299 -------TFRKNLDPYEQW-SDQEIWKVADEVGLRSViEQFPGKldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLLD 1370
Cdd:cd03231 82 pgikttlSVLENLRFWHADhSDEQVEEALARVGLNGF-EDRPVA----------QLSAGQQRRVALARLLLSGRPLWILD 150
|
....*..
gi 90421313 1371 EPSAHLD 1377
Cdd:cd03231 151 EPTTALD 157
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1222-1405 |
1.36e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 59.26 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRLlnTEGEIQIDG--VSWDSItLQQWRKAFGVIPQKV--F 1294
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLmkiLSGVYQP--DSGEILLDGepVRFRSP-RDAQAAGIAIIHQELnlV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1295 --------IFSGTFRKN---LDpyeqWSDQEIW--KVADEVGLRsvieqfpgkLDF-VLVDGgcvLSHGHKQLMCLARSV 1360
Cdd:COG1129 92 pnlsvaenIFLGREPRRgglID----WRAMRRRarELLARLGLD---------IDPdTPVGD---LSVAQQQLVEIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 90421313 1361 LSKAKILLLDEPSAHLDP----VTYQIIRRtLKQafADCTVILCEHRIE 1405
Cdd:COG1129 156 SRDARVLILDEPTASLTEreveRLFRIIRR-LKA--QGVAIIYISHRLD 201
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
448-636 |
1.71e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 55.66 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 448 IERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-RISFCSQFswimpgtikeniifgvsydeyryrsvikacql 526
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 527 eediskfaekdnivlgeggITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVltEKEIFESCVCKLM---ANKTRILV 603
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI--EQRLNAARAIRRLseeGKKTALVV 128
|
170 180 190
....*....|....*....|....*....|...
gi 90421313 604 TSKMEHLKKADKILILHEGSSYFYGTFSELQNL 636
Cdd:cd03222 129 EHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGT 161
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1213-1421 |
1.74e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.40 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYTEGGNA----ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGEIQIDGVSW-DSITLQQWRKAF 1286
Cdd:PRK13633 8 KNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDGLDTsDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQK--------------VFifsGTFRKNLDPyeqwsdQEIWKVADEvGLRSV----IEQFPGKLdfvlvdggcvLSH 1348
Cdd:PRK13633 88 GMVFQNpdnqivativeedvAF---GPENLGIPP------EEIRERVDE-SLKKVgmyeYRRHAPHL----------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1349 GHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKygITIILITHYMEEAVEADRIIVMDSGKV 222
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
432-582 |
1.77e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKhsgrisfCsqfswimpGTIKEniifgVS 511
Cdd:PRK11147 326 NYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-------C--------GTKLE-----VA 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 512 Y-DEYRyrsvikacqLEEDISKFAEkDNIVLGEGGIT----------------------------LSGGQRARISLARAV 562
Cdd:PRK11147 386 YfDQHR---------AELDPEKTVM-DNLAEGKQEVMvngrprhvlgylqdflfhpkramtpvkaLSGGERNRLLLARLF 455
|
170 180
....*....|....*....|
gi 90421313 563 YKDADLYLLDSPFGYLDVLT 582
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVET 475
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1227-1439 |
2.15e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.79 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGvswdsITLQQWRKAF----GVipqkVFifsG--- 1298
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVpTSGEVRVLG-----YVPFKRRKEFarriGV----VF---Gqrs 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1299 ----------TFRKNldpyeqwsdQEIWKVADEVgLRSVIEQFPGKLDfvlvdggcV----------LSHGHKQLMCLAR 1358
Cdd:COG4586 106 qlwwdlpaidSFRLL---------KAIYRIPDAE-YKKRLDELVELLD--------LgelldtpvrqLSLGQRMRCELAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ--AFADCTVILCEHR---IEAMleCQQFLVIEENKVrQYD-SIQKLLN 1432
Cdd:COG4586 168 ALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDmddIEAL--CDRVIVIDHGRI-IYDgSLEELKE 244
|
....*..
gi 90421313 1433 ERSLFRQ 1439
Cdd:COG4586 245 RFGPYKT 251
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-622 |
2.24e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 56.77 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLL-----MVIMGELEPSEGKIKHSGR---------------ISFCSQFSWIMP 499
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVRLFGRniyspdvdpievrreVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 G-TIKENIIFGVSYD---------EYRYRSVIKACQLEEDIskfaeKDNivLGEGGITLSGGQRARISLARAVYKDADLY 569
Cdd:PRK14267 99 HlTIYDNVAIGVKLNglvkskkelDERVEWALKKAALWDEV-----KDR--LNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90421313 570 LLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVT-SKMEHLKKADKILILHEG 622
Cdd:PRK14267 172 LMDEPTANIDPVGTAKI-EELLFELKKEYTIVLVThSPAQAARVSDYVAFLYLG 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1210-1377 |
2.81e-08 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 57.54 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTegGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVswDSITLQQWRK 1284
Cdd:PRK11607 20 LEIRNLTKSFD--GQHAVDDVSLTIYKGEIFALLGASGCGKSTL----LRMLAgfeqpTAGQIMLDGV--DLSHVPPYQR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQKVFIFSG-TFRKNLD---PYEQWSDQEI-WKVADEVGLRSvIEQFPGKLDFvlvdggcVLSHGHKQLMCLARS 1359
Cdd:PRK11607 92 PINMMFQSYALFPHmTVEQNIAfglKQDKLPKAEIaSRVNEMLGLVH-MQEFAKRKPH-------QLSGGQRQRVALARS 163
|
170
....*....|....*...
gi 90421313 1360 VLSKAKILLLDEPSAHLD 1377
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALD 181
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
97-302 |
2.87e-08 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 56.79 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 97 VQPLLLGRIIASYDPDnkEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKIS 176
Cdd:cd07346 17 ALPLLTKLLIDDVIPA--GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 177 IGQLVSLLSNNLNKFDEGLALAHFVWIAPLqVALLMGLI------WELlqasAFCGLGFLIVLALFQAGLGRMMMK-YRD 249
Cdd:cd07346 95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDV-LTLIGALVilfylnWKL----TLVALLLLPLYVLILRYFRRRIRKaSRE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 250 QR--AGKISERLVitsEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYV 302
Cdd:cd07346 170 VResLAELSAFLQ---ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARL 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
440-623 |
3.08e-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: 55.61 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMG--ELEPSEGKIKHSGrisfcsqfswimpgtikENIIFgVSYDEYRY 517
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKG-----------------EDITD-LPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 518 RSVIKACQLEEDISKFAEKDNI-VLGEGgitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFEScVCKLMA 596
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLrYVNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV-INKLRE 152
|
170 180 190
....*....|....*....|....*....|
gi 90421313 597 NKTRILVTSKMEHL---KKADKILILHEGS 623
Cdd:cd03217 153 EGKSVLIITHYQRLldyIKPDRVHVLYDGR 182
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
440-622 |
3.16e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 58.20 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKtSLLMVIMGELE-PSEGKIKHSGRiSFCSQFSWIMPGTIKENiiFGVSYDEYRYR 518
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGK-STLMNILGCLDkPTSGTYRVAGQ-DVATLDADALAQLRREH--FGFIFQRYHLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 519 SVIKACQLEEDISKFA--------EKDNIVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 581
Cdd:PRK10535 99 SHLTAAQNVEVPAVYAglerkqrlLRAQELLQRLGLedrveyqpsQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90421313 582 TEKEIFesCVCKLMANK--TRILVTSKMEHLKKADKILILHEG 622
Cdd:PRK10535 179 SGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
437-586 |
3.47e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 57.72 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR--------------ISFCSQ-FSwIMPG- 500
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvrfrsprdaqaagIAIIHQeLN-LVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENIIFGvsyDEYRYRSVIKACQLEEDiskfAEKdniVLGEGGI---------TLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG1129 95 SVAENIFLG---REPRRGGLIDWRAMRRR----ARE---LLARLGLdidpdtpvgDLSVAQQQLVEIARALSRDARVLIL 164
|
170
....*....|....*
gi 90421313 572 DSPfgyLDVLTEKEI 586
Cdd:COG1129 165 DEP---TASLTEREV 176
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1210-1439 |
3.93e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 56.33 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVK--DLTAKYTEGG---NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSIT----L 1279
Cdd:PRK13646 1 MTIRfdNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKpTTGTVTVDDITITHKTkdkyI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1280 QQWRKAFGVIPQ------------KVFIFS-GTFRKNLDPYEQWSdqeiWKVADEVGL-RSVIEQFPGKldfvlvdggcv 1345
Cdd:PRK13646 81 RPVRKRIGMVFQfpesqlfedtveREIIFGpKNFKMNLDEVKNYA----HRLLMDLGFsRDVMSQSPFQ----------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1346 LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLK--QAFADCTVILCEHRieaMLECQQFlvIEENKVRQ 1423
Cdd:PRK13646 146 MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHD---MNEVARY--ADEVIVMK 220
|
250
....*....|....*.
gi 90421313 1424 YDSIQKLLNERSLFRQ 1439
Cdd:PRK13646 221 EGSIVSQTSPKELFKD 236
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
437-493 |
4.40e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.59 E-value: 4.40e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHS--GRISFCSQ 493
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSenANIGYYAQ 389
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
437-639 |
4.43e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-ISFCSQFSWIMPG--------------T 501
Cdd:PRK11288 16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQeMRFASTTAALAAGvaiiyqelhlvpemT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKENIIFG--------VSYDEYRYRSVIKACQLEEDISKfaekdNIVLGEggitLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK11288 96 VAENLYLGqlphkggiVNRRLLNYEAREQLEHLGVDIDP-----DTPLKY----LSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 574 PFGYLDVlTEKEIFESCVCKLMANKTRIL-VTSKMEHL-KKADKILILHEGSsyFYGTFSELQNLQPD 639
Cdd:PRK11288 167 PTSSLSA-REIEQLFRVIRELRAEGRVILyVSHRMEEIfALCDAITVFKDGR--YVATFDDMAQVDRD 231
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1212-1403 |
4.67e-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: 57.64 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsaFLRLLNTE----GEIQIDgvswDSITLqqwrkafG 1287
Cdd:TIGR03719 325 AENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTL---FRMITGQEqpdsGTIEIG----ETVKL-------A 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQkvfifsgtFRKNLDP----YEQWSD-QEIWKVAD-EVGLRSVIEQFPGKldfvlvdGG------CVLSHGHKQLMC 1355
Cdd:TIGR03719 389 YVDQ--------SRDALDPnktvWEEISGgLDIIKLGKrEIPSRAYVGRFNFK-------GSdqqkkvGQLSGGERNRVH 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 1356 LARSVLSKAKILLLDEPSAHLDPVTYqiirRTLKQA---FADCTVILCEHR 1403
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETL----RALEEAllnFAGCAVVISHDR 500
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1210-1402 |
5.47e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 55.77 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRllNTEGEIQIDGVSWDSI--------- 1277
Cdd:PRK11300 6 LSVSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVfncLTGFYK--PTGGTILLRGQHIEGLpghqiarmg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1278 ---TLQQWR--KAFGVIPQ---------KVFIFSGTF---------RKNLDPYEQWSDQeiwkvadeVGLRSVIEQFPGK 1334
Cdd:PRK11300 82 vvrTFQHVRlfREMTVIENllvaqhqqlKTGLFSGLLktpafrraeSEALDRAATWLER--------VGLLEHANRQAGN 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1335 LdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTY----QIIRRtLKQAFaDCTVILCEH 1402
Cdd:PRK11300 154 L-----------AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETkeldELIAE-LRNEH-NVTVLLIEH 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1222-1400 |
5.87e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 54.55 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEI------------QIDGVSW-------DSITLQQ 1281
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRpTSGTVrraggarvayvpQRSEVPDslpltvrDLVAMGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1282 WRKafgvipqkvfifsgtfRKNLDPYEQWSDQEIWKVADEVGL-----RSVIEqfpgkldfvlvdggcvLSHGHKQLMCL 1356
Cdd:NF040873 83 WAR----------------RGLWRRLTRDDRAAVDDALERVGLadlagRQLGE----------------LSGGQRQRALL 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILC 1400
Cdd:NF040873 131 AQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVV 174
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
438-623 |
7.47e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELE--PSEGKIKhsgrisfcsqfswimpgtIKENIIfgvsydeY 515
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD------------------VPDNQF-------G 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 516 RYRSVIKACQLEEDISKFAEkdniVLGEGGI-----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEK 584
Cdd:COG2401 98 REASLIDAIGRKGDFKDAVE----LLNAVGLsdavlwlrrfkELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 90421313 585 EIfESCVCKLM--ANKTRILVTSKMEhLKKA---DKILILHEGS 623
Cdd:COG2401 174 RV-ARNLQKLArrAGITLVVATHHYD-VIDDlqpDLLIFVGYGG 215
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1212-1404 |
7.60e-08 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.11 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYTEGGNAiLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGEIQIDGvswDSITLQqwrkaf 1286
Cdd:cd03237 1 YTYPTMKKTLGEFT-LEVEGGSISESEVIGILGPNGIGKTT----FIKMLAgvlkpDEGDIEIEL---DTVSYK------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 gviPQKV----------FIFSGTFRKNLDPYeqwsdqeiWK--VADEVGLRSVIEQfpgkldfVLVDggcvLSHGHKQLM 1354
Cdd:cd03237 67 ---PQYIkadyegtvrdLLSSITKDFYTHPY--------FKteIAKPLQIEQILDR-------EVPE----LSGGELQRV 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 90421313 1355 CLARSVLSKAKILLLDEPSAHLDP----VTYQIIRRTLKQafADCTVILCEHRI 1404
Cdd:cd03237 125 AIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFAEN--NEKTAFVVEHDI 176
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
437-642 |
8.06e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 57.48 E-value: 8.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTP-VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-------ISFCSQFSWI------MPGTI 502
Cdd:PTZ00243 1321 GLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGReigayglRELRRQFSMIpqdpvlFDGTV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 503 KENIIfgvSYDEYRYRSVIKACQL---EEDISKFAEK-DNIVLgEGGITLSGGQRARISLARAVYK-DADLYLLDSPFGY 577
Cdd:PTZ00243 1401 RQNVD---PFLEASSAEVWAALELvglRERVASESEGiDSRVL-EGGSNYSVGQRQLMCMARALLKkGSGFILMDEATAN 1476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 578 LDVLTEKEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL-QNLQPDFSS 642
Cdd:PTZ00243 1477 IDPALDRQI-QATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHS 1541
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
439-623 |
8.09e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 8.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEP---SEGKIKHSGrISFCSQFSW----------------IMP 499
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG-ITLTAKTVWdirekvgivfqnpdnqFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 GTIKENIIFGVsydeyRYRSVIKacqleEDISKFAEKdniVLGEGGIT---------LSGGQRARISLARAVYKDADLYL 570
Cdd:PRK13640 100 ATVGDDVAFGL-----ENRAVPR-----PEMIKIVRD---VLADVGMLdyidsepanLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 571 LDSPFGYLDVLTEKEIFeSCVCKLMANK--TRILVTSKMEHLKKADKILILHEGS 623
Cdd:PRK13640 167 LDESTSMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGK 220
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
437-588 |
8.75e-08 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 54.90 E-value: 8.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEpsegkiKHSGRISFCSQFSWIMPgtIKENIIFGVSY---- 512
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP------RDAGNIIIDDEDISLLP--LHARARRGIGYlpqe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 513 -DEYR----YRSVIKACQLEEDISKFAEKD--NIVLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK10895 87 aSIFRrlsvYDNLMAVLQIRDDLSAEQREDraNELMEEFHIEhlrdsmgqsLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170
....*....|....*
gi 90421313 577 YLD---VLTEKEIFE 588
Cdd:PRK10895 167 GVDpisVIDIKRIIE 181
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
440-643 |
9.43e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 55.19 E-value: 9.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR---------------ISFCSQFSWIMPGTIKE 504
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEpitkenirevrkfvgLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFG---VSYDE----YRYRSVIKACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK13652 99 DIAFGpinLGLDEetvaHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 578 LDVLTEKEIFescvckLMANK-------TRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELqNLQPDFSSK 643
Cdd:PRK13652 168 LDPQGVKELI------DFLNDlpetygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI-FLQPDLLAR 234
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1222-1402 |
9.57e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.73 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQidgvswdsitlQQWRKAFGVIPQKVFIFSG-- 1298
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIK-----------RNGKLRIGYVPQKLYLDTTlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1299 -TFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:PRK09544 84 lTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
170 180 190
....*....|....*....|....*....|...
gi 90421313 1378 pVTYQI--------IRRTLkqafaDCTVILCEH 1402
Cdd:PRK09544 153 -VNGQValydlidqLRREL-----DCAVLMVSH 179
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1223-1404 |
9.95e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.18 E-value: 9.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1223 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGV---SWDSitlqqwrKAF----GVIPQKVF 1294
Cdd:PRK10575 23 GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPpSEGEILLDAQpleSWSS-------KAFarkvAYLPQQLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1295 IFSG-TFRK-----------NLDPYEQWSDQEIWKVADEVGLRSVIEQfpgkldfvLVDGgcvLSHGHKQLMCLARSVLS 1362
Cdd:PRK10575 96 AAEGmTVRElvaigrypwhgALGRFGAADREKVEEAISLVGLKPLAHR--------LVDS---LSGGERQRAWIAMLVAQ 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90421313 1363 KAKILLLDEPSAHLDpVTYQI-----IRRTLKQafADCTVILCEHRI 1404
Cdd:PRK10575 165 DSRCLLLDEPTSALD-IAHQVdvlalVHRLSQE--RGLTVIAVLHDI 208
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
440-632 |
1.01e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.81 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPS--EGKIKHSG---------RISFCSQFSWIMPG-TIKENII 507
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNrkptkqilkRTGFVTQDDILYPHlTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 508 F--------GVSYDEyryrsviKACQLEEDISK--FAEKDNIVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PLN03211 163 FcsllrlpkSLTKQE-------KILVAESVISElgLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 577 YLDVLTEKEIFESCVCklMANKTRILVTSKMEHLKKA----DKILILHEGSSYFYGTFSE 632
Cdd:PLN03211 236 GLDATAAYRLVLTLGS--LAQKGKTIVTSMHQPSSRVyqmfDSVLVLSEGRCLFFGKGSD 293
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1210-1421 |
1.03e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.63 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGN---AILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQI-DGVSWDSITLQqwRK 1284
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKyGTIQVgDIYIGDKKNNH--EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQKVFIFSgTFRKNLDPYEQWSDQEIWKVADE-------VGLRSVIEQFPGKLDFVLVDGGC----------VLS 1347
Cdd:PRK13631 100 ITNPYSKKIKNFK-ELRRRVSMVFQFPEYQLFKDTIEkdimfgpVALGVKKSEAKKLAKFYLNKMGLddsylerspfGLS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1348 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADC-TVILCEHRIEAMLE-CQQFLVIEENKV 1421
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNkTVFVITHTMEHVLEvADEVIVMDKGKI 254
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-604 |
1.13e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.53 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVI--MGELEPS---EGKIKHSG-------------RISFCSQFSWIMP 499
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGqdifkmdvielrrRVQMVFQIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 G-TIKENIIFGVSYD---------EYRYRSVIKACQLEEDIskfaeKDNivLGEGGITLSGGQRARISLARAVYKDADLY 569
Cdd:PRK14247 96 NlSIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-----KDR--LDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190
....*....|....*....|....*....|....*
gi 90421313 570 LLDSPFGYLDVLTEKEIfESCVCKLMANKTRILVT 604
Cdd:PRK14247 169 LADEPTANLDPENTAKI-ESLFLELKKDMTIVLVT 202
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
441-644 |
1.14e-07 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 56.59 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPS---EGKIKHSG---------RIS-FCSQFSWIMPG-TIKENI 506
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGmpidakemrAISaYVQQDDLFIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 IF--------GVSYDEYRYRsvIKACQLEEDISKFAekdNIVLGEGGIT--LSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:TIGR00955 121 MFqahlrmprRVTKKEKRER--VDEVLQALGLRKCA---NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90421313 577 YLDVLTEKEIFEscVCKLMANKTRILV------TSKMEHLkkADKILILHEGSSYFYGTFSELqnlqPDFSSKL 644
Cdd:TIGR00955 196 GLDSFMAYSVVQ--VLKGLAQKGKTIIctihqpSSELFEL--FDKIILMAEGRVAYLGSPDQA----VPFFSDL 261
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
437-622 |
1.33e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 54.37 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK--------------HSGRISFCSQ--------F 494
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidtarslsqQKGLIRQLRQhvgfvfqnF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 495 SWIMPGTIKENIIFGvsydeyryRSVIKACQLEEDISKFAEkdniVLGEGGIT---------LSGGQRARISLARAVYKD 565
Cdd:PRK11264 95 NLFPHRTVLENIIEG--------PVIVKGEPKEEATARARE----LLAKVGLAgketsyprrLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 566 ADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQG 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1211-1377 |
1.39e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLntEGEIQIDG--VSWDSitlqqwRKAFGV 1288
Cdd:PRK15064 321 EVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLL----RTL--VGELEPDSgtVKWSE------NANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 IPQKVfifSGTFRKNLDPYEqWSDQeiWKVA--DEVGLRSVIeqfpGKLDFVLVDGG---CVLSHGHKQLMCLARSVLSK 1363
Cdd:PRK15064 387 YAQDH---AYDFENDLTLFD-WMSQ--WRQEgdDEQAVRGTL----GRLLFSQDDIKksvKVLSGGEKGRMLFGKLMMQK 456
|
170
....*....|....
gi 90421313 1364 AKILLLDEPSAHLD 1377
Cdd:PRK15064 457 PNVLVMDEPTNHMD 470
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1223-1377 |
1.59e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 54.45 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1223 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL---------RLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQ-- 1291
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggapRGARVTGDVTLNGEPLAAIDAPRLARLRAVLPQaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1292 -KVFIFSGTFRKNLDPYEQWSDQEIWKVADevglRSVIEQFPGKLDFVLVDGGCV--LSHGHKQLMCLARsVLSK----- 1363
Cdd:PRK13547 93 qPAFAFSAREIVLLGRYPHARRAGALTHRD----GEIAWQALALAGATALVGRDVttLSGGELARVQFAR-VLAQlwpph 167
|
170
....*....|....*....
gi 90421313 1364 -----AKILLLDEPSAHLD 1377
Cdd:PRK13547 168 daaqpPRYLLLDEPTAALD 186
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
432-622 |
2.26e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.48 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVI-------MGELE-----------PSEGKIKHSGR---ISF 490
Cdd:PRK11124 9 NCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNiagnhfdfsktPSDKAIRELRRnvgMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 491 CSQFSWimPG-TIKENII------FGVSYDEYRYRS--VIKACQLEEDISKFAekdnivlgeggITLSGGQRARISLARA 561
Cdd:PRK11124 89 QQYNLW--PHlTVQQNLIeapcrvLGLSKDQALARAekLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 562 VYKDADLYLLDSPFGYLD-------VLTEKEIFESCVcklmankTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDpeitaqiVSIIRELAETGI-------TQVIVTHEVEVARKtASRVVYMENG 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
439-645 |
2.66e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.97 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------------RISFC-----SQFswiMPG 500
Cdd:PRK13650 21 YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGdllteenvwdirhKIGMVfqnpdNQF---VGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 TIKENIIFG-----VSYDEYRYRsVIKACQLEeDISKFAEKDNIvlgeggiTLSGGQRARISLARAVYKDADLYLLDS-- 573
Cdd:PRK13650 98 TVEDDVAFGlenkgIPHEEMKER-VNEALELV-GMQDFKEREPA-------RLSGGQKQRVAIAGAVAMRPKIIILDEat 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 574 ----PFGYLDVL-TEKEIFEScvcklmANKTRILVTSKMEHLKKADKILILHEG---SSY----FYGTFSELQNLQPD-- 639
Cdd:PRK13650 169 smldPEGRLELIkTIKGIRDD------YQMTVISITHDLDEVALSDRVLVMKNGqveSTStpreLFSRGNDLLQLGLDip 242
|
....*.
gi 90421313 640 FSSKLM 645
Cdd:PRK13650 243 FTTSLV 248
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1222-1377 |
2.83e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.18 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSaflrLLntEGEIQIDGVS------WDSITLQQWRKAFGViPQKVFI 1295
Cdd:PRK10636 12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLA----LL--KNEISADGGSytfpgnWQLAWVNQETPALPQ-PALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1296 FSG--TFRKnldpyeqwSDQEIwKVADEVGLRSVIEQFPGKLDFV-----------LVDGgcvLSHGHKQL--------- 1353
Cdd:PRK10636 85 IDGdrEYRQ--------LEAQL-HDANERNDGHAIATIHGKLDAIdawtirsraasLLHG---LGFSNEQLerpvsdfsg 152
|
170 180
....*....|....*....|....*....
gi 90421313 1354 -----MCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:PRK10636 153 gwrmrLNLAQALICRSDLLLLDEPTNHLD 181
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1227-1402 |
2.88e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVS---WDSITL--------QQWRKAFGVipqKVFI 1295
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPleaWSAAELarhraylsQQQTPPFAM---PVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1296 FsgtfrknLDPYEQWSDQEiwkVADEVGLRSVIEQFpgKLDFVLVDGGCVLSHGHKQLMCLARSVL-------SKAKILL 1368
Cdd:PRK03695 89 Y-------LTLHQPDKTRT---EAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 90421313 1369 LDEPSAHLDpVT-----YQIIRRTLKQAFAdctVILCEH 1402
Cdd:PRK03695 157 LDEPMNSLD-VAqqaalDRLLSELCQQGIA---VVMSSH 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1226-1377 |
3.20e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1226 ILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTE-----GEIQIDG---VSwdsiTLQQ--WRKAFGvipqKVFI 1295
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTL----MKILNGEvllddGRIIYEQdliVA----RLQQdpPRNVEG----TVYD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1296 FS----GTFRKNLDPYEQWSDQeiwkVADE---------VGLRSVIE-----QFPGKLDFVLVDGG-------CVLSHGH 1350
Cdd:PRK11147 86 FVaegiEEQAEYLKRYHDISHL----VETDpseknlnelAKLQEQLDhhnlwQLENRINEVLAQLGldpdaalSSLSGGW 161
|
170 180
....*....|....*....|....*..
gi 90421313 1351 KQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:PRK11147 162 LRKAALGRALVSNPDVLLLDEPTNHLD 188
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
439-586 |
3.32e-07 |
|
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: 53.90 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 439 PVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGeLEPSEGKIkhSGRISFCSQFSWIMPGtiKEniifgvsYDEYRYR 518
Cdd:COG0444 19 KAVDGVSFDVRRGETLGLVGESGSGKSTLARAILG-LLPPPGIT--SGEILFDGEDLLKLSE--KE-------LRKIRGR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 519 SV----------------IKAcQLEE------DISKfAEKDNIV---LGEGGIT------------LSGGQRARISLARA 561
Cdd:COG0444 87 EIqmifqdpmtslnpvmtVGD-QIAEplrihgGLSK-AEARERAielLERVGLPdperrldrypheLSGGMRQRVMIARA 164
|
170 180
....*....|....*....|....*
gi 90421313 562 VYKDADLYLLDSPFGYLDVLTEKEI 586
Cdd:COG0444 165 LALEPKLLIADEPTTALDVTIQAQI 189
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
437-574 |
3.69e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 54.67 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR--------------ISFCSQFSWIMPG-T 501
Cdd:PRK15439 23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNpcarltpakahqlgIYLVPQEPLLFPNlS 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 502 IKENIIFGVSYDEYRYRSVIK-----ACQLEEDISkfaekdnivlgegGITLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQllaalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1227-1399 |
3.75e-07 |
|
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: 52.82 E-value: 3.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-LLNTEGEIQIdgvswdsitlqqwRKAFGVIpqkvfifsgtfrkNLd 1305
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPDSGSILV-------------RHDGGWV-------------DL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1306 pyEQWSDQEIWKV-ADEVGLRSvieQF----P--GKLDFV---LVDGGC-----------VLSH---------------- 1348
Cdd:COG4778 80 --AQASPREILALrRRTIGYVS---QFlrviPrvSALDVVaepLLERGVdreeararareLLARlnlperlwdlppatfs 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1349 -GHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVIL 1399
Cdd:COG4778 155 gGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
411-623 |
3.90e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 411 KAKQNNNNRKTSNGDDSLFFS--NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-R 487
Cdd:PRK09700 247 QNRFNAMKENVSNLAHETVFEvrNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 488 ISFCSQFSWIMPG-----------------TIKENIIFGVSYDEYRYRSVIKACQlEEDISKFAEKDNIVLG------EG 544
Cdd:PRK09700 327 ISPRSPLDAVKKGmayitesrrdngffpnfSIAQNMAISRSLKDGGYKGAMGLFH-EVDEQRTAENQRELLAlkchsvNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 545 GIT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFescvcKLM-----ANKTRILVTSKM-EHLKKADKIL 617
Cdd:PRK09700 406 NITeLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY-----KVMrqladDGKVILMVSSELpEIITVCDRIA 480
|
....*.
gi 90421313 618 ILHEGS 623
Cdd:PRK09700 481 VFCEGR 486
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1210-1394 |
3.91e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.79 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEI--------------QIDGVSW 1274
Cdd:PRK10636 313 LKMEKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPvSGEIglakgiklgyfaqhQLEFLRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1275 DSITLQQW-RKAFGVIPQKVFIFSGTFRKNLDpyeqwsdqeiwKVADEVglrsviEQFPGkldfvlvdggcvlshGHKQL 1353
Cdd:PRK10636 391 DESPLQHLaRLAPQELEQKLRDYLGGFGFQGD-----------KVTEET------RRFSG---------------GEKAR 438
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 90421313 1354 MCLARSVLSKAKILLLDEPSAHLDpvtyQIIRRTLKQAFAD 1394
Cdd:PRK10636 439 LVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEALID 475
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
425-590 |
3.94e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 54.75 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 425 DDSLFFSNFSLLgTP----VLKDINFKIERGQLLAVAGSTGAGKTSLLMVImGELEPSEG---KIKHSGRISFCSQFSWI 497
Cdd:TIGR00954 449 DNGIKFENIPLV-TPngdvLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGgrlTKPAKGKLFYVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 498 MPGTIKENIIFGVSYDEYRYRSVIKAcQLEEdISKFAEKDNIVLGEGGIT--------LSGGQRARISLARAVYKDADLY 569
Cdd:TIGR00954 527 TLGTLRDQIIYPDSSEDMKRRGLSDK-DLEQ-ILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFA 604
|
170 180
....*....|....*....|.
gi 90421313 570 LLDSPFGYLDVLTEKEIFESC 590
Cdd:TIGR00954 605 ILDECTSAVSVDVEGYMYRLC 625
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1205-1423 |
4.08e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.47 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1205 PSGGQMTVKDLTAKYTEGGN--AILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQ 1281
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQGEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQPLHQMDEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1282 wRKAF-----GVIPQKvFIFSGTF--RKNLD-------PYEQWSDQEIWKVADEVGLRSVIEQFPGKLdfvlvdggcvlS 1347
Cdd:PRK10584 82 -RAKLrakhvGFVFQS-FMLIPTLnaLENVElpallrgESSRQSRNGAKALLEQLGLGKRLDHLPAQL-----------S 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1348 HGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRR---TLKQAFAdCTVILCEHRIEAMLECQQFLVIEENKVRQ 1423
Cdd:PRK10584 149 GGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADllfSLNREHG-TTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1210-1430 |
4.14e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.20 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKY-TEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGvswDSITLQQ-W--RK 1284
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDG---DLLTEENvWdiRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVI---PQKVFIFS--------GTFRKNLDpyeqwsDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHG 1349
Cdd:PRK13650 82 KIGMVfqnPDNQFVGAtveddvafGLENKGIP------HEEMKERVNEalelVGMQDFKEREPAR-----------LSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1350 HKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVILCEHRIEAMLECQQFLVIEENKVRQYDSI 1427
Cdd:PRK13650 145 QKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyqMTVISITHDLDEVALSDRVLVMKNGQVESTSTP 224
|
...
gi 90421313 1428 QKL 1430
Cdd:PRK13650 225 REL 227
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1210-1399 |
4.72e-07 |
|
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: 51.66 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTeggnaiLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSWDSITLQQWRKA-FG 1287
Cdd:cd03215 5 LEVRGLSVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPAsGEITLDGKPVTRRSPRDAIRAgIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKvfifsgtfRKnldpyeqwsdqeiwkvadEVGL---RSVIEqfpgklDFVLvdgGCVLSHGHKQLMCLARSVLSKA 1364
Cdd:cd03215 79 YVPED--------RK------------------REGLvldLSVAE------NIAL---SSLLSGGNQQKVVLARWLARDP 123
|
170 180 190
....*....|....*....|....*....|....*.
gi 90421313 1365 KILLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVIL 1399
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAgKAVLL 159
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1222-1377 |
4.80e-07 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 53.80 E-value: 4.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSITLQQwRK------------ 1284
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTV----LRLIAgfetpDSGRIMLDGQDITHVPAEN-RHvntvfqsyalfp 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 --------AFGVIPQKVfifsgtfrknldpyeqwSDQEIWK-VADevGLRSV-IEQF----PGKldfvlvdggcvLSHGH 1350
Cdd:PRK09452 100 hmtvfenvAFGLRMQKT-----------------PAAEITPrVME--ALRMVqLEEFaqrkPHQ-----------LSGGQ 149
|
170 180
....*....|....*....|....*..
gi 90421313 1351 KQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:PRK09452 150 QQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
956-1289 |
4.95e-07 |
|
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: 54.42 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 956 VLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLtIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQ 1035
Cdd:COG4615 91 ILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1036 TSQQLKQLESEGRSPIFTHLVTSLKG-----LWTLRafgRQPYFETLFH------KALNLHTANWFLylSTLRWFQMrie 1104
Cdd:COG4615 170 RARRHLRRAREAEDRLFKHFRALLEGfkelkLNRRR---RRAFFDEDLQptaeryRDLRIRADTIFA--LANNWGNL--- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1105 MIF----VIFFIAVTFISIlttgEGEGRVGIILTLaMNIMSTLQWAVNSsidVDSLMR---SVSRVFKFIDMPTEGKPTK 1177
Cdd:COG4615 242 LFFaligLILFLLPALGWA----DPAVLSGFVLVL-LFLRGPLSQLVGA---LPTLSRanvALRKIEELELALAAAEPAA 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1178 STKPykngqlskvmiienshvkkDDIWPSGGQ-MTVKDLTAKY--TEGGNA-ILENISFSISPGQRVGLLGRTGSGKSTl 1253
Cdd:COG4615 314 ADAA-------------------APPAPADFQtLELRGVTYRYpgEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKST- 373
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 90421313 1254 lsaFLRLLN-----TEGEIQIDGVSWDSITLQQWRKAFGVI 1289
Cdd:COG4615 374 ---LAKLLTglyrpESGEILLDGQPVTADNREAYRQLFSAV 411
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1226-1405 |
4.97e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.27 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1226 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-LLNTEGEIQIDgVSWDSItlqqwrkafgvipqkvfifsgtfrknl 1304
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVD-VPDNQF--------------------------- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1305 dpyeqwsDQEiwkvadevglRSVIEQFPGKLDF-----VLVDGGCV-----------LSHGHKQLMCLARSVLSKAKILL 1368
Cdd:COG2401 97 -------GRE----------ASLIDAIGRKGDFkdaveLLNAVGLSdavlwlrrfkeLSTGQKFRFRLALLLAERPKLLV 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 90421313 1369 LDEPSAHLDPVTYQIIRRTLKQAF--ADCTVILCEHRIE 1405
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHHYD 198
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1210-1405 |
5.05e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.06 E-value: 5.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRLLNTEGEIQIDGVSWDSITLQQW-RKA 1285
Cdd:TIGR02633 2 LEMKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWDGEIYWSGSPLKASNIRDTeRAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1286 FGVIPQKVfifsgTFRKNLDPYEQ-WSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCV------LSHGHKQLMCLAR 1358
Cdd:TIGR02633 80 IVIIHQEL-----TLVPELSVAENiFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVtrpvgdYGGGQQQLVEIAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVTYQI---IRRTLKQAFADCTVIlcEHRIE 1405
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEIlldIIRDLKAHGVACVYI--SHKLN 202
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1210-1409 |
5.33e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 52.96 E-value: 5.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAiLENISFSISPGQRVGLLGRTGSGKSTLLSA---FLRLlnTEGEIQIDGvswdsitlQQWRKAf 1286
Cdd:PRK15056 7 IVVNDVTVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKAlmgFVRL--ASGKISILG--------QPTRQA- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 gvipqkvfifsgtFRKNLDPYEQWSDQEIWK----VADEVGL----------------RSVIEQFPGKLDFVLVDGGCV- 1345
Cdd:PRK15056 75 -------------LQKNLVAYVPQSEEVDWSfpvlVEDVVMMgryghmgwlrrakkrdRQIVTAALARVDMVEFRHRQIg 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1346 -LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEHRIEAMLE 1409
Cdd:PRK15056 142 eLSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTE 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
441-635 |
5.70e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 52.71 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLM----VIMGELEPS------------EGKIK--------HSGRISfcSQFSW 496
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGshiellgrtvqrEGRLArdirksraNTGYIF--QQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 497 IMPGTIKENIIFGVSYDEYRYRSVIK---ACQLEEDISKFAEKDNIVLGEGGI-TLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK09984 98 VNRLSVLENVLIGALGSTPFWRTCFSwftREQKQRALQALTRVGMVHFAHQRVsTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 573 SPFGYLDVLTEKEIFESCVCKLMANKTRILVT-SKMEH-LKKADKILILHEGSSYFYGTFSELQN 635
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQGHVFYDGSSQQFDN 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
441-659 |
6.47e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 6.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR--------------ISFCSQ-FSWIMPGTIKEN 505
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQeLSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFG------------VSYDEYRYRSVI--KACQLEEDISKFAEKdnivlgeggitLSGGQRARISLARAVYKDADLYLL 571
Cdd:PRK09700 101 LYIGrhltkkvcgvniIDWREMRVRAAMmlLRVGLKVDLDEKVAN-----------LSISHKQMLEIAKTLMLDAKVIIM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 572 DSPfgyLDVLTEKEI---FescvckLMANKTR------ILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELQNlqPDFS 641
Cdd:PRK09700 170 DEP---TSSLTNKEVdylF------LIMNQLRkegtaiVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSN--DDIV 238
|
250
....*....|....*...
gi 90421313 642 SKLMGCDSFDQFSAERRN 659
Cdd:PRK09700 239 RLMVGRELQNRFNAMKEN 256
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1227-1434 |
6.77e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 53.76 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSwdsitlQQWRKAFGVIPQKVFIFSgtfr 1301
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL----LKILSgnyqpDAGSILIDGQE------MRFASTTAALAAGVAIIY---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1302 knldpyeqwsdQEIWKVADevglRSVIE-----QFPGKLDFvlVDGGCV-----------------------LSHGHKQL 1353
Cdd:PRK11288 86 -----------QELHLVPE----MTVAEnlylgQLPHKGGI--VNRRLLnyeareqlehlgvdidpdtplkyLSIGQRQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1354 MCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVIL-CEHRIEAMLE-CQQFLVIEE-NKVRQYDSIQKL 1430
Cdd:PRK11288 149 VEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDgRYVATFDDMAQV 228
|
....
gi 90421313 1431 LNER 1434
Cdd:PRK11288 229 DRDQ 232
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1215-1383 |
6.96e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.30 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1215 LTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGVIPQKV 1293
Cdd:PRK10253 13 LTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1294 FIFSGTFRKNLDPYEQWSDQEI---WKVADEVGLRSVIeQFPGKLDFVL--VDggcVLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:PRK10253 91 TTPGDITVQELVARGRYPHQPLftrWRKEDEEAVTKAM-QATGITHLADqsVD---TLSGGQRQRAWIAMVLAQETAIML 166
|
170
....*....|....*
gi 90421313 1369 LDEPSAHLDpVTYQI 1383
Cdd:PRK10253 167 LDEPTTWLD-ISHQI 180
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1210-1284 |
7.16e-07 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 53.53 E-value: 7.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNA--ILENISFSISPGQRVGLLGRTGSGKS-TLLSAfLRLL-----NTEGEIQIDGVSWDSITLQQ 1281
Cdd:COG4172 7 LSVEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvTALSI-LRLLpdpaaHPSGSILFDGQDLLGLSERE 85
|
...
gi 90421313 1282 WRK 1284
Cdd:COG4172 86 LRR 88
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1210-1390 |
9.31e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGG--NAILENISFSISPGQRVGLLGRTGSGKS-TLLSaFLRLLNT------EGEIQIDGVSW---DSI 1277
Cdd:PRK15134 6 LAIENLSVAFRQQQtvRTVVNDVSLQIEAGETLALVGESGSGKSvTALS-ILRLLPSppvvypSGDIRFHGESLlhaSEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1278 TLQQWRKAfgvipQKVFIFS---------GTFRKNLdpYEQWS----------DQEIWKVADEVGLRsvieQFPGKLDfv 1338
Cdd:PRK15134 85 TLRGVRGN-----KIAMIFQepmvslnplHTLEKQL--YEVLSlhrgmrreaaRGEILNCLDRVGIR----QAAKRLT-- 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 1339 lvDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD-PVTYQIIR--RTLKQ 1390
Cdd:PRK15134 152 --DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDvSVQAQILQllRELQQ 204
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
437-622 |
9.33e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.72 E-value: 9.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVI-----------------MGELEPSEGKIkhsGRIsFcsQFSWIMP 499
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIagleditsgdlfigekrMNDVPPAERGV---GMV-F--QSYALYP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 500 G-TIKENIIFGVSYdeyryrSVIKACQLEEDISKFAEkdniVLGEGGI------TLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK11000 89 HlSVAENMSFGLKL------AGAKKEEINQRVNQVAE----VLQLAHLldrkpkALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 573 SPFGYLD----VLTEKEIfescvCKLMA--NKTRILVT-SKMEHLKKADKILILHEG 622
Cdd:PRK11000 159 EPLSNLDaalrVQMRIEI-----SRLHKrlGRTMIYVThDQVEAMTLADKIVVLDAG 210
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1227-1407 |
1.03e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.11 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRLlnTEGEIQIDGV------SWDSITL------QQwrkaFGVIPQ 1291
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLmkiLYGLYQP--DSGEILIDGKpvrirsPRDAIALgigmvhQH----FMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1292 kvfiFS----------GTFRKNLDpyeqwsdqeiWKVADEVgLRSVIEQFPGKLDF-VLVDGgcvLSHGHKQ----LMCL 1356
Cdd:COG3845 95 ----LTvaenivlglePTKGGRLD----------RKAARAR-IRELSERYGLDVDPdAKVED---LSVGEQQrveiLKAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 1357 ARsvlsKAKILLLDEPSAHLDP--VT--YQIIRRtLKQafADCTVILCEHRI-EAM 1407
Cdd:COG3845 157 YR----GARILILDEPTAVLTPqeADelFEILRR-LAA--EGKSIIFITHKLrEVM 205
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1227-1384 |
1.07e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEIQIDGVSWDSIT---LQQWRKAFGvipqkvFIFSGTFrK 1302
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESqGGEIIFNGQRIDTLSpgkLQALRRDIQ------FIFQDPY-A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1303 NLDPYEQ--WSDQEIWKV----------------ADEVGLRSVIE-QFPGKldfvlvdggcvLSHGHKQLMCLARSVLSK 1363
Cdd:PRK10261 413 SLDPRQTvgDSIMEPLRVhgllpgkaaaarvawlLERVGLLPEHAwRYPHE-----------FSGGQRQRICIARALALN 481
|
170 180
....*....|....*....|..
gi 90421313 1364 AKILLLDEPSAHLD-PVTYQII 1384
Cdd:PRK10261 482 PKVIIADEAVSALDvSIRGQII 503
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1209-1409 |
1.08e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.40 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1209 QMTVKDLTAKYTEGGNA---ILENISFSISPGQRVGLLGRTGSGKSTL---LSAFlrLLNTEGEIQIDGVSW-------- 1274
Cdd:PRK13651 2 QIKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNAL--LLPDTGTIEWIFKDEknkkktke 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1275 -----DSITLQ-----------QWRKAFGVIPQkvF----IFSGTFRKNL--DPYEQW-SDQEIWKVADE----VGLRsv 1327
Cdd:PRK13651 80 kekvlEKLVIQktrfkkikkikEIRRRVGVVFQ--FaeyqLFEQTIEKDIifGPVSMGvSKEEAKKRAAKyielVGLD-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1328 iEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADC-TVILCEHRIEA 1406
Cdd:PRK13651 156 -ESYLQRSPF-------ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGkTIILVTHDLDN 227
|
...
gi 90421313 1407 MLE 1409
Cdd:PRK13651 228 VLE 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1210-1421 |
1.11e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 52.02 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNA-ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGEIQIDGVSWDSITLQQWRKAFG 1287
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VI---PQKVFIfSGTFRKNLD---PYEQWSDQEIWKVADEVGLRSVIeqfpgkLDFVLVDGGcVLSHGHKQLMCLARSVL 1361
Cdd:PRK13642 85 MVfqnPDNQFV-GATVEDDVAfgmENQGIPREEMIKRVDEALLAVNM------LDFKTREPA-RLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1362 SKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD--CTVILCEHRIEAMLECQQFLVIEENKV 1421
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
440-622 |
1.16e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 51.42 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPG---------------TIKE 504
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 505 NIIFGVSY-DEYRYRSVIKacQLEEDISKFAEKDNIVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIK--WVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 90421313 584 KEIFEScVCKLMANKTRILVTSK--MEHLKKADKILILHEG 622
Cdd:PRK11614 174 QQIFDT-IEQLREQGMTIFLVEQnaNQALKLADRGYVLENG 213
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1227-1405 |
1.17e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 51.94 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGvswDSITLQQWRKAFGVIPQKVFI---------F 1296
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIGE---RVITAGKKNKKLKPLRKKVGIvfqfpehqlF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1297 SGTFRK-------NLDPYEQWSDQEIWKVADEVGL-RSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:PRK13634 100 EETVEKdicfgpmNFGVSEEDAKQKAREMIELVGLpEELLARSPFE-----------LSGGQMRRVAIAGVLAMEPEVLV 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 90421313 1369 LDEPSAHLDPVTyqiiRRTLKQAFA------DCTVILCEHRIE 1405
Cdd:PRK13634 169 LDEPTAGLDPKG----RKEMMEMFYklhkekGLTTVLVTHSME 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1210-1423 |
1.33e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.68 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKAFGV 1288
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKvKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1289 I---PQKVFIFSGT-------FRKNLDPYEQWSdQEIWKVADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLAR 1358
Cdd:PRK13648 88 VfqnPDNQFVGSIVkydvafgLENHAVPYDEMH-RRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1359 SVLSKAKILLLDEPSAHLDPVTYQIIRRTLK--QAFADCTVILCEHRIEAMLECQQFLVIEENKVRQ 1423
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1227-1378 |
1.59e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 51.66 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQ----WRKAFGVIPQ--KVFIFSGT 1299
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1300 FRKNLDPYEQ---WSDQEIWKVADE----VGLRsviEQFPGKLDFvlvdggcVLSHGHKQLMCLARSVLSKAKILLLDEP 1372
Cdd:PRK13643 102 VLKDVAFGPQnfgIPKEKAEKIAAEklemVGLA---DEFWEKSPF-------ELSGGQMRRVAIAGILAMEPEVLVLDEP 171
|
....*.
gi 90421313 1373 SAHLDP 1378
Cdd:PRK13643 172 TAGLDP 177
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1211-1403 |
1.60e-06 |
|
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: 50.22 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1211 TVKDLTAKytEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL---RLLNTEGEIQIDGvswDSITlqqwrkafg 1287
Cdd:cd03217 2 EIKDLHVS--VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKG---EDIT--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 vipqkvfifsgtfrkNLDPYE----------QwSDQEIWKVADEVGLRSVIEQFPGkldfvlvdggcvlshGHK------ 1351
Cdd:cd03217 68 ---------------DLPPEErarlgiflafQ-YPPEIPGVKNADFLRYVNEGFSG---------------GEKkrneil 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1352 QLMCLarsvlsKAKILLLDEPSAHLDPVTYQIIRRTLKQ-AFADCTVILCEHR 1403
Cdd:cd03217 117 QLLLL------EPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHY 163
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
450-613 |
1.66e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 49.29 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 450 RGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKhsgrisfcsqfsWIMPGTIKENIIFgvsydeyryrsvikacqleed 529
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------------YIDGEDILEEVLD--------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 530 iskfaEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTR------ILV 603
Cdd:smart00382 48 -----QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSeknltvILT 122
|
170
....*....|
gi 90421313 604 TSKMEHLKKA 613
Cdd:smart00382 123 TNDEKDLGPA 132
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1222-1376 |
1.74e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.48 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQ-QWRKAFGVIPQK------- 1292
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINYNKLDHKlAAQLGIGIIYQElsvidel 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1293 -----VFIFSGTFRKNLD-PYEQWSDQEIWK--VADEVGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKA 1364
Cdd:PRK09700 96 tvlenLYIGRHLTKKVCGvNIIDWREMRVRAamMLLRVGLKVDLDEKVAN-----------LSISHKQMLEIAKTLMLDA 164
|
170
....*....|..
gi 90421313 1365 KILLLDEPSAHL 1376
Cdd:PRK09700 165 KVIIMDEPTSSL 176
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1222-1379 |
1.87e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 52.36 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1222 GGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSWDSITLQQWRKaFGV--IPQKVFIFSG 1298
Cdd:PRK15439 22 SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDsGTLEIGGNPCARLTPAKAHQ-LGIylVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1299 -TFRKNLD---PYEQwsdqeiwkvADEVGLRSVIEQFPGKLDFVLVDGgcVLSHGHKQLMCLARSVLSKAKILLLDEPSA 1374
Cdd:PRK15439 101 lSVKENILfglPKRQ---------ASMQKMKQLLAALGCQLDLDSSAG--SLEVADRQIVEILRGLMRDSRILILDEPTA 169
|
....*
gi 90421313 1375 HLDPV 1379
Cdd:PRK15439 170 SLTPA 174
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
441-580 |
1.96e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLL-MVIMGElEPSEGKIKHSGRisfcsQFSWIMPGTIKE-----NIIFGVSYDE 514
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLArLLTMIE-TPTGGELYYQGQ-----DLLKADPEAQKLlrqkiQIVFQNPYGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 515 YRYRSVIKAcQLEE------DISKFAEKDNI--VLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK11308 105 LNPRKKVGQ-ILEEpllintSLSAAERREKAlaMMAKVGLrpehydryphMFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
....
gi 90421313 577 YLDV 580
Cdd:PRK11308 184 ALDV 187
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1221-1402 |
2.13e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 52.42 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1221 EGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGEIQIDG---VSWDSITLQQWRKA-FGVIPQKVF 1294
Cdd:PRK10535 18 EEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDkpTSGTYRVAGqdvATLDADALAQLRREhFGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1295 IFSG-TFRKNLD-P--YEQWSDQEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCLARSVLSKAKI 1366
Cdd:PRK10535 97 LLSHlTAAQNVEvPavYAGLERKQRLLRAQEllqrLGLEDRVEYQPSQ-----------LSGGQQQRVSIARALMNGGQV 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 90421313 1367 LLLDEPSAHLDPVTYQIIRRTLKQAFADC-TVILCEH 1402
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGhTVIIVTH 202
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
432-575 |
2.65e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.53 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG----------------RISFCSQFS 495
Cdd:PRK11831 14 SFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGenipamsrsrlytvrkRMSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 496 WIMPG-TIKENIIFGVSydeyryrsviKACQLEEDI--SKFAEKDNIVLGEGGIT-----LSGGQRARISLARAVYKDAD 567
Cdd:PRK11831 94 ALFTDmNVFDNVAYPLR----------EHTQLPAPLlhSTVMMKLEAVGLRGAAKlmpseLSGGMARRAALARAIALEPD 163
|
....*...
gi 90421313 568 LYLLDSPF 575
Cdd:PRK11831 164 LIMFDEPF 171
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
440-582 |
3.14e-06 |
|
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: 51.86 E-value: 3.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK--HSGRISFCSQFSWIMPG--TIKENIIFGVSYDEY 515
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEigETVKLAYVDQSRDALDPnkTVWEEISGGLDIIKL 416
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 516 RYRSVikacQLEEDISKF----AEKDNIVlGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:TIGR03719 417 GKREI----PSRAYVGRFnfkgSDQQKKV-GQ----LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET 478
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1224-1384 |
3.29e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.47 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1224 NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGEIQIDGVswdSIT-LQQWRKAFGVIpqKVF--IFSGT 1299
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAgSLPPDSGSILIDGK---DVTkLPEYKRAKYIG--RVFqdPMMGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1300 ---------------------FRKNLDPYEQWSDQEIWKV---------ADEVGLrsvieqfpgkldfvlvdggcvLSHG 1349
Cdd:COG1101 94 apsmtieenlalayrrgkrrgLRRGLTKKRRELFRELLATlglglenrlDTKVGL---------------------LSGG 152
|
170 180 190
....*....|....*....|....*....|....*
gi 90421313 1350 HKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQII 1384
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALV 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1226-1402 |
3.69e-06 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 51.59 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1226 ILENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRLLNTE--GEIQIDGVswdSITLQQWRKAFGVIPQ-KVFI----- 1295
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNalAFRSPKGVKgsGSVLLNGM---PIDAKEMRAISAYVQQdDLFIptltv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1296 -----FSGTFRKNLDPYEQWSDQEIWKVADEVGLRS---VIEQFPGKLDfvlvdggcVLSHGHKQLMCLARSVLSKAKIL 1367
Cdd:TIGR00955 117 rehlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcanTRIGVPGRVK--------GLSGGERKRLAFASELLTDPPLL 188
|
170 180 190
....*....|....*....|....*....|....*.
gi 90421313 1368 LLDEPSAHLDPVT-YQIIRRTLKQAFADCTVILCEH 1402
Cdd:TIGR00955 189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIH 224
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
121-300 |
4.18e-06 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 50.11 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 121 IYLGIGLCLLFIVRTLLLHPAIFGLHHIG----MQMRIAMFsliyKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGL- 195
Cdd:cd18552 39 LLVPLAIIGLFLLRGLASYLQTYLMAYVGqrvvRDLRNDLF----DKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALt 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 196 -ALAHFVwIAPLQVALLMGLI----WELlqasAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQ 270
Cdd:cd18552 115 sALTVLV-RDPLTVIGLLGVLfyldWKL----TLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIR 189
|
170 180 190
....*....|....*....|....*....|....
gi 90421313 271 SVKAYCWEEAM----EKMIENLRQTELKLTRKAA 300
Cdd:cd18552 190 VVKAFGAEDYEikrfRKANERLRRLSMKIARARA 223
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1210-1271 |
4.21e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.92 E-value: 4.21e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAF-LRLLNTEGEIQIDG 1271
Cdd:PRK11701 7 LSVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYRM 67
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1210-1402 |
5.48e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 5.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTEG----GNAiLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDSIT-- 1278
Cdd:PRK13649 3 INLQNVSYTYQAGtpfeGRA-LFDVNLTIEDGSYTAFIGHTGSGKSTI----MQLLNglhvpTQGSVRVDDTLITSTSkn 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1279 --LQQWRKAFGVIPQ--KVFIFSGTFRKNLDPYEQ---WSDQEIWKVADE-VGLRSVIEQFPGKLDFvlvdggcVLSHGH 1350
Cdd:PRK13649 78 kdIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQnfgVSQEEAEALAREkLALVGISESLFEKNPF-------ELSGGQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1351 KQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFAD-CTVILCEH 1402
Cdd:PRK13649 151 MRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTH 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1210-1376 |
5.72e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.70 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRLLNTEGEIQIDG--VSWDSITLQQwRK 1284
Cdd:PRK13549 6 LEMKNITKTF--GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTYEGEIIFEGeeLQASNIRDTE-RA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1285 AFGVIPQKVfifsgTFRKNLdpyeqwsdqeiwKVADEVGLRSVIEQFpGKLDFVLVDGGCV------------------L 1346
Cdd:PRK13549 83 GIAIIHQEL-----ALVKEL------------SVLENIFLGNEITPG-GIMDYDAMYLRAQkllaqlkldinpatpvgnL 144
|
170 180 190
....*....|....*....|....*....|
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEPSAHL 1376
Cdd:PRK13549 145 GLGQQQLVEIAKALNKQARLLILDEPTASL 174
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
441-645 |
8.88e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 49.32 E-value: 8.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR---------------ISFCSQFSWIMPGTIKEN 505
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkigMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 506 IIFGVSYDEYRYRSVIKACQ---LEEDISKFAEKDNIvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDealLAVNMLDFKTREPA-------RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 583 EKEIFEscVCKLMANK---TRILVTSKMEHLKKADKILILHEGS-------SYFYGTFSELQNLQPD--FSSKLM 645
Cdd:PRK13642 176 RQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEiikeaapSELFATSEDMVEIGLDvpFSSNLM 248
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
433-580 |
9.82e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDinfkierGQLLAVAGSTGAGKTSLLMVIMGELEP------------------------------SEGKI 482
Cdd:PRK13409 88 FKLYGLPIPKE-------GKVTGILGPNGIGKTTAVKILSGELIPnlgdyeeepswdevlkrfrgtelqnyfkklYNGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 483 KHSGRISFCSQFSWIMPGTIKENIIfgvSYDEY-RYRSVIKACQLEE----DISkfaekdnivlgeggiTLSGGQRARIS 557
Cdd:PRK13409 161 KVVHKPQYVDLIPKVFKGKVRELLK---KVDERgKLDEVVERLGLENildrDIS---------------ELSGGELQRVA 222
|
170 180
....*....|....*....|...
gi 90421313 558 LARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK13409 223 IAAALLRDADFYFFDEPTSYLDI 245
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
433-580 |
1.09e-05 |
|
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: 48.52 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKDinfkierGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKikhsgrisFCSQFSW--IMP---GTIKENII 507
Cdd:cd03236 15 FKLHRLPVPRE-------GQVLGLVGPNGIGKSTALKILAGKLKPNLGK--------FDDPPDWdeILDefrGSELQNYF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 508 FGVSYDEYR------YRSVI------KACQLEEDISKFAEKDNIV--LGEGGI------TLSGGQRARISLARAVYKDAD 567
Cdd:cd03236 80 TKLLEGDVKvivkpqYVDLIpkavkgKVGELLKKKDERGKLDELVdqLELRHVldrnidQLSGGELQRVAIAAALARDAD 159
|
170
....*....|...
gi 90421313 568 LYLLDSPFGYLDV 580
Cdd:cd03236 160 FYFFDEPSSYLDI 172
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
86-297 |
1.09e-05 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 48.95 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 86 IFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIY----LGIGLC---LLFIVRTLLLHPAifglHHIGMQMRIAMFS 158
Cdd:cd18541 6 LFLILVDLLQLLIPRIIGRAIDALTAGTLTASQLLRYalliLLLALLigiFRFLWRYLIFGAS----RRIEYDLRNDLFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 159 liykKTLKLSSRVLDKISIGQLVSLLSNNLNKFDE--GLALAHFV--WIAPLQVALLMGLI-WELlqasAFCGLGFLIVL 233
Cdd:cd18541 82 ----HLLTLSPSFYQKNRTGDLMARATNDLNAVRMalGPGILYLVdaLFLGVLVLVMMFTIsPKL----TLIALLPLPLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90421313 234 ALFQAGLGRMMMK-YRD-QRA-GKISERlviTSEMIENIQSVKAYCWEEAM----EKMIENLRQTELKLTR 297
Cdd:cd18541 154 ALLVYRLGKKIHKrFRKvQEAfSDLSDR---VQESFSGIRVIKAFVQEEAEierfDKLNEEYVEKNLRLAR 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
434-622 |
1.26e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 434 SLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-ISFCSQfswimpgtiKENIIFGVSY 512
Cdd:PRK10982 7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFKSS---------KEALENGISM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 513 -----DEYRYRSVIKACQL----------------EEDISKFAEKD-NIVLGEGGITLSGGQRARISLARAVYKDADLYL 570
Cdd:PRK10982 78 vhqelNLVLQRSVMDNMWLgryptkgmfvdqdkmyRDTKAIFDELDiDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 90421313 571 LDSPfgyLDVLTEKEI--FESCVCKLMANKTRILVTS-KMEHLKK-ADKILILHEG 622
Cdd:PRK10982 158 MDEP---TSSLTEKEVnhLFTIIRKLKERGCGIVYIShKMEEIFQlCDEITILRDG 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
437-623 |
1.56e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.59 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTP----VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR-ISFCSQFSWIMPGTIKENIIFGVS 511
Cdd:PRK13649 15 GTPfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlITSTSKNKDIKQIRKKVGLVFQFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 512 YDEYRYRSVIKACQL--------EEDISKFA-EKDNIVlgegGIT----------LSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK13649 95 ESQLFEETVLKDVAFgpqnfgvsQEEAEALArEKLALV----GISeslfeknpfeLSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 573 SPFGYLDVLTEKE---IFESCVCKLMankTRILVTSKMEHLKK-ADKILILHEGS 623
Cdd:PRK13649 171 EPTAGLDPKGRKElmtLFKKLHQSGM---TIVLVTHLMDDVANyADFVYVLEKGK 222
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
437-580 |
2.02e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 48.87 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGR--------------ISF---------Csq 493
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEditglsprerrrlgVAYipedrlgrgL-- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 494 fswIMPGTIKENIIFGvSYDEYRY-------RSVIKAcQLEEDISKFaekdNIVLgeGGI-----TLSGG--QRArIsLA 559
Cdd:COG3845 348 ---VPDMSVAENLILG-RYRRPPFsrggfldRKAIRA-FAEELIEEF----DVRT--PGPdtparSLSGGnqQKV-I-LA 414
|
170 180
....*....|....*....|..
gi 90421313 560 RAVYKDADLYLLDSP-FGyLDV 580
Cdd:COG3845 415 RELSRDPKLLIAAQPtRG-LDV 435
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1219-1388 |
2.07e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.15 E-value: 2.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1219 YTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GEIQIDGVSWDSITLQQWRKAFGVIPqkvfifs 1297
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKTATRGDRSRFMAYLGHLP------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1298 gTFRKNLDPYEQwsdqeIWKVADEVGLRSviEQFPGK-LDFVLVDGGC-----VLSHGHKQLMCLARSVLSKAKILLLDE 1371
Cdd:PRK13543 92 -GLKADLSTLEN-----LHFLCGLHGRRA--KQMPGSaLAIVGLAGYEdtlvrQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
170
....*....|....*..
gi 90421313 1372 PSAHLDPVTYQIIRRTL 1388
Cdd:PRK13543 164 PYANLDLEGITLVNRMI 180
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1226-1377 |
3.00e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1226 ILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLL-----NTEGEIQI-DGVSwdsitlqqwrkaFGVIPQ-------K 1292
Cdd:PRK11819 22 ILKDISLSFFPGAKIGVLGLNGAGKSTL----LRIMagvdkEFEGEARPaPGIK------------VGYLPQepqldpeK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1293 vfifsgTFRKN-----------LDPYEQWS------DQEIWKVADEVG-------------LRSVIEQF-------PGKL 1335
Cdd:PRK11819 86 ------TVRENveegvaevkaaLDRFNEIYaayaepDADFDALAAEQGelqeiidaadawdLDSQLEIAmdalrcpPWDA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 90421313 1336 DfvlVDggcVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:PRK11819 160 K---VT---KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1227-1449 |
3.33e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 3.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1227 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE------GEIQIDGVSWDSITLQQWRKAFGVIPQ--KVFIFSG 1298
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1299 TFRKNL--DPYEQWSD-QEIWK-VADEVGLRSVIEQFPGKLDFVLvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSA 1374
Cdd:PRK13645 107 TIEKDIafGPVNLGENkQEAYKkVPELLKLVQLPEDYVKRSPFEL-------SGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1375 HLDPVTYQ----IIRRTLKQAFAdcTVILCEHRIEAMLE-CQQFLVIEENKVRQYDS-IQKLLNERSLFRQAISPSDRVK 1448
Cdd:PRK13645 180 GLDPKGEEdfinLFERLNKEYKK--RIIMVTHNMDQVLRiADEVIVMHEGKVISIGSpFEIFSNQELLTKIEIDPPKLYQ 257
|
.
gi 90421313 1449 L 1449
Cdd:PRK13645 258 L 258
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
441-586 |
3.59e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.14 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGeLEPSEGKIKHSGR------------------ISFCSQFSWIMPG-T 501
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdldglsrralrplrrrmqVVFQDPFGSLSPRmT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 502 IKEnII--------FGVSYDEyRYRSVIKAcqLEE------DISKF-AEkdnivlgeggitLSGGQRARISLARAVYKDA 566
Cdd:COG4172 381 VGQ-IIaeglrvhgPGLSAAE-RRARVAEA--LEEvgldpaARHRYpHE------------FSGGQRQRIAIARALILEP 444
|
170 180
....*....|....*....|
gi 90421313 567 DLYLLDSPFGYLDVLTEKEI 586
Cdd:COG4172 445 KLLVLDEPTSALDVSVQAQI 464
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
437-579 |
3.80e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGeLEP-SEGKIKHSGR-----------ISFCSQFSWIMPG-TIK 503
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERiTSGEIWIGGRvvnelepadrdIAMVFQNYALYPHmSVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 504 ENI-----IFGVSYDEYRYRsVIKACQLEEdISKFAE-KDNivlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK11650 95 ENMayglkIRGMPKAEIEER-VAEAARILE-LEPLLDrKPR--------ELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
..
gi 90421313 578 LD 579
Cdd:PRK11650 165 LD 166
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1214-1377 |
3.93e-05 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 46.73 E-value: 3.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1214 DLTAKYTEGG--NAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDGVSWDsiTLQQWRKAF 1286
Cdd:PRK11629 10 NLCKRYQEGSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTL----LHLLGgldtpTSGDVIFNGQPMS--KLSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1287 GVIPQKVFIFSgtFRKNLDPYEQWSD------------QEIWKVADE----VGLRSVIEQFPGKldfvlvdggcvLSHGH 1350
Cdd:PRK11629 84 LRNQKLGFIYQ--FHHLLPDFTALENvamplligkkkpAEINSRALEmlaaVGLEHRANHRPSE-----------LSGGE 150
|
170 180
....*....|....*....|....*..
gi 90421313 1351 KQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1215-1399 |
5.82e-05 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 45.72 E-value: 5.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1215 LTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFlrLLNTEGEIQIDG-VSWDSITLqqwrKAFGVIPQKV 1293
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL--ANRTEGNVSVEGdIHYNGIPY----KEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1294 FIFSGtfrknldpyeqwsdQEIWKVAdEVGLRSVIEqFPGKL---DFVLvdggcVLSHGHKQLMCLARSVLSKAKILLLD 1370
Cdd:cd03233 85 IIYVS--------------EEDVHFP-TLTVRETLD-FALRCkgnEFVR-----GISGGERKRVSIAEALVSRASVLCWD 143
|
170 180 190
....*....|....*....|....*....|...
gi 90421313 1371 EPSAHLDPVT----YQIIRRTLKQAFADCTVIL 1399
Cdd:cd03233 144 NSTRGLDSSTaleiLKCIRTMADVLKTTTFVSL 176
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
79-302 |
6.13e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 46.68 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 79 WRFMFYGIFLYLgeVTKAVQPL---LLGRIIAS-YDPDNKEERSIA-----IYLGIGLCLLFIvrTLLLHpAIFGL--HH 147
Cdd:cd18578 8 WPLLLLGLIGAI--IAGAVFPVfaiLFSKLISVfSLPDDDELRSEAnfwalMFLVLAIVAGIA--YFLQG-YLFGIagER 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 148 IGMQMRIAMFSLIykktlkLSSRV----LDKISIGQLVSLLSNNLNKFDE--GLALAHFVWIAplqVALLMGLI------ 215
Cdd:cd18578 83 LTRRLRKLAFRAI------LRQDIawfdDPENSTGALTSRLSTDASDVRGlvGDRLGLILQAI---VTLVAGLIiafvyg 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 216 WELlqasAFCGLGFLIVLALFQAGLGRMMMKY--RDQRAGKISERlvITSEMIENIQSVKAYCWEEAMEKMIENLRQTEL 293
Cdd:cd18578 154 WKL----ALVGLATVPLLLLAGYLRMRLLSGFeeKNKKAYEESSK--IASEAVSNIRTVASLTLEDYFLEKYEEALEEPL 227
|
....*....
gi 90421313 294 KLTRKAAYV 302
Cdd:cd18578 228 KKGLRRALI 236
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1213-1388 |
6.18e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1213 KDLTAKYTEGGNAiLENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGEIQIDGVSWDSITLQQWRKAFG 1287
Cdd:PRK10522 326 RNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKST----LAMLLTglyqpQSGEILLDGKPVTAEQPEDYRKLFS 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1288 VIPQKVFIFSgtfrKNLDPYEQWSDQEI---WkvADEVGLRSvieqfpgKLDFvlvDGGCV----LSHGHKQLMCLARSV 1360
Cdd:PRK10522 401 AVFTDFHLFD----QLLGPEGKPANPALvekW--LERLKMAH-------KLEL---EDGRIsnlkLSKGQKKRLALLLAL 464
|
170 180
....*....|....*....|....*...
gi 90421313 1361 LSKAKILLLDEPSAHLDPVTYQIIRRTL 1388
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVL 492
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1236-1402 |
6.37e-05 |
|
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: 46.21 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1236 PGQRVGLLGRTGSGKSTLLsaflRLLNTE-----GEIQiDGVSWDSItLQQWRkafGVIPQKVF--IFSGTFRKNLDPye 1308
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTAL----KILAGKlkpnlGKFD-DPPDWDEI-LDEFR---GSELQNYFtkLLEGDVKVIVKP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1309 QWSDQ----------EIWKVADEVG-LRSVIEQFpgKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:cd03236 94 QYVDLipkavkgkvgELLKKKDERGkLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
170 180 190
....*....|....*....|....*....|.
gi 90421313 1378 pvTYQ------IIRRTLKQAFAdctVILCEH 1402
Cdd:cd03236 172 --IKQrlnaarLIRELAEDDNY---VLVVEH 197
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
433-580 |
8.60e-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: 47.09 E-value: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 433 FSLLGTPVLKdinfkieRGQLLAVAGSTGAGKTSLLMVIMGELEP------------------------------SEGKI 482
Cdd:COG1245 88 FRLYGLPVPK-------KGKVTGILGPNGIGKSTALKILSGELKPnlgdydeepswdevlkrfrgtelqdyfkklANGEI 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 483 KHSGRISFCSQFSWIMPGTIKENIifgVSYDEY-RYRSVIKACQLEE----DISkfaekdnivlgeggiTLSGGQRARIS 557
Cdd:COG1245 161 KVAHKPQYVDLIPKVFKGTVRELL---EKVDERgKLDELAEKLGLENildrDIS---------------ELSGGELQRVA 222
|
170 180
....*....|....*....|...
gi 90421313 558 LARAVYKDADLYLLDSPFGYLDV 580
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLDI 245
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1219-1427 |
8.86e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.91 E-value: 8.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1219 YTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTE-----GEIQIDGVSWDSIT---LQQWRKAFGVIP 1290
Cdd:PRK11831 15 FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTL----LRLIGGQiapdhGEILFDGENIPAMSrsrLYTVRKRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1291 QkvfifSGTFRKNLDPYEQ--WSDQEIWKVADE------------VGLRSVIEQFPGKldfvlvdggcvLSHGHKQLMCL 1356
Cdd:PRK11831 91 Q-----SGALFTDMNVFDNvaYPLREHTQLPAPllhstvmmkleaVGLRGAAKLMPSE-----------LSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1357 ARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQ--------------------AFADCTVILCEHRIEAMLECQQFLVI 1416
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnsalgvtcvvvshdvpevlSIADHAYIVADKKIVAHGSAQALQAN 234
|
250
....*....|..
gi 90421313 1417 EENKVRQY-DSI 1427
Cdd:PRK11831 235 PDPRVRQFlDGI 246
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
440-579 |
9.49e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.15 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPS--EGKIKHSG---------RIS-FCSQFSWIMPG-TIKENI 506
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGfpkkqetfaRISgYCEQNDIHSPQvTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 507 IFG--------VSYDEyRYRSVIKACQLEEDISKfaeKDNIVlGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PLN03140 975 IYSaflrlpkeVSKEE-KMMFVDEVMELVELDNL---KDAIV-GLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
..
gi 90421313 578 LD 579
Cdd:PLN03140 1050 LD 1051
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
438-482 |
1.05e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 46.22 E-value: 1.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGeLE-PSEGKI 482
Cdd:COG1135 18 VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LErPTSGSV 62
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
432-622 |
1.06e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 432 NFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK-HSGRISFCSQFSWIMPGtikeniiFGV 510
Cdd:PRK10982 255 NLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlHGKKINNHNANEAINHG-------FAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 511 SYDEYR-----------YRSVIKacQLEEDISKFAEKDNI--------------VLGEGGIT----LSGGQRARISLARA 561
Cdd:PRK10982 328 VTEERRstgiyayldigFNSLIS--NIRNYKNKVGLLDNSrmksdtqwvidsmrVKTPGHRTqigsLSGGNQQKVIIGRW 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90421313 562 VYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKM-EHLKKADKILILHEG 622
Cdd:PRK10982 406 LLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNG 467
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
440-622 |
1.12e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 440 VLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGElepSEGKiKHSGRIsfcsqfswIMPG------TIKENIIFGVSY- 512
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGR-NISGTV--------FKDGkevdvsTVSDAIDAGLAYv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 513 --DEYRYRSVikacqLEEDIskfaeKDNIVLG------EGGI-----------------------------TLSGGQRAR 555
Cdd:NF040905 343 teDRKGYGLN-----LIDDI-----KRNITLAnlgkvsRRGVideneeikvaeeyrkkmniktpsvfqkvgNLSGGNQQK 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 556 ISLARAVYKDADLYLLDSPFGYLDVLTEKEIFesCVCKLMAN--KTRILVTSKM-EHLKKADKILILHEG 622
Cdd:NF040905 413 VVLSKWLFTDPDVLILDEPTRGIDVGAKYEIY--TIINELAAegKGVIVISSELpELLGMCDRIYVMNEG 480
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
442-582 |
1.60e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 442 KDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK--HSGRISFCSQFSWIMPG--TIKENIIFGVSYdeyry 517
Cdd:PRK11819 341 DDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKigETVKLAYVDQSRDALDPnkTVWEEISGGLDI----- 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 518 rsvIKACQLEED----ISKFAEKdnivlgeGGI------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:PRK11819 416 ---IKVGNREIPsrayVGRFNFK-------GGDqqkkvgVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1210-1400 |
1.61e-04 |
|
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: 44.16 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTakYTEGGNA----ILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-------TEGEIQIDGvswdsit 1278
Cdd:cd03232 4 LTWKNLN--YTVPVKGgkrqLLNNISGYVKPGTLTALMGESGAGKTTL----LDVLAgrktagvITGEILING------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1279 lQQWRKAF----GVIPQK-VFIFSGTFRKNLdpyeqwsdqeiwkvadevglrsvieQFPGKLDfvlvdggcVLSHGHKQL 1353
Cdd:cd03232 71 -RPLDKNFqrstGYVEQQdVHSPNLTVREAL-------------------------RFSALLR--------GLSVEQRKR 116
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 90421313 1354 MCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILC 1400
Cdd:cd03232 117 LTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILC 163
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
951-1083 |
1.82e-04 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 45.24 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 951 KMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLR 1030
Cdd:cd18557 74 DLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIAS 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 1031 AYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALN 1083
Cdd:cd18557 154 KIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALD 206
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
951-1120 |
1.86e-04 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 45.11 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 951 KMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPY---IFVATVPVIVAFI 1027
Cdd:cd18552 77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKltlIALVVLPLAALPI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1028 M-----LRAYFLQTSQQLKQLesegrspifTHLVT-SLKGLWTLRAFGRQPYFETLFHKALNlhtanwflylsTLRWFQM 1101
Cdd:cd18552 157 RrigkrLRKISRRSQESMGDL---------TSVLQeTLSGIRVVKAFGAEDYEIKRFRKANE-----------RLRRLSM 216
|
170 180
....*....|....*....|....*
gi 90421313 1102 RIEMI------FVIFFIAVTFISIL 1120
Cdd:cd18552 217 KIARAralsspLMELLGAIAIALVL 241
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
441-482 |
2.01e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.18 E-value: 2.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKI 482
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
441-572 |
2.12e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSG-------RISFCSQFS------WIMPGTIKENii 507
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGkpvtaeqPEDYRKLFSavftdfHLFDQLLGPE-- 416
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 508 fGVSYDEYRYRSVIKACQLEEdisKFAEKDNIVLGeggITLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK10522 417 -GKPANPALVEKWLERLKMAH---KLELEDGRISN---LKLSKGQKKRLALLLALAEERDILLLD 474
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
875-1140 |
2.12e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 45.16 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 875 AASLVVLWLLGNtpLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVAdtLLAMGFFRGLPLVHTLITVSKILHHKMLH 954
Cdd:cd18577 13 AALPLMTIVFGD--LFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIG--SFVLSYIQTACWTITGERQARRIRKRYLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 955 SVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPY---IFVATVPVIVAFIMLRA 1031
Cdd:cd18577 89 ALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKltlVLLATLPLIAIVGGIMG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1032 YFLQTSQQlKQLESEGR-SPIFTHLVTSLKglwTLRAFGRQPYFETLFHKALNlHTANWFLYLSTLRWFQMRIEMIFVIF 1110
Cdd:cd18577 169 KLLSKYTK-KEQEAYAKaGSIAEEALSSIR---TVKAFGGEEKEIKRYSKALE-KARKAGIKKGLVSGLGLGLLFFIIFA 243
|
250 260 270
....*....|....*....|....*....|..
gi 90421313 1111 FIAVTFI--SILTTgEGEGRVGIILTLAMNIM 1140
Cdd:cd18577 244 MYALAFWygSRLVR-DGEISPGDVLTVFFAVL 274
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
99-301 |
2.31e-04 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 44.75 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 99 PLLLGRIIASYDPdNKEERSIaIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIG 178
Cdd:cd18549 22 PLIVRYIIDDLLP-SKNLRLI-LIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLSFSFFDNNKTG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 179 QLVSLLSNNLNKFDEglaLAH------FVWIAPLQVAL-LMGLIWELLQASAFCGLGFLIVLALFQAglGRMMMKYRDQR 251
Cdd:cd18549 100 QLMSRITNDLFDISE---LAHhgpedlFISIITIIGSFiILLTINVPLTLIVFALLPLMIIFTIYFN--KKMKKAFRRVR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 252 AgKISErlvITSEmIEN----IQSVKAYCWEE-AMEKMIENLRqtELKLTRKAAY 301
Cdd:cd18549 175 E-KIGE---INAQ-LEDslsgIRVVKAFANEEyEIEKFDEGND--RFLESKKKAY 222
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
960-1120 |
2.86e-04 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 44.40 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 960 PMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQP---YIFVATVPVIVAFIMLRAYFLQ- 1035
Cdd:cd18576 83 PLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLLMLATVPVVVLVAVLFGRRIRk 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1036 --TSQQLKQLESegrspiFTHLVTSLKGLWTLRAFGRQPYFETLFHKALN--LHTAnwfLYLSTLR-WFqmrieMIFVIF 1110
Cdd:cd18576 163 lsKKVQDELAEA------NTIVEETLQGIRVVKAFTREDYEIERYRKALErvVKLA---LKRARIRaLF-----SSFIIF 228
|
170
....*....|
gi 90421313 1111 FIAVTFISIL 1120
Cdd:cd18576 229 LLFGAIVAVL 238
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
950-1029 |
2.91e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 44.73 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 950 HKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIF---VATVPVIVAF 1026
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTlvtLAVVPLAFLI 152
|
...
gi 90421313 1027 IML 1029
Cdd:cd18551 153 ILP 155
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1236-1402 |
3.01e-04 |
|
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: 45.16 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1236 PGQRVGLLGRTGSGKST---LLSAFLR--LLNTEGEiqidgVSWDSI-------TLQQWRKAF--GVI-----PQKV-FI 1295
Cdd:COG1245 98 KGKVTGILGPNGIGKSTalkILSGELKpnLGDYDEE-----PSWDEVlkrfrgtELQDYFKKLanGEIkvahkPQYVdLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1296 ---FSGTFRknldpyeqwsdqEIWKVADEVG-LRSVIEQFpgKLDFVL---VDggcVLSHGHKQLMCLARSVLSKAKILL 1368
Cdd:COG1245 173 pkvFKGTVR------------ELLEKVDERGkLDELAEKL--GLENILdrdIS---ELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 90421313 1369 LDEPSAHLDpvTYQ------IIRRTLKqafADCTVILCEH 1402
Cdd:COG1245 236 FDEPSSYLD--IYQrlnvarLIRELAE---EGKYVLVVEH 270
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
928-1124 |
3.34e-04 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 44.36 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 928 AMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSkDIAILDDLLPLTIFD-FIQLLLIVIGAIa 1006
Cdd:cd18570 57 LLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISlFLDLLMVIISGI- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1007 VVAVLQPYIF---VATVPV-IVAFIMLRAYFLQTSQQLKQLESEGRSpiftHLVTSLKGLWTLRAFGRQPYF----ETLF 1078
Cdd:cd18570 135 ILFFYNWKLFlitLLIIPLyILIILLFNKPFKKKNREVMESNAELNS----YLIESLKGIETIKSLNAEEQFlkkiEKKF 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 90421313 1079 HKALN--LHTANWFLYLSTLRWFqmrIEMIFVIFFIAVTFISI----LTTGE 1124
Cdd:cd18570 211 SKLLKksFKLGKLSNLQSSIKGL---ISLIGSLLILWIGSYLVikgqLSLGQ 259
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
97-302 |
3.72e-04 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 44.35 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 97 VQPLLLGRIIasydpDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMriaMFSL---IYKKTLKLSSRVLD 173
Cdd:cd18551 17 AQPLLVKNLI-----DALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERV---VLDLrrrLWRRLLRLPVSFFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 174 KISIGQLVSLLSNNLNKFDEGLA--LAHFVwIAPLQVA---LLMGLI-WELLQASAFC-GLGFLIVLAlfqagLGRMMMK 246
Cdd:cd18551 89 RRRSGDLVSRVTNDTTLLRELITsgLPQLV-TGVLTVVgavVLMFLLdWVLTLVTLAVvPLAFLIILP-----LGRRIRK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 247 Y--RDQRA-GKISERLvitSEMIENIQSVKAYCWE----EAMEKMIENLRQTELKLTRKAAYV 302
Cdd:cd18551 163 AskRAQDAlGELSAAL---ERALSAIRTVKASNAEeretKRGGEAAERLYRAGLKAAKIEALI 222
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
451-597 |
4.30e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.10 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 451 GQLLAVAGSTGAGKTSLLMVIMGELEP---SEGKIKHSGR---------ISFCSQFSWIMP-GTIKENIIFG-------- 509
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRpldssfqrsIGYVQQQDLHLPtSTVRESLRFSaylrqpks 868
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 510 VS-YDEYRY-RSVIKACQLEEdiskFAEKdniVLGEGGITLSGGQRARISLA-RAVYKDADLYLLDSPFGYLDVLTEKEI 586
Cdd:TIGR00956 869 VSkSEKMEYvEEVIKLLEMES----YADA---VVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTSGLDSQTAWSI 941
|
170
....*....|.
gi 90421313 587 fescvCKLMAN 597
Cdd:TIGR00956 942 -----CKLMRK 947
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
441-640 |
5.33e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSqfswIMPG-----TIKENIIFGVSYDEY 515
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA----ISAGlsgqlTGIENIEFKMLCMGF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 516 RyRSVIKacQLEEDISKFAEkdnivLGE----GGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD-VLTEKeifesC 590
Cdd:PRK13546 116 K-RKEIK--AMTPKIIEFSE-----LGEfiyqPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDqTFAQK-----C 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 90421313 591 VCKLM----ANKTRILVTSKMEHLKK-ADKILILHEGssyFYGTFSELQNLQPDF 640
Cdd:PRK13546 183 LDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGG---KLKDYGELDDVLPKY 234
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
547-580 |
6.25e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.47 E-value: 6.25e-04
10 20 30
....*....|....*....|....*....|....
gi 90421313 547 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1220-1371 |
7.71e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.97 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1220 TEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLnteGEIqidgvsW----DSITLQQWRKAFgVIPQKVFI 1295
Cdd:TIGR00954 461 TPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLF----RIL---GEL------WpvygGRLTKPAKGKLF-YVPQRPYM 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1296 FSGTFRKNL---DPYEQ-----WSDQEIWKVADEVGLRSVIEQfPGKLDFVlVDGGCVLSHGHKQLMCLARSVLSKAKIL 1367
Cdd:TIGR00954 527 TLGTLRDQIiypDSSEDmkrrgLSDKDLEQILDNVQLTHILER-EGGWSAV-QDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
....
gi 90421313 1368 LLDE 1371
Cdd:TIGR00954 605 ILDE 608
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
437-586 |
9.18e-04 |
|
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: 43.66 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIM---------GELEPSEGKIKHSG-------RISFCSQFSWIMPG 500
Cdd:TIGR02633 13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSgvyphgtwdGEIYWSGSPLKASNirdteraGIVIIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 501 -TIKENIIFG--VSYDEYR--YRSVIKACQ-LEEDISKFAEKDNIVLGEGGitlsGGQRARISLARAVYKDADLYLLDSP 574
Cdd:TIGR02633 93 lSVAENIFLGneITLPGGRmaYNAMYLRAKnLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170
....*....|..
gi 90421313 575 FGyldVLTEKEI 586
Cdd:TIGR02633 169 SS---SLTEKET 177
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-622 |
1.16e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.78 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 437 GTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMViMGELEPSEGKIKHSG--------------------RISFCSQFSW 496
Cdd:PRK14271 33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRT-LNRMNDKVSGYRYSGdvllggrsifnyrdvlefrrRVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 497 IMPGTIKENIIFGVSYDEY----RYRSVIKAcQLEEDISKFAEKDNivLGEGGITLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLvprkEFRGVAQA-RLTEVGLWDAVKDR--LSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 90421313 573 SPFGYLDVLTEKEIfESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 622
Cdd:PRK14271 189 EPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDG 238
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1210-1372 |
1.34e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 43.08 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1210 MTVKDLTAKYTeggnaiLENISFSISPGQRVGLLGRTGSGKSTLLSA-FLRLLNTEGEIQIDGVSWDSITLQQW------ 1282
Cdd:COG1129 257 LEVEGLSVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARAlFGADPADSGEIRLDGKPVRIRSPRDAiragia 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1283 -----RKAFGVIPQKvfifsgTFRKN-----LDPYEQW---SDQEIWKVADEvglrsVIEQF---PGKLDfVLVDGgcvL 1346
Cdd:COG1129 331 yvpedRKGEGLVLDL------SIRENitlasLDRLSRGgllDRRRERALAEE-----YIKRLrikTPSPE-QPVGN---L 395
|
170 180
....*....|....*....|....*.
gi 90421313 1347 SHGHKQLMCLARSVLSKAKILLLDEP 1372
Cdd:COG1129 396 SGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
438-604 |
1.38e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 42.32 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGelEPS----EGKIKHSGRiSFCSqfswIMPGTIKENIIF----- 508
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGE-SILD----LEPEERAHLGIFlafqy 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 509 -----GVSYDEY---RYRSVIKACQLEE-DISKF----AEKDNIV----------LGEGgitLSGGQRARISLARAVYKD 565
Cdd:CHL00131 93 pieipGVSNADFlrlAYNSKRKFQGLPElDPLEFleiiNEKLKLVgmdpsflsrnVNEG---FSGGEKKRNEILQMALLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 90421313 566 ADLYLLDSPFGYLDVLTEKEIFEScVCKLM-ANKTRILVT 604
Cdd:CHL00131 170 SELAILDETDSGLDIDALKIIAEG-INKLMtSENSIILIT 208
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1207-1377 |
1.61e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 42.94 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1207 GGQMTVKDLTAKYTEggNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFlrllntEGEIQIDGVSWDSIT-----LQQ 1281
Cdd:PLN03211 66 GHKPKISDETRQIQE--RTILNGVTGMASPGEILAVLGPSGSGKSTLLNAL------AGRIQGNNFTGTILAnnrkpTKQ 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1282 WRKAFGVIPQ-----------KVFIFSGTFR--KNLDPYEQWSDQEiwKVADEVGLRSVIEQFPGKldfVLVDGgcvLSH 1348
Cdd:PLN03211 138 ILKRTGFVTQddilyphltvrETLVFCSLLRlpKSLTKQEKILVAE--SVISELGLTKCENTIIGN---SFIRG---ISG 209
|
170 180
....*....|....*....|....*....
gi 90421313 1349 GHKQLMCLARSVLSKAKILLLDEPSAHLD 1377
Cdd:PLN03211 210 GERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1212-1255 |
1.61e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.19 E-value: 1.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQRVGLLGRTGSGKSTLLS 1255
Cdd:NF033858 4 LEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLS 45
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
441-508 |
1.97e-03 |
|
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: 41.07 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPS--EGKIKHSGR---------ISFCSQFSWIMPG-TIKENIIF 508
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRpldknfqrsTGYVEQQDVHSPNlTVREALRF 102
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
441-622 |
2.32e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.70 E-value: 2.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 441 LKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIK------HSGRISFCSQfswimpgtiKENIIFGVSYDE 514
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplHFGDYSYRSQ---------RIRMIFQDPSTS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 515 YRYRSVIKAC-----QLEEDISKFAEKDNIV--LGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK15112 100 LNPRQRISQIldfplRLNTDLEPEQREKQIIetLRQVGLlpdhasyyphMLAPGQKQRLGLARALILRPKVIIADEALAS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 90421313 578 LDVLTEKEIFeSCVCKLMANK--TRILVTSK---MEHLkkADKILILHEG 622
Cdd:PRK15112 180 LDMSMRSQLI-NLMLELQEKQgiSYIYVTQHlgmMKHI--SDQVLVMHQG 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1212-1290 |
3.30e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 41.94 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKyTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGEIQIDGVSWDSITLQQWRKA-FGVI 1289
Cdd:COG3845 260 VENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPpASGSIRLDGEDITGLSPRERRRLgVAYI 338
|
.
gi 90421313 1290 P 1290
Cdd:COG3845 339 P 339
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
438-490 |
4.21e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 41.59 E-value: 4.21e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 90421313 438 TPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIkhSGRISF 490
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAAHP--SGSILF 73
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
86-300 |
4.88e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 40.62 E-value: 4.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 86 IFLYLGEVTKAVQPLLLGRIIasydpDN--KEERSIAI-YLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYK 162
Cdd:cd18557 3 LFLLISSAAQLLLPYLIGRLI-----DTiiKGGDLDVLnELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 163 KTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLA--LAHFVWiAPLQVALLMGLIWEL---LQASAFCGLGFLIVLALFQ 237
Cdd:cd18557 78 SLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTdnLSQLLR-NILQVIGGLIILFILswkLTLVLLLVIPLLLIASKIY 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90421313 238 AGLGRMMMKYRDQRAGKISErlvITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAA 300
Cdd:cd18557 157 GRYIRKLSKEVQDALAKAGQ---VAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKA 216
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1209-1271 |
5.06e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.98 E-value: 5.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90421313 1209 QMTVKDLTAKYtEGGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGEIQIDG 1271
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LRMVAgleriTSGEIWIGG 65
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1236-1302 |
5.43e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.89 E-value: 5.43e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 90421313 1236 PGQRVGLLGRTGSGKSTLLSAFLRLLNTEGE--IQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRK 1302
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgvIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL 69
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
969-1085 |
6.31e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 40.51 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 969 AGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAV----------VAVlqpyifvATVPVIVAFIMLRAYFLQTSQ 1038
Cdd:cd18578 110 TGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIafvygwklalVGL-------ATVPLLLLAGYLRMRLLSGFE 182
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 90421313 1039 QLKQLESEGRSPIFTHLVTSLKglwTLRAFGRQPYFETLFHKALNLH 1085
Cdd:cd18578 183 EKNKKAYEESSKIASEAVSNIR---TVASLTLEDYFLEKYEEALEEP 226
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1212-1402 |
8.10e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 39.71 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1212 VKDLTAKYteGGNAILENISFSISPGQ-RVgLLGRTGSGKSTLLSAFL-RLLNTEGEIQIDGVSwdsitLQQW------- 1282
Cdd:COG4674 13 VEDLTVSF--DGFKALNDLSLYVDPGElRV-IIGPNGAGKTTLMDVITgKTRPDSGSVLFGGTD-----LTGLdeheiar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1283 ----RKaFgvipQKVFIFSG-TFRKNLD-----PYEQWS------DQEIWK----VADEVGLRSVIEQFPGkldfvlvdg 1342
Cdd:COG4674 85 lgigRK-F----QKPTVFEElTVFENLElalkgDRGVFAslfarlTAEERDrieeVLETIGLTDKADRLAG--------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 90421313 1343 gcVLSHGHKQ-L---MCLARsvlsKAKILLLDEPSAHLdpvTYQIIRRT---LKQAFADCTVILCEH 1402
Cdd:COG4674 151 --LLSHGQKQwLeigMLLAQ----DPKLLLLDEPVAGM---TDAETERTaelLKSLAGKHSVVVVEH 208
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1210-1253 |
8.65e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 8.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 90421313 1210 MTVKDLTAkyTEGGNAILENISFSISPGQRVGLLGRTGSGKSTL 1253
Cdd:CHL00131 8 LEIKNLHA--SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTL 49
|
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
964-1143 |
9.67e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 39.77 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 964 LNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPyifvaTVPVIVAFIMLRAYFL--------- 1034
Cdd:cd18585 86 LQKYRSGDLLNRIVADIDTLDNLYLRVLSPPVVALLVILATILFLAFFSP-----ALALILLAGLLLAGVVipllfyrlg 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90421313 1035 -QTSQQLKQLESEGRspifTHLVTSLKGLWTLRAFGRQP-YFETLFHKALNLHTANWflYLSTLRWFQMRIeMIFVIFFI 1112
Cdd:cd18585 161 kKIGQQLVQLRAELR----TELVDGLQGMAELLIFGALErQRQQLEQLSDALIKEQR--RLARLSGLSQAL-MILLSGLT 233
|
170 180 190
....*....|....*....|....*....|.
gi 90421313 1113 AVTFISILTTGEGEGRVGIILtLAMNIMSTL 1143
Cdd:cd18585 234 VWLVLWLGAPLVQNGALDGAL-LAMLVFAVL 263
|
|
| |
