|
Name |
Accession |
Description |
Interval |
E-value |
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-1464 |
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: 2332.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1 MQKSPLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSSDSADHLSEKLEREWDREQAS-KKKPQLIHALRRCFVW 79
Cdd:TIGR01271 1 MQRSPVEKANFLSKLFFWWTRPILRKGYRQKLELSDIYQIPSFDSADNLSERLEREWDRELASaKKNPKLLNALRRCFFW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 80 RFVFYGVLLYLGEVTKAVQPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSL 159
Cdd:TIGR01271 81 RFVFYGILLYFGEATKAVQPLLLGRIIASYDPFNAPEREIAYYLALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 160 IYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAI 239
Cdd:TIGR01271 161 IYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVILLMGLIWELLEVNGFCGLGFLILLALFQAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 240 LGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVF 319
Cdd:TIGR01271 241 LGQKMMPYRDKRAGKISERLAITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYLRYFYSSAFFFSGFFVVF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 320 LSVLPYTVINGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSLGMIRKIQDFLQTQEYKVLEYNLMFTGLVMENVTA 399
Cdd:TIGR01271 321 LSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEVEMVNVTA 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 400 FWEEGFQELLEKVQLNNDDRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASE 479
Cdd:TIGR01271 401 SWDEGIGELFEKIKQNNKARKQPNGDDGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 480 GIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLA 559
Cdd:TIGR01271 481 GKIKHSGRISFSPQTSWIMPGTIKDNIIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLA 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 560 RAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPD 639
Cdd:TIGR01271 561 RAVYKDADLYLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPD 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 640 FSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDAST--TWNKA-KQSFRQTG-EFGEKRKNS-ILSSFSSVKKISIVQK 714
Cdd:TIGR01271 641 FSSLLLGLEAFDNFSAERRNSILTETLRRVSIDGDSTvfSGPETiKQSFKQPPpEFAEKRKQSiILNPIASARKFSFVQM 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 715 TPL-----SIEGESDDLQERRLSLVPDSEHGEAALPRSNMITAGPTFPGRRRQSVLDLMTFTPSSvSSSLQRTRASIRKI 789
Cdd:TIGR01271 721 GPQkaqatTIEDAVREPSERKFSLVPEDEQGEESLPRGNQYHHGLQHQAQRRQSVLQLMTHSNRG-ENRREQLQTSFRKK 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 790 SLAPR--ISLKEEDIYSRRLSQDSTLNITEEINEEDLKECFFDDMVKIPTVTTWNTYLRYFTLHRGLFAVLIWCVLVFLV 867
Cdd:TIGR01271 800 SSITQqnELASELDIYSRRLSKDSVYEISEEINEEDLKECFADERENVFETTTWNTYLRYITTNRNLVFVLIFCLVIFLA 879
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 868 EVAASLFVLWLLKNNPVNGGNNGTKIAN-----TSYVVVITSSSFYYIFYIYVGVADTLLALSLFRGLPLVHTLITASKI 942
Cdd:TIGR01271 880 EVAASLLGLWLITDNPSAPNYVDQQHANasspdVQKPVIITPTSAYYIFYIYVGTADSVLALGFFRGLPLVHTLLTVSKR 959
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 943 LHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFI 1022
Cdd:TIGR01271 960 LHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAIFVVSVLQPYIFIAAIPVAVIFI 1039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1023 LLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIF 1102
Cdd:TIGR01271 1040 MLRAYFLRTSQQLKQLESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIF 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1103 VLFFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESICTKIMKELHSED 1182
Cdd:TIGR01271 1120 VFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILSTLQWAVNSSIDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKYQLST 1199
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1183 spnALVIKNEHVKKCdtWPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGE 1262
Cdd:TIGR01271 1200 ---VLVIENPHAQKC--WPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGE 1274
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1263 IQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVL 1342
Cdd:TIGR01271 1275 IQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVL 1354
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1343 SHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYES 1422
Cdd:TIGR01271 1355 SNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDS 1434
|
1450 1460 1470 1480
....*....|....*....|....*....|....*....|....
gi 91982740 1423 LQALLSEKSVFQRALSSSEKMKLF--HGRHSSKQKPRTQITAVK 1464
Cdd:TIGR01271 1435 IQKLLNETSLFKQAMSAADRLKLFplHRRNSSKRKPQPKITALR 1478
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
390-670 |
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: 552.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 390 TGLVMENVTAFWEEGFQELLEKVQLNNDDRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLM 469
Cdd:cd03291 2 TGVIMENVTAFWDEGFGELLEKAKQENNDRKHSSDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 470 LILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLS 549
Cdd:cd03291 82 LILGELEPSEGKIKHSGRISFSSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 550 GGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGT 629
Cdd:cd03291 162 GGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 91982740 630 FSELQSLRPDFSSKLMGYDTFDQFTEERRSSILTETLRRFS 670
Cdd:cd03291 242 FSELQSLRPDFSSKLMGYDTFDQFSAERRNSILTETLRRFS 282
|
|
| ABC_6TM_CFTR_D2 |
cd18600 |
Six-transmembrane helical domain 2 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
839-1162 |
2.13e-171 |
|
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: 515.51 E-value: 2.13e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 839 TTWNTYLRYFTLHRGLFAVLIWCVLVFLVEVAASLFVLWLLKNNPVNGGNNGTKIANTSYVVVITSSSFYYIFYIYVGVA 918
Cdd:cd18600 1 TTWNTYLRYITSHKSLIFVLILCLVIFAIEVAASLVGLWLLRSQADRVNTTRPESSSNTYAVIVTFTSSYYVFYIYVGVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 919 DTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVG 998
Cdd:cd18600 81 DSLLAMGFFRGLPLVHTLITVSKTLHQKMLHAVLHAPMSTFNTMKAGRILNRFSKDTAILDDLLPLTIFDFIQLFLIVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 999 AIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALN 1078
Cdd:cd18600 161 AITVVSILQPYIFLATVPVIIAFIVLRAYFLRTSQQLKQLESEARSPIFAHLVTSLKGLWTLRAFGRQPYFETLFHKALN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1079 LHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRV 1158
Cdd:cd18600 241 LHTANWFLYLSTLRWFQMRIEMIFVIFFTAVTFISIGTTGDGEGRVGIILTLAMNIMSTLQWAVNTSIDVDSLMRSVSRI 320
|
....
gi 91982740 1159 FKFI 1162
Cdd:cd18600 321 FKFI 324
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1204-1464 |
1.08e-163 |
|
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: 493.22 E-value: 1.08e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1204 GEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFG 1283
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSWNSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKII 1363
Cdd:cd03289 81 VIPQKVFIFSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1364 LLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSSEKM 1443
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRL 240
|
250 260
....*....|....*....|...
gi 91982740 1444 KLFHGRHSS--KQKPRTQITAVK 1464
Cdd:cd03289 241 KLFPRRNSSksKRKPRPQIQALQ 263
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-1433 |
9.91e-161 |
|
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: 525.67 E-value: 9.91e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 5 PLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSSDSADHLSEKLEREWDREQASKKK------------------ 66
Cdd:TIGR00957 203 PESSASFLSRITFWWITGMAVYGYRQPLEESDLWSLNKEDTSEMVVPVLVENWKKECKKTRKqpvsavygkkdpskpkgs 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 67 ----------------------PQLIHALRRCFVWRFVFYGVLLYLGEVTKAVQPVLLGRIIASYDpdNTEERSIAIYLG 124
Cdd:TIGR00957 283 sqldaneevealivksphkprkPSLFKVLYKTFGPYFLMSFCFKAIHDLMMFIGPQILSLLIRFVN--DPMAPDWQGYFY 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 125 IGLclLFI---VRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFI 201
Cdd:TIGR00957 361 TGL--LFVcacLQTLILHQYFHICFVSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATYINMI 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 202 WIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAM 281
Cdd:TIGR00957 439 WSAPLQVILALYFLWLNLGPSVLAGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKLYAWELAF 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 282 EKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSVLPYTVI---NGIVLRKIFTTISFCIVLRMSVTrQFPTAV 358
Cdd:TIGR00957 519 LDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALITFAVYVTVdenNILDAEKAFVSLALFNILRFPLN-ILPMVI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 359 QIWYDSLGMIRKIQDFLQTQEYK--VLEYNLMFTG----LVMENVTAFWEEGFQellekvqlnnddrktsngenhlsfsh 432
Cdd:TIGR00957 598 SSIVQASVSLKRLRIFLSHEELEpdSIERRTIKPGegnsITVHNATFTWARDLP-------------------------- 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 433 lclvgnPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSY 512
Cdd:TIGR00957 652 ------PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKAL 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 513 DEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVC 592
Cdd:TIGR00957 726 NEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIG 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 593 K--LMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSlrpdfssklmgydtfdqfteerRSSILTETLRRFS 670
Cdd:TIGR00957 806 PegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ----------------------RDGAFAEFLRTYA 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 671 VDDAsttwnkakqsfrqtgefgekrknsilssfssvkkisivqktplsiEGESDDlqerrlslvpdsehgeaalprsnMI 750
Cdd:TIGR00957 864 PDEQ---------------------------------------------QGHLED-----------------------SW 875
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 751 TAGPTFPGRRRQSVLDLMTFTpSSVSSSLQRTRASIrkislapriSLKEEDIySRRLSQDSTLNITEEiNEEDLKeCFFD 830
Cdd:TIGR00957 876 TALVSGEGKEAKLIENGMLVT-DVVGKQLQRQLSAS---------SSDSGDQ-SRHHGSSAELQKAEA-KEETWK-LMEA 942
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 831 DMVKIPTV---TTWNtYLRYFtlhrGLFAVLIWCVLVFLVEVAASLFVLWLlkNNPVNGGNNGTKIANTSYVVvitssSF 907
Cdd:TIGR00957 943 DKAQTGQVelsVYWD-YMKAI----GLFITFLSIFLFVCNHVSALASNYWL--SLWTDDPMVNGTQNNTSLRL-----SV 1010
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 908 YYIFYIYVGVADTLLALSLFRGLplvhtlITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIF 987
Cdd:TIGR00957 1011 YGALGILQGFAVFGYSMAVSIGG------IQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIK 1084
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 988 DFIQLLFIVVGAIIVVSALQPyIFLATVPGLA-VFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQ 1066
Cdd:TIGR00957 1085 MFMGSLFNVIGALIVILLATP-IAAVIIPPLGlLYFFVQRFYVASSRQLKRLESVSRSPVYSHFNETLLGVSVIRAFEEQ 1163
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1067 TYFETLFHKALNLHTANWFMYLATLRWFQMRIDMI---FVLFfiVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVN 1143
Cdd:TIGR00957 1164 ERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVgncIVLF--AALFAVISRHSLSAGLVGLSVSYSLQVTFYLNWLVR 1241
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1144 SSIDTDSLMRSVSRVFKFIDIQTEesictkimkelhsedSPNALviknEHVKKCDTWPSGGEMVVKDLTVKYVDDGNAIL 1223
Cdd:TIGR00957 1242 MSSEMETNIVAVERLKEYSETEKE---------------APWQI----QETAPPSGWPPRGRVEFRNYCLRYREDLDLVL 1302
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1224 ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-NIKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDP 1302
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINeSAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDP 1382
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1303 NGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRR 1382
Cdd:TIGR00957 1383 FSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS 1462
|
1450 1460 1470 1480 1490
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1383 VLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVF 1433
Cdd:TIGR00957 1463 TIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
5-1440 |
6.80e-159 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 519.92 E-value: 6.80e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 5 PLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSSDSADHLSEKLEREWdREQASKKKPQLIHALRRCFVWRFVFY 84
Cdd:PLN03232 228 PERYASIFSRIYFSWMTPLMQLGYRKPITEKDVWQLDQWDQTETLIKRFQRCW-TEESRRPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 85 GVLLYLGEVTKAVQPVLLGRIIASY---DPDNTEE-RSIAIYLGIGLCLLFIVRTLLlhpaifGLHHIGMQMRIAMFSLI 160
Cdd:PLN03232 307 GIFKIGHDLSQFVGPVILSHLLQSMqegDPAWVGYvYAFLIFFGVTFGVLCESQYFQ------NVGRVGFRLRSTLVAAI 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 161 YKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAIL 240
Cdd:PLN03232 381 FHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLI 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 241 GKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFL 320
Cdd:PLN03232 461 VRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSFILNSIPVVVTLV 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 321 SVLPYTVING-IVLRKIFTTISFCIVLRMSVTrQFPTAVQIWYDSLGMIRKIQDFLQTQEyKVLEYNLMFT----GLVME 395
Cdd:PLN03232 541 SFGVFVLLGGdLTPARAFTSLSLFAVLRSPLN-MLPNLLSQVVNANVSLQRIEELLLSEE-RILAQNPPLQpgapAISIK 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 396 NVTAFWeegfqellekvqlnndDRKTSNgenhlsfshlclvgnPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGEL 475
Cdd:PLN03232 619 NGYFSW----------------DSKTSK---------------PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGEL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 476 ---EASEGIIKhsGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQ 552
Cdd:PLN03232 668 shaETSSVVIR--GSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQ 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 553 RARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSE 632
Cdd:PLN03232 746 KQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 633 LQslrpdfssklmgydtfdqfteerRSSILTETLRRfsvddasttwNKAKQSFRQTgefgEKRKNSILSSFSSVKKIsiv 712
Cdd:PLN03232 826 LS-----------------------KSGSLFKKLME----------NAGKMDATQE----VNTNDENILKLGPTVTI--- 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 713 qktplsiegesdDLQERRLslvpdsehgeaalprsnmitaGPTFPGRRRQSVLdlmtftpssvssslqrtrasirkisla 792
Cdd:PLN03232 866 ------------DVSERNL---------------------GSTKQGKRGRSVL--------------------------- 885
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 793 prisLKEEDiysrrlsqdstlniteeineedlkecffddmvKIPTVTTWNTYLRYFTLHRGLFAVLIWCVLVFLVEVAAS 872
Cdd:PLN03232 886 ----VKQEE--------------------------------RETGIISWNVLMRYNKAVGGLWVVMILLVCYLTTEVLRV 929
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 873 LFVLWLlknnpvngGNNGTKIANTSYvvvitSSSFYYIFYIYVGVADtlLALSLFRGLPLVHTLITASKILHRKMLHSIL 952
Cdd:PLN03232 930 SSSTWL--------SIWTDQSTPKSY-----SPGFYIVVYALLGFGQ--VAVTFTNSFWLISSSLHAAKRLHDAMLNSIL 994
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 953 HAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTS 1032
Cdd:PLN03232 995 RAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVSTISLWAIMPLLILFYAAYLYYQSTS 1074
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1033 QQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIF-VLFFIVVTF 1111
Cdd:PLN03232 1075 REVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTIRLETLGgVMIWLTATF 1154
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1112 iSILTT------GEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFIDIQTEESIctkimkelhsedspn 1185
Cdd:PLN03232 1155 -AVLRNgnaenqAGFASTMGLLLSYTLNITTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATA--------------- 1218
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1186 alVIKNEhvKKCDTWPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQ 1264
Cdd:PLN03232 1219 --IIENN--RPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELeKGRIM 1294
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1265 IDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSH 1344
Cdd:PLN03232 1295 IDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSV 1374
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1345 GHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQ 1424
Cdd:PLN03232 1375 GQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQ 1454
|
1450
....*....|....*..
gi 91982740 1425 ALLS-EKSVFQRALSSS 1440
Cdd:PLN03232 1455 ELLSrDTSAFFRMVHST 1471
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-1440 |
1.78e-140 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 471.53 E-value: 1.78e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 5 PLEKASFISKLFFSWTTPILRKGYRHHLELSDIYQAPSSDSADHLSEKLEREWDrEQASKKKPQLIHALRRCFVWRFVFY 84
Cdd:PLN03130 228 PERHANIFSRIFFGWMTPLMQLGYKRPLTEKDVWKLDTWDQTETLYRSFQKCWD-EELKKPKPWLLRALNNSLGGRFWLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 85 GVLLYLGEVTKAVQPVLLGRIIASYDPDNTEER----SIAIYLGIGLCLLF-------IVRTlllhpaifglhhiGMQMR 153
Cdd:PLN03130 307 GFFKIGNDLSQFVGPLLLNLLLESMQNGEPAWIgyiyAFSIFVGVVLGVLCeaqyfqnVMRV-------------GFRLR 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 154 IAMFSLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVL 233
Cdd:PLN03130 374 STLVAAVFRKSLRLTHEGRKKFTSGKITNLMTTDAEALQQICQQLHTLWSAPFRIIIAMVLLYQQLGVASLIGSLMLVLM 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 234 VIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFS 313
Cdd:PLN03130 454 FPIQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKAQLLSAFNSFILNSI 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 314 GFFVVFLSVLPYTVINGIVL-RKIFTTISFCIVLRMSVTrQFPTAVQIWYDSLGMIRKIQDFLQTQEyKVLEYNLMFT-- 390
Cdd:PLN03130 534 PVLVTVVSFGVFTLLGGDLTpARAFTSLSLFAVLRFPLF-MLPNLITQAVNANVSLKRLEELLLAEE-RVLLPNPPLEpg 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 391 --GLVMENVTAFWEegfqellekvqlnnddrktSNGENhlsfshlclvgnPVLKNINLNIKKGEMLAITGSTGAGKTSLL 468
Cdd:PLN03130 612 lpAISIKNGYFSWD-------------------SKAER------------PTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 469 MLILGELEA-SEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVT 547
Cdd:PLN03130 661 SAMLGELPPrSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVN 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 548 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFY 627
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 628 GTFSELQSLRPDFSsKLMgydtfdqfteerrssiltetlrrfsvDDASttwnKAKQSFRQTGEFGEKRKNSilssfssvk 707
Cdd:PLN03130 821 GTYEELSNNGPLFQ-KLM--------------------------ENAG----KMEEYVEENGEEEDDQTSS--------- 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 708 kisivqktplsiegesddlqerrlslVPDSEHGEAALPRSnmitAGPTFPGRRRQSVLdlmtftpssvssslqrtrasir 787
Cdd:PLN03130 861 --------------------------KPVANGNANNLKKD----SSSKKKSKEGKSVL---------------------- 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 788 kislaprislkeediysrrlsqdstlnITEEINEEDlkecffddmvkiptVTTWNTYLRYFTLHRGLFAVLIwcvlVFLV 867
Cdd:PLN03130 889 ---------------------------IKQEERETG--------------VVSWKVLERYKNALGGAWVVMI----LFLC 923
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 868 EVAASLFvlwllknnpvnggnngtKIANTSYVVVITSSS-------FYYIFyIYVGVADTLLALSLFRGLPLVHTLITAS 940
Cdd:PLN03130 924 YVLTEVF-----------------RVSSSTWLSEWTDQGtpkthgpLFYNL-IYALLSFGQVLVTLLNSYWLIMSSLYAA 985
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 941 KILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFI----QLL--FIVVGAIIVVSalqpyiFLAT 1014
Cdd:PLN03130 986 KRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqifQLLstFVLIGIVSTIS------LWAI 1059
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1015 VPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWF 1094
Cdd:PLN03130 1060 MPLLVLFYGAYLYYQSTAREVKRLDSITRSPVYAQFGEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLVNMSSNRWL 1139
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1095 QMRID-----MIFVL-FFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVN-SSIDTDSLmRSVSRVFKFIDIQTE 1167
Cdd:PLN03130 1140 AIRLEtlgglMIWLTaSFAVMQNGRAENQAAFASTMGLLLSYALNITSLLTAVLRlASLAENSL-NAVERVGTYIDLPSE 1218
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1168 esictkimkelhsedSPnaLVIKNEhvKKCDTWPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKS 1247
Cdd:PLN03130 1219 ---------------AP--LVIENN--RPPPGWPSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKS 1279
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1248 TLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQ 1326
Cdd:PLN03130 1280 SMLNALFRIVELeRGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRR 1359
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1327 FPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDC 1406
Cdd:PLN03130 1360 NSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDC 1439
|
1450 1460 1470
....*....|....*....|....*....|....*
gi 91982740 1407 QRFLVIEQGNVWQYESLQALLS-EKSVFQRALSSS 1440
Cdd:PLN03130 1440 DRILVLDAGRVVEFDTPENLLSnEGSAFSKMVQST 1474
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
69-1433 |
8.41e-116 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 400.31 E-value: 8.41e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 69 LIHALRRCFVWRFVFygvlLYLGEVTKAVQPVLLGRIIASYDPDNTeersiAIYLGIGLCLLFIVRTLLLHPAIFGLHHI 148
Cdd:PTZ00243 238 LFAALPYYVWWQIPF----KLLSDVCTLTLPVLLKYFVKFLDADNA-----TWGRGLGLVLTLFLTQLIQSVCLHRFYYI 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 149 ----GMQMRIAMFSLIYKKTLKLSSRVLDK--ISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFS 222
Cdd:PTZ00243 309 sircGLQYRSALNALIFEKCFTISSKSLAQpdMNTGRIINMMSTDVERINSFMQYCMYLWSSPMVLLLSILLLSRLVGWC 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 223 AFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYM 302
Cdd:PTZ00243 389 ALMAVAVLLVTLPLNGAIMKHQMAARRKIAKAADARVKATNEFFSGIRIAKFMAWEPCFVANIEDKRARELRYLRDVQLA 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 303 RFFTSSAFFFSGFFVVFLSVLPYTVInGIVLRK--IFTTISFCIVLRMSVtRQFPTAVQIWYDSLGMIRKIQDFLQ---- 376
Cdd:PTZ00243 469 RVATSFVNNATPTLMIAVVFTVYYLL-GHELTPevVFPTIALLGVLRMPF-FMIPWVFTTVLQFLVSIKRISTFLEcdna 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 377 --TQEYKVLEYNLMFTGL--------VMEN--VTAFW------------------------------------------- 401
Cdd:PTZ00243 547 tcSTVQDMEEYWREQREHstacqlaaVLENvdVTAFVpvklprapkvktsllsralrmlcceqcrptkrhpspsvvvedt 626
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 402 -------------EEGFQELLEKVQLNNDDRKTSNGENHLSFShlcLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLL 468
Cdd:PTZ00243 627 dygspssasrhivEGGTGGGHEATPTSERSAKTPKMKTDDFFE---LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL 703
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 469 MLILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTL 548
Cdd:PTZ00243 704 QSLLSQFEISEGRVWAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNL 783
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYG 628
Cdd:PTZ00243 784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 629 TFSelqslrpDFSsklmgydtfdqfteerRSSIlTETLRrfsvddasttwnkakqsfrqtgefgekrknsilssfssvkk 708
Cdd:PTZ00243 864 SSA-------DFM----------------RTSL-YATLA----------------------------------------- 878
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 709 isivqktplsieGESDDLQERRLSLVPDSEHGEAALPrsnmitAGPTFPGRrrqsvldlmtftpssvSSSLQRTRAsirk 788
Cdd:PTZ00243 879 ------------AELKENKDSKEGDADAEVAEVDAAP------GGAVDHEP----------------PVAKQEGNA---- 920
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 789 islaprislkEEDIYSRRLSQDSTLNITEEineedlkecffddmvKIPTVTTWNTYLRYFTLHRGLFAVLIWCVLVFLVE 868
Cdd:PTZ00243 921 ----------EGGDGAALDAAAGRLMTREE---------------KASGSVPWSTYVAYLRFCGGLHAAGFVLATFAVTE 975
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 869 VAASLFVLWLlknnpVNGGNNGTKIANTSYVVVitsssfyYIFYIYVGVADTLLALSLfrglpLVHTLITASKILHRKML 948
Cdd:PTZ00243 976 LVTVSSGVWL-----SMWSTRSFKLSAATYLYV-------YLGIVLLGTFSVPLRFFL-----SYEAMRRGSRNMHRDLL 1038
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 949 HSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYF 1028
Cdd:PTZ00243 1039 RSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILVTSASQPFVLVALVPCGYLYYRLMQFY 1118
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1029 LHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIV 1108
Cdd:PTZ00243 1119 NSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTV 1198
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1109 VTFISILTTGEGEGTTGI-----ILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFID-IQTEEsictkiMKELHSE- 1181
Cdd:PTZ00243 1199 IALIGVIGTMLRATSQEIglvslSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDeVPHED------MPELDEEv 1272
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1182 -----------DSPNALVIKNEHVKKCDTWP-SGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTL 1249
Cdd:PTZ00243 1273 dalerrtgmaaDVTGTVVIEPASPTSAAPHPvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTL 1352
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1250 LSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFP 1328
Cdd:PTZ00243 1353 LLTFMRMVEVcGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASES 1432
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1329 GQLNFTLVDGGYVLSHGHKQLMCLARSVLSK-AKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQ 1407
Cdd:PTZ00243 1433 EGIDSRVLEGGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYD 1512
|
1450 1460
....*....|....*....|....*..
gi 91982740 1408 RFLVIEQGNVWQYESLQAL-LSEKSVF 1433
Cdd:PTZ00243 1513 KIIVMDHGAVAEMGSPRELvMNRQSIF 1539
|
|
| ABC_6TM_CFTR_D1 |
cd18594 |
Six-transmembrane helical domain 1 of Cystic Fibrosis Transmembrane Conductance Regulator; ... |
83-372 |
3.80e-112 |
|
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: 355.40 E-value: 3.80e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 83 FYGVLLYLGEVTKAVQPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYK 162
Cdd:cd18594 1 LLGILLFLEESLKIVQPLLLGRLVAYFVPDSTVTKTEAYLYALGLSLCAFLRVLLHHPYFFGLHRYGMQLRIALSSLIYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 163 KTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGK 242
Cdd:cd18594 81 KTLKLSSSALSKITTGHIVNLLSNDVQKFDEVLVYLHFLWIAPLQVIVLTGLLWREIGPSSLAGLGVLLLLLPLQAYLGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 243 MMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSV 322
Cdd:cd18594 161 LFAKYRRKTAGLTDERVKIMNEIISGMRVIKMYTWEESFAKLIENIRKKELKLIRKAAYIRAFNMAFFFFSPTLVSFATF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 323 LPYTVI-NGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSLGMIRKIQ 372
Cdd:cd18594 241 VPYVLTgNTLTARKVFTVISLLNALRMTITRFFPESIQTLSESRVSLKRIQ 291
|
|
| CFTR_R |
pfam14396 |
Cystic fibrosis TM conductance regulator (CFTR), regulator domain; |
639-844 |
1.43e-106 |
|
Cystic fibrosis TM conductance regulator (CFTR), regulator domain;
Pssm-ID: 464164 Cd Length: 213 Bit Score: 337.09 E-value: 1.43e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 639 DFSSKLMGYDTFDQFTEERRSSILTETLRRFSVD-DASTTWNKA-KQSFRQTGEFGEKRKNS-ILSSFSSVKKISIVQKT 715
Cdd:pfam14396 1 DFSSLLMGLEAFDNFSAERRNSILTETLRRFSVDeDAGGSRNEPkKQSFKQTDDFNEKRKNSvILNPLAASRKFSIIQKS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 716 PLSIEGESD---DLQERRLSLVPDSEHGEAALPRSNMITAGPTFPGRRRQSVLDLMTFTPSSVSSSLQRTRASIRKISLA 792
Cdd:pfam14396 81 QLQMNGIEEglsELPERRLSLVPESEQGEAALPRSNVLNTGPTLQGQRRQSVLALMTNTVAQGQGRREKGQSSFRKMSVV 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 793 PRISLKEE-DIYSRRLSQDSTLNITEEINEEDLKECFFDDMVKIPTVTTWNTY 844
Cdd:pfam14396 161 PQSNLASElDIYARRLSKDSVLDITEEINEEDLKECFADDIENVFETTTWNTY 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
392-623 |
4.16e-92 |
|
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: 296.30 E-value: 4.16e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 392 LVMENVTAFWEEGFQEllekvqlnnddrktsngenhlsfshlclvGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLI 471
Cdd:cd03250 1 ISVEDASFTWDSGEQE-----------------------------TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 472 LGELEASEGIIKHSGRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGG 551
Cdd:cd03250 52 LGELEKLSGSVSVPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 552 QRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCK-LMASKTRILVTSKMEQLKKADKILILHEGS 623
Cdd:cd03250 132 QKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENCILGlLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1204-1422 |
3.65e-88 |
|
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: 285.93 E-value: 3.65e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1204 GEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1363 ILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYES 1422
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
840-1417 |
2.38e-79 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 273.96 E-value: 2.38e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 840 TWNTYLRYFTLHRGLFAVLIwcvLVFLVEVAASLFVLWLLKnnpvnggnngtKIANTsYVVVITSSSFYYIFYIYVGVAD 919
Cdd:COG1132 8 LLRRLLRYLRPYRGLLILAL---LLLLLSALLELLLPLLLG-----------RIIDA-LLAGGDLSALLLLLLLLLGLAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 920 TLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGA 999
Cdd:COG1132 73 LRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1000 IIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNL 1079
Cdd:COG1132 153 LVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1080 HTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTT---GIILTLAMNIMSTLQWAVNSSIDTDSLMRSVS 1156
Cdd:COG1132 233 LRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVgdlVAFILYLLRLFGPLRQLANVLNQLQRALASAE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1157 RVFKFIDIQTEEsictkimkelhsEDSPNALVIKnehvkkcdtwPSGGEMVVKDLTVKYvDDGNAILENISFSISPGQRV 1236
Cdd:COG1132 313 RIFELLDEPPEI------------PDPPGAVPLP----------PVRGEIEFENVSFSY-PGDRPVLKDISLTIPPGETV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1237 GLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNL---DPNGkwRDEEIW 1312
Cdd:COG1132 370 ALVGPSGSGKSTLVNLLLRFYDPtSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIrygRPDA--TDEEVE 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1313 KVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCT 1392
Cdd:COG1132 448 EAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRT 527
|
570 580
....*....|....*....|....*
gi 91982740 1393 VVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:COG1132 528 TIVIAHRLSTIRNADRILVLDDGRI 552
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
853-1158 |
1.17e-75 |
|
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: 254.17 E-value: 1.17e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 853 GLFAVLIWCVLVFLvevAASLFVL--WLL----KNNPVNGGNNGTKIANTSYVVVITSSSFYYIFYIYVGVADTLLALSL 926
Cdd:cd18601 1 GVFVFILLVLLNIA---AQVLYVLsdWWLsywaNLEEKLNDTTDRVQGENSTNVDIEDLDRDFNLGIYAGLTAATFVFGF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 927 FRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSAL 1006
Cdd:cd18601 78 LRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQLLLQVVGVVLLAVVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1007 QPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFM 1086
Cdd:cd18601 158 NPWVLIPVIPLVILFLFLRRYYLKTSREVKRIEGTTRSPVFSHLSSTLQGLWTIRAYSAQERFQEEFDAHQDLHSEAWFL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1087 YLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTG-IILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRV 1158
Cdd:cd18601 238 FLATSRWLAVRLDALCALFVTVVAFGSLFLAESLDAGLVgLSLSYALTLMGTFQWCVRQSAEVENLMTSVERV 310
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
857-1162 |
5.31e-74 |
|
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: 248.57 E-value: 5.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 857 VLIWCVLVFLVEVAASLFVLWLlknnpvnggnngtKIANTSYVVVITSSSFYYIFYIYVGVADTLLALSLFRGLPLVHTL 936
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWL-------------DWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 937 ITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVP 1016
Cdd:cd18580 68 LRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1017 GLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQM 1096
Cdd:cd18580 148 LLVVYYLLQRYYLRTSRQLRRLESESRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRWLGL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1097 RIDMIFVLFFIVVTFISILTTGEGEGTTG-IILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFI 1162
Cdd:cd18580 228 RLDLLGALLALVVALLAVLLRSSISAGLVgLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
829-1435 |
2.15e-66 |
|
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: 239.74 E-value: 2.15e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 829 FDDMVKIPTVTTWntYLRYFTLHRGLFA-VLIWCVLVFLVEVAASLFVLWLLknnpvnggnngtkiantSYVVVITSSSF 907
Cdd:COG2274 134 FDKRGEKPFGLRW--FLRLLRRYRRLLLqVLLASLLINLLALATPLFTQVVI-----------------DRVLPNQDLST 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 908 YYIFYIYVGVAdTLL--ALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSkDIAILDDFLPLT 985
Cdd:COG2274 195 LWVLAIGLLLA-LLFegLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGS 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 986 IFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAF-- 1063
Cdd:COG2274 273 LLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALga 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1064 --RRQTYFETLFHKALNL-----HTANWFMYLATLrwfqmridmIFVLFFIVVTFISILTtgegegttgII---LTLAMN 1133
Cdd:COG2274 353 esRFRRRWENLLAKYLNArfklrRLSNLLSTLSGL---------LQQLATVALLWLGAYL---------VIdgqLTLGQL 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1134 IM-STLQWAVNSSIDT--DSLMR------SVSRVFKFIDIQTEESictkimkelhsedsPNALVIKNEHVKkcdtwpsgG 1204
Cdd:COG2274 415 IAfNILSGRFLAPVAQliGLLQRfqdakiALERLDDILDLPPERE--------------EGRSKLSLPRLK--------G 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1205 EMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-NIKGEIQIDGVSWNSMTLQEWRKAFG 1283
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYePTSGRILIDGIDLRQIDPASLRRQIG 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKVFIFSGTFRQNL-----DPNgkwrDEEIWKVADQVGLKSVIEQFPGQLNfTLV-DGGYVLSHGHKQLMCLARSVL 1357
Cdd:COG2274 553 VVLQDVFLFSGTIRENItlgdpDAT----DEEIIEAARLAGLHDFIEALPMGYD-TVVgEGGSNLSGGQRQRLAIARALL 627
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1358 SKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQR 1435
Cdd:COG2274 628 RNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAE 705
|
|
| ABC_6TM_MRP4_D1_like |
cd18593 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 4 (MRP4) ... |
83-371 |
3.13e-64 |
|
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: 220.17 E-value: 3.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 83 FYGVLLYLGEVTKAVQPVLLGRIIASYDPDNTE-ERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIY 161
Cdd:cd18593 1 LLGIFLFLEEAIRVVQPIFLGKLIRYFEGNGSSiSLTEAYLYAGGVSLCSFLFIITHHPYFFGMQRIGMRLRVACSSLIY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 162 KKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILG 241
Cdd:cd18593 81 RKALRLSQAALGKTTVGQIVNLLSNDVNRFDQAVLFLHYLWVAPLQLIAVIYILWFEIGWSCLAGLAVLLILIPLQSFFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 242 KMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLS 321
Cdd:cd18593 161 KLFSKLRRKTAARTDKRIRIMNEIINGIRVIKMYAWEKAFAKLVDDLRRKEIKKVRRTSFLRALNMGLFFVSSKLILFLT 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 322 VLPYTVI-NGIVLRKIFTTISFCIVLRMSVTRQFPTAVQIWYDSLGMIRKI 371
Cdd:cd18593 241 FLAYILLgNILTAERVFVTMALYNAVRLTMTLFFPFAIQFGSELSVSIRRI 291
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
959-1438 |
1.99e-60 |
|
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: 218.48 E-value: 1.99e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 959 FNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILL---RAYFL--HTSQ 1033
Cdd:COG4987 106 LARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGLLLAGLLlplLAARLgrRAGR 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1034 QLKQLESEGRspifTHLVTSLKGLWTLRAFRRQTYFEtlfhKALNLHTANWFMYLATLRWFQMRID--MIFVLFFIVVTF 1111
Cdd:COG4987 186 RLAAARAALR----ARLTDLLQGAAELAAYGALDRAL----ARLDAAEARLAAAQRRLARLSALAQalLQLAAGLAVVAV 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1112 ISILTTGEGEGTTGIILtLAMNIMSTL--------------QWAvnssidtdSLMRSVSRVFKFIDIQTEESictkimke 1177
Cdd:COG4987 258 LWLAAPLVAAGALSGPL-LALLVLAALalfealaplpaaaqHLG--------RVRAAARRLNELLDAPPAVT-------- 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1178 lhSEDSPNALviknehvkkcdtwPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML 1257
Cdd:COG4987 321 --EPAEPAPA-------------PGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1258 NI-KGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNF 1333
Cdd:COG4987 386 DPqSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLrlaRPDAT--DEELWAALERVGLGDWLAALPDGLDT 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1334 TLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIE 1413
Cdd:COG4987 464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
|
490 500
....*....|....*....|....*
gi 91982740 1414 QGNVWQYESLQALLSEKSVFQRALS 1438
Cdd:COG4987 544 DGRIVEQGTHEELLAQNGRYRQLYQ 568
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
85-365 |
1.67e-57 |
|
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: 200.79 E-value: 1.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 85 GVLLYLGEVTKAVQPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKT 164
Cdd:cd18579 3 GLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 165 LKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMM 244
Cdd:cd18579 83 LRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWSAPLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFLAKLI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 245 VKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSVLP 324
Cdd:cd18579 163 SKLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKPFLKRIEELRKKELKALRKFGYLRALNSFLFFSTPVLVSLATFAT 242
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 91982740 325 YTVING-IVLRKIFTTISFCIVLRMsVTRQFPTAVQIWYDSL 365
Cdd:cd18579 243 YVLLGNpLTAAKVFTALSLFNLLRF-PLLMLPQAISSLIEAL 283
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1200-1422 |
2.82e-57 |
|
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: 197.25 E-value: 2.82e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1200 WPSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEW 1278
Cdd:cd03369 1 WPEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1279 RKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVadqvglksvieqfpgqlnFTLVDGGYVLSHGHKQLMCLARSVLS 1358
Cdd:cd03369 81 RSSLTIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALLK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1359 KAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYES 1422
Cdd:cd03369 143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1199-1430 |
5.94e-53 |
|
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: 196.13 E-value: 5.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1199 TWPSGGEMVVKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-NIKGEIQIDGVSWNSMTLQE 1277
Cdd:COG4988 330 PAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLpPYSGSILINGVDLSDLDPAS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 WRKAFGVITQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLAR 1354
Cdd:COG4988 409 WRRQIAWVPQNPYLFAGTIRENLrlgRPDAS--DEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1355 SVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEK 1430
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
69-622 |
1.75e-52 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 195.00 E-value: 1.75e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 69 LIHALRRCfvWRFVFYGVLLYLGE-VTKAVQPVLLGRIIASYDpdNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHH 147
Cdd:COG1132 12 LLRYLRPY--RGLLILALLLLLLSaLLELLLPLLLGRIIDALL--AGGDLSALLLLLLLLLGLALLRALLSYLQRYLLAR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 148 IGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEglALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGL 227
Cdd:COG1132 88 LAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQ--FLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 228 GLLIVLVIFQAILGKMMVKYRdKRAAKINERL----VITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAymr 303
Cdd:COG1132 166 IVLLVLPLLLLVLRLFGRRLR-KLFRRVQEALaelnGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA--- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 304 fftssafffsgffvvFLSVLPYTVINgivlrkIFTTISFCIVL----------RMSVTrQFPTAVQIwydSLGMIRKIQD 373
Cdd:COG1132 242 ---------------RLSALFFPLME------LLGNLGLALVLlvggllvlsgSLTVG-DLVAFILY---LLRLFGPLRQ 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 374 FLQTqeykvleYNLMFTGLvmenvtAFWEEGFQELLEKVQLNN--DDRKTSNGENHLSFSHLCLV---GNPVLKNINLNI 448
Cdd:COG1132 297 LANV-------LNQLQRAL------ASAERIFELLDEPPEIPDppGAVPLPPVRGEIEFENVSFSypgDRPVLKDISLTI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 449 KKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIKENIIFGV-SYDE 514
Cdd:COG1132 364 PPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrQIGVVPQDTFLFSGTIRENIRYGRpDATD 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 515 YRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFEScVCKL 594
Cdd:COG1132 444 EEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEA-LERL 522
|
570 580
....*....|....*....|....*...
gi 91982740 595 MASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:COG1132 523 MKGRTTIVIAHRLSTIRNADRILVLDDG 550
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1206-1415 |
1.79e-51 |
|
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: 179.12 E-value: 1.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGV 1284
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPtSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSGTFRQNLdpngkwrdeeiwkvadqvglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1365 LDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQG 1415
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1203-1433 |
3.26e-51 |
|
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: 181.65 E-value: 3.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1203 GGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKA 1281
Cdd:cd03288 17 GGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIfDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAK 1361
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1362 IILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEK-SVF 1433
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
855-1162 |
2.27e-48 |
|
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: 175.44 E-value: 2.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 855 FAVLIWCVLVFLVEVAASLFVLWLLKNNPVNGGNNGTKIANTSYVVVITSS-----SFYYIFYIYVGVAdtLLALSLFRG 929
Cdd:cd18599 2 YVVFLFVLLLFILSVGSTVFSDWWLSYWLKQGSGNTTNNVDNSTVDSGNISdnpdlNFYQLVYGGSILV--ILLLSLIRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 930 LPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPY 1009
Cdd:cd18599 80 FVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLIIIAIVFPW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1010 IFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLA 1089
Cdd:cd18599 160 FLIALIPLAIIFVFLSKIFRRAIRELKRLENISRSPLFSHLTATIQGLSTIHAFNKEKEFLSKFKKLLDQNSSAFFLFNC 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1090 TLRWFQMRIDMIFVLF-FIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFI 1162
Cdd:cd18599 240 AMRWLAVRLDILAVLItLITALLVVLLKGSISPAFAGLALSYALQLSGLFQFTVRLASETEARFTSVERILEYI 313
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
904-1158 |
4.55e-48 |
|
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: 173.82 E-value: 4.55e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 904 SSSFYYIFYIYVGVADTLLALSLFrgLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLP 983
Cdd:cd18606 33 SQGFYIGIYAGLGVLQAIFLFLFG--LLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 984 LTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAF 1063
Cdd:cd18606 111 DSLRMFLYTLSSIIGTFILIIIYLPWFAIALPPLLVLYYFIANYYRASSRELKRLESILRSFVYANFSESLSGLSTIRAY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1064 RRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTG-IILTLAMNIMSTLQWAV 1142
Cdd:cd18606 191 GAQDRFIKKNEKLIDNMNRAYFLTIANQRWLAIRLDLLGSLLVLIVALLCVTRRFSISPSSTgLVLSYVLQITQVLSWLV 270
|
250
....*....|....*.
gi 91982740 1143 NSSIDTDSLMRSVSRV 1158
Cdd:cd18606 271 RQFAEVENNMNSVERL 286
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
903-1158 |
5.78e-48 |
|
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: 173.81 E-value: 5.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 903 TSSSFYYIfYIYVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFL 982
Cdd:cd18604 39 EVSVLYYL-GIYALISLLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 983 PLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRA 1062
Cdd:cd18604 118 ADSLSSLLESTLSLLVILIAIVVVSPAFLLPAVVLAALYVYIGRLYLRASRELKRLESVARSPILSHFGETLAGLVTIRA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1063 FRRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAV 1142
Cdd:cd18604 198 FGAEERFIEEMLRRIDRYSRAFRYLWNLNRWLSVRIDLLGALFSFATAALLVYGPGIDAGLAGFSLSFALGFSSAILWLV 277
|
250
....*....|....*.
gi 91982740 1143 NSSIDTDSLMRSVSRV 1158
Cdd:cd18604 278 RSYNELELDMNSVERI 293
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
904-1158 |
7.42e-47 |
|
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: 170.86 E-value: 7.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 904 SSSFYYIFyIYVGVADTLLALSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLP 983
Cdd:cd18602 47 DEVSYYIS-VYAGLSLGAVILSLVTNLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLP 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 984 LTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAF 1063
Cdd:cd18602 126 TTLERLLRFLLLCLSAIIVNAIVTPYFLIALIPIIIVYYFLQKFYRASSRELQRLDNITKSPVFSHFSETLGGLTTIRAF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1064 RRQTYFETLFHKALNLHTANWFMYLATLRWFQMRIDMIFVLFFIVVTFISILTTGEGEGTTGII---LTLAMNIMSTLQW 1140
Cdd:cd18602 206 RQQARFTQQMLELIDRNNTAFLFLNTANRWLGIRLDYLGAVIVFLAALSSLTAALAGYISPSLVglaITYALLVPIYLNW 285
|
250
....*....|....*...
gi 91982740 1141 AVNSSIDTDSLMRSVSRV 1158
Cdd:cd18602 286 VVRNLADVEMQMNSVERV 303
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
857-1142 |
1.43e-46 |
|
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: 168.98 E-value: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 857 VLIWCVLVFLVEVAASLFVLWLlknnpvnggNNGTKIANTSYVVVITSSSFYYIFYIYVGVADTLLalSLFRGLPLVHTL 936
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVL---------GRILDVLLPDGDPETQALNVYSLALLLLGLAQFIL--SFLQSYLLNHTG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 937 ITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVP 1016
Cdd:pfam00664 70 ERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1017 GLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQM 1096
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFG 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 91982740 1097 RIDMIFVLFFIVVTFISILTTGEGEGTTGIILTLAMnIMSTLQWAV 1142
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLS-LFAQLFGPL 274
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
437-623 |
6.36e-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: 159.42 E-value: 6.36e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII-----------------KHSGRVSFSSQISWIMP 499
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatrsRNRYSVAYAAQKPWLLN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 GTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03290 93 ATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 91982740 580 VLTEEQIFESCVCKLMA--SKTRILVTSKMEQLKKADKILILHEGS 623
Cdd:cd03290 173 IHLSDHLMQEGILKFLQddKRTLVLVTHKLQYLPHADWIIAMKDGS 218
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
937-1158 |
1.26e-43 |
|
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: 161.11 E-value: 1.26e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 937 ITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVP 1016
Cdd:cd18603 70 VRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVISTLVVISISTPIFLVVIIP 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1017 GLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQM 1096
Cdd:cd18603 150 LAILYFFIQRFYVATSRQLKRLESVSRSPIYSHFSETLQGASTIRAYGVQERFIRESDRRVDENQRAYYPSIVSNRWLAV 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1097 RIDMI--FVLFFIVVtFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRV 1158
Cdd:cd18603 230 RLEFLgnLIVLFAAL-FAVLSRDSLSPGLVGLSISYALQITQTLNWLVRMTSELETNIVSVERI 292
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1204-1430 |
3.73e-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: 157.39 E-value: 3.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1204 GEMVVKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPqKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIrlgRPNAT--DEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1360 AKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEK 1430
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
857-1162 |
3.81e-43 |
|
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: 160.00 E-value: 3.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 857 VLIWCVLVFLVEVAASLFVLWLlknnpvngGNNGTKIANTSYVVVITSSSFYYIFYIYVGVADTLLALslFRGLPLVHTL 936
Cdd:cd18605 1 LILILLSLILMQASRNLIDFWL--------SYWVSHSNNSFFNFINDSFNFFLTVYGFLAGLNSLFTL--LRAFLFAYGG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 937 ITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVP 1016
Cdd:cd18605 71 LRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLLLP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1017 GLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLRWFQM 1096
Cdd:cd18605 151 LAFIYYRIQRYYRATSRELKRLNSVNLSPLYTHFSETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQLASQAASQWLSI 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1097 RIDMI--FVLFFIVVTFISILTTGEGEGTTGIILTL--AMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFI 1162
Cdd:cd18605 231 RLQLLgvLIVTFVALTAVVQHFFGLSIDAGLIGLALsyALPITGLLSGLLNSFTETEKEMVSVERVRQYF 300
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
394-635 |
1.53e-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: 1.53e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 394 MENVTAFweEGFQELLEK---VQLNNDDRKTSNGENHLSFSHLCLV---GNPVLKNINLNIKKGEMLAITGSTGAGKTSL 467
Cdd:COG4988 302 ANGIAAA--EKIFALLDApepAAPAGTAPLPAAGPPSIELEDVSFSypgGRPALDGLSLTIPPGERVALVGPSGAGKSTL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 468 LMLILGELEASEGIIKHSGR-------VSFSSQISWI------MPGTIKENIIFG-VSYDEYRYKSVVKACQLQEDITKF 533
Cdd:COG4988 380 LNLLLGFLPPYSGSILINGVdlsdldpASWRRQIAWVpqnpylFAGTIRENLRLGrPDASDEELEAALEAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 534 AEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFEScVCKLMASKTRILVTSKMEQLKKA 613
Cdd:COG4988 460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQA-LRRLAKGRTVILITHRLALLAQA 538
|
250 260
....*....|....*....|..
gi 91982740 614 DKILILHEGSSYFYGTFSELQS 635
Cdd:COG4988 539 DRILVLDDGRIVEQGTHEELLA 560
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
437-622 |
4.84e-42 |
|
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: 151.77 E-value: 4.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIK 503
Cdd:cd03228 14 PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdldleslrkNIAYVPQDPFLFSGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIifgvsydeyryksvvkacqlqeditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03228 94 ENI-----------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190
....*....|....*....|....*....|....*....
gi 91982740 584 EQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:cd03228 133 ALILEA-LRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
123-640 |
3.20e-41 |
|
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: 163.47 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 123 LGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLISLLS--NNLNKFDEGLALAhf 200
Cdd:COG2274 198 LAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRdvESIREFLTGSLLT-- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 201 IWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESA 280
Cdd:COG2274 276 ALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESR 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 281 MEKIIESLREEELKMTRRSAymrfftssafffsgffvvFLSVLPYTVINGIvlRKIFTTISFCIVLRMSVTRQFptavqi 360
Cdd:COG2274 356 FRRRWENLLAKYLNARFKLR------------------RLSNLLSTLSGLL--QQLATVALLWLGAYLVIDGQL------ 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 361 wydSLGMIrkiqdflqtqeykvleynLMFTGLV------MENVTAFWEEgFQEL---LEKV----------QLNNDDRKT 421
Cdd:COG2274 410 ---TLGQL------------------IAFNILSgrflapVAQLIGLLQR-FQDAkiaLERLddildlpperEEGRSKLSL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 422 SNGENHLSFSHLCL----VGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------RVSF 490
Cdd:COG2274 468 PRLKGDIELENVSFrypgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidPASL 547
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 491 SSQIS------WIMPGTIKENIIFG---VSYDEyryksVVKACQ---LQEDITKFAEQDNTVLGEGGVTLSGGQRARISL 558
Cdd:COG2274 548 RRQIGvvlqdvFLFSGTIRENITLGdpdATDEE-----IIEAARlagLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAI 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 559 ARAVYKDADLYLLDSPFGYLDVLTEEQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRP 638
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILEN-LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKG 701
|
..
gi 91982740 639 DF 640
Cdd:COG2274 702 LY 703
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1207-1435 |
4.91e-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: 145.84 E-value: 4.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGVI 1285
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1286 TQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03251 82 SQDVFLFNDTVAENIaygRPGAT--REEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1363 ILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQR 1435
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAK 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1201-1430 |
9.48e-39 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 153.83 E-value: 9.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1201 PSGGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQIDGVSWNSMTLQEWR 1279
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQqGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1280 KAFGVITQKVFIFSGTFRQNL---DPNGkwRDEEIWKVADQVGLKSVIEQFPGqLNFTLVDGGYVLSHGHKQLMCLARSV 1356
Cdd:PRK11160 414 QAISVVSQRVHLFSATLRDNLllaAPNA--SDEALIEVLQQVGLEKLLEDDKG-LNAWLGEGGRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1357 LSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEK 1430
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1204-1415 |
4.29e-38 |
|
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: 142.34 E-value: 4.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1204 GEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNItlgAPLAD--DERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1360 AKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIeAMLD-CQRFLVIEQG 1415
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDlVDRIIVMDSG 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
437-633 |
6.84e-38 |
|
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: 142.36 E-value: 6.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR----VSFSS---------QISWIMPGTIK 503
Cdd:cd03254 15 KKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIdirdISRKSlrsmigvvlQDTFLFSGTIM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFGVSY-DEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03254 95 ENIRLGRPNaTDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 583 EEQIfESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03254 175 EKLI-QEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1206-1399 |
3.10e-37 |
|
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: 148.66 E-value: 3.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGV 1284
Cdd:TIGR02868 335 LELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDpLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAK 1361
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLrlaRPDAT--DEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*...
gi 91982740 1362 IILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHR 1399
Cdd:TIGR02868 492 ILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
423-640 |
6.21e-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: 148.38 E-value: 6.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 423 NGENHLSFSHLCL----VGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------------ 486
Cdd:COG4987 329 PGGPSLELEDVSFrypgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGvdlrdldeddlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 487 -RVSFSSQISWIMPGTIKENIIFG---VSYDEYRykSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAV 562
Cdd:COG4987 409 rRIAVVPQRPHLFDTTLRENLRLArpdATDEELW--AALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 563 YKDADLYLLDSPFGYLDVLTEEQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDF 640
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALLAD-LLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1205-1438 |
6.80e-37 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 148.45 E-value: 6.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1205 EMVVKDLTVkYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFGV 1284
Cdd:PRK11174 349 TIEAEDLEI-LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSGTFRQNL---DPNGkwRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAK 1361
Cdd:PRK11174 428 VGQNPQLPHGTLRDNVllgNPDA--SDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQ 505
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1362 IILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALS 1438
Cdd:PRK11174 506 LLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1207-1415 |
8.83e-37 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 138.37 E-value: 8.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVI 1285
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGpTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1286 TQ--KVFIFSGTFRQ-------NLDPNGKWRDEEIWKVADQVGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCLArSV 1356
Cdd:cd03225 81 FQnpDDQFFGPTVEEevafgleNLGLPEEEIEERVEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIA-GV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1357 LS-KAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIEAMLD-CQRFLVIEQG 1415
Cdd:cd03225 149 LAmDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| ABC_6TM_YOR1_D1_like |
cd18597 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Yor1p and similar proteins; ABCC ... |
85-365 |
9.25e-37 |
|
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: 141.05 E-value: 9.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 85 GVLLYLGEVTKAVQPVLLGRII----ASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLI 160
Cdd:cd18597 3 GLLKLLADVLQVLSPLLLKYLInfveDAYLGGPPPSIGYGIGYAIGLFLLQLLSSLLLNHFFYRSMLTGAQVRAALTKAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 161 YKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAIL 240
Cdd:cd18597 83 YRKSLRLSGKSRHEFPNGKITNLMSTDLSRIDFALGFFHFLWTAPIQIIIAIALLIVNLGPSALVGIGVLILSIPLQGFL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 241 GKMMVKYRdKRAAKI-NERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVF 319
Cdd:cd18597 163 MKKLFKLR-KKANKItDKRVKLTQEILQGIRVIKFYAWEDAFLERITEIRKKELKYVRKLQILRSILTAVAFSLPVLASM 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 91982740 320 LSVLPYTVINGiVLR--KIFTTISFCIVLRMSVTrQFPTAVQIWYDSL 365
Cdd:cd18597 242 LSFITYYATGH-TLDpaNIFSSLALFNVLRMPLM-FLPLALSSLADAL 287
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1207-1433 |
9.85e-37 |
|
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: 139.29 E-value: 9.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGVI 1285
Cdd:cd03253 2 EFENVTFAY-DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVsSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1286 TQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03253 81 PQDTVLFNDTIGYNIrygRPDAT--DEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1363 ILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVF 1433
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLY 229
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1208-1417 |
1.40e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 138.62 E-value: 1.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:COG1122 3 LENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTL----LRLLNgllkpTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVitqkVF------IFSGTFRQ-------NLDPNGKWRDEEIWKVADQVGLKSVIEQFPgqlnftlvdggYVLSHGHKQL 1349
Cdd:COG1122 78 GL----VFqnpddqLFAPTVEEdvafgpeNLGLPREEIRERVEEALELVGLEHLADRPP-----------HELSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1350 MCLArSVLS-KAKIILLDEPSANLDPI-TYQVIRRVLRQAFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:COG1122 143 VAIA-GVLAmEPEVLVLDEPTAGLDPRgRRELLELLKRLNKEGKTVIIVTHDLDLVAElADRVIVLDDGRI 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1223-1370 |
2.83e-36 |
|
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: 134.70 E-value: 2.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSG-TFRQNL 1300
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSpTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1301 -------DPNGKWRDEEIWKVADQVGLksvieqfPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSA 1370
Cdd:pfam00005 81 rlglllkGLSKREKDARAEEALEKLGL-------GDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
437-633 |
4.30e-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: 137.36 E-value: 4.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-------------VSFSSQISWIMPGTIK 503
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdytlaslrrqIGLVSQDVFLFNDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFGVS-YDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03251 94 ENIAYGRPgATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 583 EEQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03251 174 ERLVQAA-LERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEEL 223
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1199-1412 |
9.40e-36 |
|
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: 143.97 E-value: 9.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1199 TWPSGGEMVVKDLTVKYVDDGNAiLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQE 1277
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYPGRRPA-LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPtEGSIAVNGVPLADADADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 WRKAFGVITQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLAR 1354
Cdd:TIGR02857 394 WRDQIAWVPQHPFLFAGTIAENIrlaRPDAS--DAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1355 SVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVI 1412
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
438-619 |
1.47e-32 |
|
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: 134.34 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIKE 504
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGvpladadadswrdQIAWVPQHPFLFAGTIAE 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVSY-DEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:TIGR02857 415 NIRLARPDaSDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 91982740 584 EQIFEScVCKLMASKTRILVTSKMEQLKKADKILIL 619
Cdd:TIGR02857 495 AEVLEA-LRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
437-633 |
1.47e-32 |
|
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: 126.96 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-------VSFSSQISwIMP-------GTI 502
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQdirevtlDSLRRAIG-VVPqdtvlfnDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIFG---VSYDEYRykSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03253 92 GYNIRYGrpdATDEEVI--EAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 580 VLTEEQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03253 170 THTEREIQAA-LRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEEL 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1207-1417 |
3.80e-32 |
|
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: 123.87 E-value: 3.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVI 1285
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1286 TQKVFIFSGTFRQNldpngkwrdeeiwkvadqvglksvieqfpgqlnftlvdggyVLSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:cd03246 82 PQDDELFSGSIAEN-----------------------------------------ILSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1366 DEPSANLDPITYQVIRRVLRQA-FAGCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_MRP1_2_3_6_D1_like |
cd18595 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 1, ... |
82-303 |
5.85e-32 |
|
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: 127.20 E-value: 5.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 82 VFYGVLLYlgevtkaVQPVLLGRIIaSYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIY 161
Cdd:cd18595 7 LLSDILLF-------ASPQLLKLLI-NFVEDPDEPLWKGYLYAVLLFLVSIIQSLLLHQYFHRCFRLGMRIRTALTSAIY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 162 KKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILG 241
Cdd:cd18595 79 RKALRLSNSARKKSTVGEIVNLMSVDAQRIQDLVPYLNMLWSAPLQIILALYFLWQTLGPSVLAGLGVMILLIPLNAVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 242 KMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMR 303
Cdd:cd18595 159 RKIKKLQVKQMKLKDERIKLMNEILNGIKVLKLYAWEESFEKKILKIREKELKLLKKAAYLN 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1222-1433 |
5.99e-32 |
|
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: 125.34 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNL 1300
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1301 ---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNfTLV-DGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPIT 1376
Cdd:cd03249 98 rygKPDAT--DEEVEEAAKKANIHDFIMSLPDGYD-TLVgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1377 YQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVF 1433
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVY 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1208-1429 |
6.95e-32 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 125.18 E-value: 6.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTlQEWRKAFGVIT 1286
Cdd:COG1131 3 VRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPtSGEVRVLGEDVARDP-AEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSG-TFRQNLD-------PNGKWRDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLS 1358
Cdd:COG1131 80 QEPALYPDlTVRENLRffarlygLPRKEARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1359 KAKIILLDEPSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRI-EAMLDCQRFLVIEQGNVWQYESLQALLSE 1429
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLeEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1211-1435 |
1.44e-31 |
|
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: 124.14 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1211 LTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM-LNIKGEIQIDGVSWNSMTLQEWRKAFGVITQKV 1289
Cdd:cd03252 6 VRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVLVDGHDLALADPAWLRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1290 FIFSGTFRQNL---DPNGKWrdEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:cd03252 86 VLFNRSIRDNIalaDPGMSM--ERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1367 EPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQR 1435
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1206-1417 |
4.06e-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: 120.88 E-value: 4.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVswNSMTLQE-WRKAFG 1283
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKpQQGEITLDGV--PVSDLEKaLSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKVFIFSGTFRQNLdpngkwrdeeiwkvadqvglksvieqfpgqlnftlvdgGYVLSHGHKQLMCLARSVLSKAKII 1363
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1364 LLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKI 174
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
437-641 |
1.09e-30 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 129.58 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELeASEGIIKHSG-------RVSFSSQISWI------MPGTIK 503
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielreldPESWRKHLSWVgqnpqlPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFG-VSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:PRK11174 441 DNVLLGnPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 583 EEQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFS 641
Cdd:PRK11174 521 EQLVMQA-LNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFA 578
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
81-303 |
1.17e-30 |
|
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: 122.75 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 81 FVFYGVLLYLGEVTKAVQPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLI 160
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 161 YKKTLKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFS-AFCGLGLLIVLVIFQAI 239
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKlTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 240 LGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMR 303
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVAN 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1208-1415 |
1.60e-30 |
|
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: 118.50 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGVIT 1286
Cdd:cd00267 2 IENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPtSGEILIDGKDIAKLPLEELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QkvfifsgtfrqnldpngkwrdeeiwkvadqvglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:cd00267 80 Q------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1367 EPSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRIE-AMLDCQRFLVIEQG 1415
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPElAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
441-575 |
4.06e-30 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 116.98 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIK-------------HSGRVSFSSQISWIMPG-TIKENI 506
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderksLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 507 IFGVsyDEYRYKSVVKACQLQEDITKFA--EQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:pfam00005 81 RLGL--LLKGLSKREKDARAEEALEKLGlgDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1208-1417 |
1.03e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.99 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGVIT 1286
Cdd:COG4619 3 LEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPtSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSGTFRQNLDPNGKWRDEEIwkvaDQVGLKSVIEQF---PGQLNFTLVDggyvLSHGHKQLMCLARSVLSKAKII 1363
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFQLRERKF----DRERALELLERLglpPDILDKPVER----LSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1364 LLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEH-RIEAMLDCQRFLVIEQGNV 1417
Cdd:COG4619 153 LLDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
438-622 |
1.17e-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: 118.08 E-value: 1.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIKE 504
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtdirqldpadlrrNIGYVPQDVTLFYGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVSY-DEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03245 97 NITLGAPLaDDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSE 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 91982740 584 EQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:cd03245 177 ERLKER-LRQLLGDKTLIIITHRPSLLDLVDRIIVMDSG 214
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1198-1430 |
1.82e-29 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 125.60 E-value: 1.82e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1198 DTWP-SGGEMVVKDLTVKYVDDgNAILENISFSISPGQRVGLLGRTGSGKSTLlsAFLRMLNI---KGEIQIDGVSWNSM 1273
Cdd:PRK10790 332 DDRPlQSGRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTL--ASLLMGYYpltEGEIRLDGRPLSSL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1274 TLQEWRKAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLA 1353
Cdd:PRK10790 409 SHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1354 RSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEK 1430
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1208-1420 |
2.17e-29 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 116.00 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVIT 1286
Cdd:cd03214 2 VENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QkvfifsgtfrqnldpngkwrdeeiwkVADQVGLKSVIEQfpgqlNFTlvdggyVLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:cd03214 80 Q--------------------------ALELLGLAHLADR-----PFN------ELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1367 EPSANLDpITYQV-----IRRVLRQafAGCTVVLCEHRIE-AMLDCQRFLVIEQGNVWQY 1420
Cdd:cd03214 123 EPTSHLD-IAHQIellelLRRLARE--RGKTVVMVLHDLNlAARYADRVILLKDGRIVAQ 179
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1208-1417 |
3.66e-29 |
|
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: 123.86 E-value: 3.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML----NIKGEIQIDGVSWNSMTLQEWRKAFG 1283
Cdd:COG1123 7 VRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLphggRISGEVLLDGRDLLELSEALRGRRIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQ---KVFIFSGTFRQ------NLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:COG1123 87 MVFQdpmTQLNPVTVGDQiaealeNLGLSRAEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1355 SVLSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEiADRVVVMDDGRI 221
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
438-622 |
4.89e-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: 114.62 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG-------IIKHSGRVSFSSQISWIM------PGTIKE 504
Cdd:cd03246 15 PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGrvrldgaDISQWDPNELGDHVGYLPqddelfSGSIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIifgvsydeyryksvvkacqlqeditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEE 584
Cdd:cd03246 95 NI-----------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190
....*....|....*....|....*....|....*...
gi 91982740 585 QIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDG 171
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1208-1417 |
7.68e-29 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 114.03 E-value: 7.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSmTLQEWRKAFGVIT 1286
Cdd:cd03230 3 VRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPdSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSG-TFRQNLDpngkwrdeeiwkvadqvglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:cd03230 80 EEPSLYENlTVRENLK----------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1366 DEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
437-622 |
4.46e-28 |
|
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: 113.74 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIK 503
Cdd:cd03244 16 LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiglhdlrsRISIIPQDPVLFSGTIR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENI-IFGVSYDEYRYkSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03244 96 SNLdPFGEYSDEELW-QALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPET 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 91982740 583 EEQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:cd03244 175 DALIQKT-IREAFKDCTVLTIAHRLDTIIDSDRILVLDKG 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
437-633 |
9.28e-28 |
|
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: 113.40 E-value: 9.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII-------------KHSGRVSFSSQISWIMPGTIK 503
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEIlldgvdirdlnlrWLRSQIGLVSQEPVLFDGTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFGVSYDEYryKSVVKACQL---QEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03249 95 ENIRYGKPDATD--EEVEEAAKKaniHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 581 LTEEQIFESCVcKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03249 173 ESEKLVQEALD-RAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
427-604 |
9.79e-28 |
|
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: 119.77 E-value: 9.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 427 HLSFSHLClvGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQ 493
Cdd:TIGR02868 339 DLSAGYPG--APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevrrRVSVCAQ 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 494 ISWIMPGTIKENIIFG---VSYDEYRykSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYL 570
Cdd:TIGR02868 417 DAHLFDTTVRENLRLArpdATDEELW--AALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....
gi 91982740 571 LDSPFGYLDVLTEEQIFEScVCKLMASKTRILVT 604
Cdd:TIGR02868 495 LDEPTEHLDAETADELLED-LLAALSGRTVVLIT 527
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1204-1429 |
1.82e-27 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 119.43 E-value: 1.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1204 GEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:PRK10789 312 GELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVsEGDIRFHDIPLTKLQLDSWRSRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:PRK10789 392 AVVSQTPFLFSDTVANNIalgRPDAT--QQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1360 AKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSE 1429
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQ 539
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1208-1431 |
2.77e-27 |
|
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: 112.26 E-value: 2.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSwNSMTLQEWRKAFGVIT 1286
Cdd:COG4555 4 VENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIDGED-VRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSG-TFRQNL-------DPNGKWRDEEIWKVADQVGLKSVIEQfpgqlnftLVDGgyvLSHGHKQLMCLARSVLS 1358
Cdd:COG4555 81 DERGLYDRlTVRENIryfaelyGLFDEELKKRIEELIELLGLEEFLDR--------RVGE---LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1359 KAKIILLDEPSANLDPITYQVIRRVLRQAFA-GCTVVLCEH---RIEAMLDcqRFLVIEQGNVWQYESLQALLSEKS 1431
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHimqEVEALCD--RVVILHKGKVVAQGSLDELREEIG 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1206-1418 |
4.49e-27 |
|
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: 111.67 E-value: 4.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGV 1284
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFI-FSGTFRQ--------NLDPNGKW--RDEEI-WKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCL 1352
Cdd:COG1120 80 VPQEPPApFGLTVRElvalgrypHLGLFGRPsaEDREAvEEALERTGLEHLADRPVDE-----------LSGGERQRVLI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDpITYQV-IRRVLRQ--AFAGCTVVLCEHRIE-AMLDCQRFLVIEQGNVW 1418
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLD-LAHQLeVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIV 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1208-1417 |
4.67e-27 |
|
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: 111.05 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMT---LQEWRKAFG 1283
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRpDSGEVLIDGEDISGLSeaeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKVFIFSG-TFRQN----LDPNGKWRDEEIWKVA----DQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:cd03261 81 MLFQSGALFDSlTVFENvafpLREHTRLSEEEIREIVleklEAVGLRGAEDLYPAE-----------LSGGMKKRVALAR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1355 SVLSKAKIILLDEPSANLDPITY----QVIRRvLRQAFaGCTVVLCEHRI-EAMLDCQRFLVIEQGNV 1417
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASgvidDLIRS-LKKEL-GLTSIMVTHDLdTAFAIADRIAVLYDGKI 215
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1206-1415 |
6.14e-27 |
|
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: 109.87 E-value: 6.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVDD---GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLrmlnikGEIQ-IDG-VSWNSMtlqewrk 1280
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALL------GELEkLSGsVSVPGS------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 aFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNfTLV-DGGYVLSHGHKQLMCLARSVLSK 1359
Cdd:cd03250 68 -IAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDL-TEIgEKGINLSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1360 AKIILLDEPSANLDPITYQ-VIRRVLRQAFAGC-TVVLCEHRIEAMLDCQRFLVIEQG 1415
Cdd:cd03250 146 ADIYLLDDPLSAVDAHVGRhIFENCILGLLLNNkTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
426-622 |
1.14e-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: 107.33 E-value: 1.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHLclvGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRvsfssQISWIMPGTIKEN 505
Cdd:cd00267 3 ENLSFRYG---GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGK-----DIAKLPLEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 IIFGVSydeyryksvvkacqlqeditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQ 585
Cdd:cd00267 75 IGYVPQ------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRER 118
|
170 180 190
....*....|....*....|....*....|....*....
gi 91982740 586 IFEScVCKLMAS-KTRILVTSKMEQLKKA-DKILILHEG 622
Cdd:cd00267 119 LLEL-LRELAEEgRTVIIVTHDPELAELAaDRVIVLKDG 156
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1206-1419 |
1.17e-26 |
|
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: 109.15 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDGVSWNSMTlqEWRK 1280
Cdd:cd03259 1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAglerpDSGEILIDGRDVTGVP--PERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVITQKVFIFSG-TFRQNL--------DPNGKWRDEEIWkVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMC 1351
Cdd:cd03259 73 NIGMVFQDYALFPHlTVAENIafglklrgVPKAEIRARVRE-LLELVGLEGLLNRYPHE-----------LSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1352 LARSVLSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKelQRELGITTIYVTHdQEEALALADRIAVMNEGRIVQ 211
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
406-622 |
1.63e-26 |
|
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: 116.39 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 406 QELLEKVQLNNDDRKTSNGENHLSFSHLCLV----GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG- 480
Cdd:COG4618 309 NELLAAVPAEPERMPLPRPKGRLSVENLTVVppgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGs 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 481 ------IIKHSGRVSFSSQISW------IMPGTIKENII-FGVSYDEyrykSVVKACQL---QEDITKFAEQDNTVLGEG 544
Cdd:COG4618 389 vrldgaDLSQWDREELGRHIGYlpqdveLFDGTIAENIArFGDADPE----KVVAAAKLagvHEMILRLPDGYDTRIGEG 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 545 GVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFEScvckLMASKTR----ILVTSKMEQLKKADKILILH 620
Cdd:COG4618 465 GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAA----IRALKARgatvVVITHRPSLLAAVDKLLVLR 540
|
..
gi 91982740 621 EG 622
Cdd:COG4618 541 DG 542
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1208-1417 |
2.35e-26 |
|
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: 108.75 E-value: 2.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDG--NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMT---LQEWRKA 1281
Cdd:cd03257 4 VKNLSVSFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPtSGSIIFDGKDLLKLSrrlRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVITQKVF-----------IFSGTFRQNLDPNGKWRDEE-IWKVADQVGL-KSVIEQFPGQlnftlvdggyvLSHGHKQ 1348
Cdd:cd03257 84 IQMVFQDPMsslnprmtigeQIAEPLRIHGKLSKKEARKEaVLLLLVGVGLpEEVLNRYPHE-----------LSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1349 LMCLARSVLSKAKIILLDEPSANLDPIT-YQVIR--RVLRQAFaGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVqAQILDllKKLQEEL-GLTLLFITHDLGVVAKiADRVAVMYAGKI 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1204-1433 |
3.12e-26 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 115.50 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1204 GEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:PRK11176 340 GDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIdEGEILLDGHDLRDYTLASLRNQV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKVFIFSGTFRQNL--DPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKA 1360
Cdd:PRK11176 420 ALVSQNVHLFNDTIANNIayARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDS 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1361 KIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVF 1433
Cdd:PRK11176 500 PILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
946-1435 |
4.51e-26 |
|
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: 115.99 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 946 KMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQL-LFIVVGAIIVVSALQPY-IFLATVPGLAVFIL 1023
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMwILVIVGLFLVRQNMLLFlLSLLSIPVYAVIII 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1024 LrayFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRA-----FRRQ---TYFETLFHKALNLHTAnwfmylatlRWFQ 1095
Cdd:TIGR01193 314 L---FKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSltseaERYSkidSEFGDYLNKSFKYQKA---------DQGQ 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1096 MRIDMIFVLFFIVVtfisilttgegegttgIILTLAMNIMSTlQWAVNSSIDTDSLMRS-VSRVFKFIDIQTE---ESIC 1171
Cdd:TIGR01193 382 QAIKAVTKLILNVV----------------ILWTGAYLVMRG-KLTLGQLITFNALLSYfLTPLENIINLQPKlqaARVA 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1172 TKIMKELHSEDSPnalviKNEHVKKCDTWPSGGEMVVKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLS 1251
Cdd:TIGR01193 445 NNRLNEVYLVDSE-----FINKKKRTELNNLNGDIVINDVSYSY-GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAK 518
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1252 AFLRMLNIK-GEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNL--DPNGKWRDEEIWKVADQVGLKSVIEQFP 1328
Cdd:TIGR01193 519 LLVGFFQARsGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLllGAKENVSQDEIWAACEIAEIKDDIENMP 598
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1329 GQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQaFAGCTVVLCEHRIEAMLDCQR 1408
Cdd:TIGR01193 599 LGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDK 677
|
490 500
....*....|....*....|....*..
gi 91982740 1409 FLVIEQGNVWQYESLQALLSEKSVFQR 1435
Cdd:TIGR01193 678 IIVLDHGKIIEQGSHDELLDRNGFYAS 704
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1208-1427 |
4.66e-26 |
|
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: 108.53 E-value: 4.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMT---LQEWRKAFG 1283
Cdd:COG1127 8 VRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPdSGEILVDGQDITGLSekeLYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VitqkVF----IFSG-TFRQN----LDPNGKWRDEEIWKVA----DQVGLKSVIEQFPGQLNftlvdGGyvlshghkqlM 1350
Cdd:COG1127 86 M----LFqggaLFDSlTVFENvafpLREHTDLSEAEIRELVleklELVGLPGAADKMPSELS-----GG----------M 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1351 C----LARSVLSKAKIILLDEPSANLDPIT----YQVIRRvLRQAFaGCTVVLCEHRIEAMLD-CQRFLVIEQGNVWQYE 1421
Cdd:COG1127 147 RkrvaLARALALDPEILLYDEPTAGLDPITsaviDELIRE-LRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*.
gi 91982740 1422 SLQALL 1427
Cdd:COG1127 225 TPEELL 230
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1208-1428 |
4.87e-26 |
|
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: 108.74 E-value: 4.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKY--VDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVswnSMTLQEWRKAFGV 1284
Cdd:COG1124 4 VRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGR---PVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ItQKVFifsgtfrQN----LDP---------------NGKWRDEEIWKVADQVGL-KSVIEQFPGQlnftlvdggyvLSH 1344
Cdd:COG1124 81 V-QMVF-------QDpyasLHPrhtvdrilaeplrihGLPDREERIAELLEQVGLpPSFLDRYPHQ-----------LSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1345 GHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEH---RIEAMldCQRFLVIEQGNVWQ 1419
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHdlaVVAHL--CDRVAVMQNGRIVE 219
|
....*....
gi 91982740 1420 YESLQALLS 1428
Cdd:COG1124 220 ELTVADLLA 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1204-1427 |
4.90e-26 |
|
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: 114.85 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1204 GEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRML-----NIKGEIQIDGV---SWNSMTL 1275
Cdd:COG4618 329 GRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLA----RLLvgvwpPTAGSVRLDGAdlsQWDREEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1276 QEWrkaFGVITQKVFIFSGTFRQNL----DPNgkwrDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMC 1351
Cdd:COG4618 405 GRH---IGYLPQDVELFDGTIAENIarfgDAD----PEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1352 LARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRIEAMLDCQRFLVIEQGNVWQY----ESLQAL 1426
Cdd:COG4618 478 LARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFgprdEVLARL 557
|
.
gi 91982740 1427 L 1427
Cdd:COG4618 558 A 558
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
416-638 |
2.36e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.61 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 416 NDDRKTSNGENHLSFSHLCL----VGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR---- 487
Cdd:PRK11160 327 PTTSTAAADQVSLTLNNVSFtypdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQpiad 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 488 ---------VSFSSQISWIMPGTIKENIIFGV--SYDEyRYKSVVKACQLQeditKFAEQD---NTVLGEGGVTLSGGQR 553
Cdd:PRK11160 407 yseaalrqaISVVSQRVHLFSATLRDNLLLAApnASDE-ALIEVLQQVGLE----KLLEDDkglNAWLGEGGRQLSGGEQ 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 554 ARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVcKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK11160 482 RRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLA-EHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
....*
gi 91982740 634 QSLRP 638
Cdd:PRK11160 561 LAQQG 565
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1208-1415 |
3.05e-25 |
|
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: 104.19 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN-----IKGEIQIDGVSWNSMT--LQEWRK 1280
Cdd:cd03229 3 LKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLL----RCIAgleepDSGSILIDGEDLTDLEdeLPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVITQKVFIFSG-TFRQNLdpngkwrdeeiwkvadqvglksvieqfpgqlnftlvdgGYVLSHGHKQLMCLARSVLSK 1359
Cdd:cd03229 77 RIGMVFQDFALFPHlTVLENI--------------------------------------ALGLSGGQQQRVALARALAMD 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1360 AKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHRI-EAMLDCQRFLVIEQG 1415
Cdd:cd03229 119 PDVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLdEAARLADRVVVLRDG 177
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
426-619 |
3.35e-25 |
|
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: 104.92 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFShlcLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG--------RVSFSSQ---I 494
Cdd:cd03235 3 EDLTVS---YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGkplekerkRIGYVPQrrsI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 495 SWIMPGTIKE--------NIIFGVSYDEYRYKSVVKAcqLQE-DITKFAEQDntvLGEggvtLSGGQRARISLARAVYKD 565
Cdd:cd03235 80 DRDFPISVRDvvlmglygHKGLFRRLSKADKAKVDEA--LERvGLSELADRQ---IGE----LSGGQQQRVLLARALVQD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 566 ADLYLLDSPFGYLDVLTEEQIFEsCVCKL-MASKTRILVTSKMEQ-LKKADKILIL 619
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYE-LLRELrREGMTILVVTHDLGLvLEYFDRVLLL 205
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
1222-1417 |
6.86e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 110.90 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLsaflRML-----NIKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGT- 1295
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLA----RLIvgiwpPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTv 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1296 ------FRQNLDPngkwrdEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPS 1369
Cdd:TIGR01842 409 aeniarFGENADP------EKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 91982740 1370 ANLDPITYQVIRRVLRQAFA-GCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
426-628 |
9.41e-25 |
|
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: 102.78 E-value: 9.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHLclvGN--PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASegiikhSGRVSFSSQISWIMPGTIK 503
Cdd:cd03247 4 NNVSFSYP---EQeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ------QGEITLDGVPVSDLEKALS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIifgvsydeyryksvvkaCQLQEDITKFaeqDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03247 75 SLI-----------------SVLNQRPYLF---DTTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 91982740 584 EQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYG 628
Cdd:cd03247 135 RQLLSL-IFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1208-1417 |
1.36e-24 |
|
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: 103.34 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNA--ILENISFSISPGQRVGLLGRTGSGKSTLlsaflrmLNI--------KGEIQIDGVSWNSMTLQE 1277
Cdd:cd03255 3 LKNLSKTYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTL-------LNIlggldrptSGEVRVDGTDISKLSEKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 W----RKAFGvitqkvFIFSG-------TFRQNLD-------PNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdgg 1339
Cdd:cd03255 76 LaafrRRHIG------FVFQSfnllpdlTALENVElplllagVPKKERRERAEELLERVGLGDRLNHYPSE--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1340 yvLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQ--AFAGCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:cd03255 141 --LSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
428-648 |
1.53e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.02 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV--GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG--------RVSF---SSQI 494
Cdd:COG1121 7 IELENLTVSygGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGkpprrarrRIGYvpqRAEV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 495 SWIMPGTIKENIIFGvsydeyRY-------------KSVVKACqLQE-DITKFAEQDntvLGEggvtLSGGQRARISLAR 560
Cdd:COG1121 87 DWDFPITVRDVVLMG------RYgrrglfrrpsradREAVDEA-LERvGLEDLADRP---IGE----LSGGQQQRVLLAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 561 AVYKDADLYLLDSPFGYLDVLTEEQIFEscvckLMAS-----KTRILVTSKMEQLKK-ADKILILHEGsSYFYGTFSELq 634
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYE-----LLRElrregKTILVVTHDLGAVREyFDRVLLLNRG-LVAHGPPEEV- 225
|
250
....*....|....
gi 91982740 635 sLRPDFSSKLMGYD 648
Cdd:COG1121 226 -LTPENLSRAYGGP 238
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
440-633 |
2.14e-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: 103.72 E-value: 2.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIKENI 506
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlaladpawlrrQVGVVLQENVLFNRSIRDNI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IFG-VSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQ 585
Cdd:cd03252 97 ALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 91982740 586 IFEScVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03252 177 IMRN-MHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDEL 223
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1208-1409 |
3.46e-24 |
|
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: 101.79 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRML-----NIKGEIQIDGVSWNSmTLQEWRKAF 1282
Cdd:COG4133 5 AENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTL----LRILagllpPSAGEVLWNGEPIRD-AREDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKVFIFSG-TFRQNLD-----PNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSV 1356
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1357 LSKAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIEAMLDCQRF 1409
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1208-1398 |
4.47e-24 |
|
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: 102.26 E-value: 4.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK------GEIQIDG--VSWNSMTLQEWR 1279
Cdd:cd03260 3 LRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdeGEVLLDGkdIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1280 KAFGVITQKVFIFSGTFRQNLD----PNGKWRDEEIwKVADQVGLKSVieQFPGQLNFTLVDGGyvLSHGHKQLMCLARS 1355
Cdd:cd03260 81 RRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEEL-DERVEEALRKA--ALWDEVKDRLHALG--LSGGQQQRLCLARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 91982740 1356 VLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEH 1398
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTH 198
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
438-633 |
5.34e-24 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 108.65 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIK-HS------------GRVSFSSQISWIMPGTIKE 504
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRfHDipltklqldswrSRLAVVSQTPFLFSDTVAN 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGV-SYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:PRK10789 408 NIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTE 487
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 91982740 584 EQIFEScVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK10789 488 HQILHN-LRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1208-1415 |
6.03e-24 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 102.47 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGvswnsMTLQEWRKAFGVIT 1286
Cdd:COG1121 9 LENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPtSGTVRLFG-----KPPRRARRRIGYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKV------------FIFSGTFRQN--LDPNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCL 1352
Cdd:COG1121 82 QRAevdwdfpitvrdVVLMGRYGRRglFRRPSRADREAVDEALERVGLEDLADRPIGE-----------LSGGQQQRVLL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDPIT----YQVIRRvLRQafAGCTVVLCEHRIEAMLD-CQRFLVIEQG 1415
Cdd:COG1121 151 ARALAQDPDLLLLDEPFAGVDAATeealYELLRE-LRR--EGKTILVVTHDLGAVREyFDRVLLLNRG 215
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1181-1417 |
6.83e-24 |
|
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: 108.37 E-value: 6.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1181 EDSPNALVIKnehvkkcdtwPSGGEMVVKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI- 1259
Cdd:COG5265 343 ADAPDAPPLV----------VGGGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVt 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1260 KGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNL---DPNGkwRDEEIWKVADQVGLKSVIEQFPGQLNfTLV 1336
Cdd:COG5265 412 SGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIaygRPDA--SEEEVEAAARAAQIHDFIESLPDGYD-TRV 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1337 -DGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQG 1415
Cdd:COG5265 489 gERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAG 568
|
..
gi 91982740 1416 NV 1417
Cdd:COG5265 569 RI 570
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1214-1417 |
7.84e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 101.28 E-value: 7.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1214 KYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMT---LQEWRKAFGVITQkv 1289
Cdd:COG2884 9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVLVNGQDLSRLKrreIPYLRRRIGVVFQ-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1290 fifsgTFR--------QN----LDPNGKwRDEEIWK----VADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLA 1353
Cdd:COG2884 87 -----DFRllpdrtvyENvalpLRVTGK-SRKEIRRrvreVLDLVGLSDKAKALPHEL-----------SGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1354 RSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRIEAMLDCQ-RFLVIEQGNV 1417
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrGTTVLIATHDLELVDRMPkRVLELEDGRL 215
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1208-1417 |
9.45e-24 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 102.06 E-value: 9.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGV---SWNSMTLQEWRKAFG 1283
Cdd:COG3638 5 LRNLSKRY-PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPtSGEILVDGQdvtALRGRALRRLRRRIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKvfifsgtFrqNLDPN----------------------GKWRDEEIWKVA---DQVGLKSVIEQFPGQLnftlvdg 1338
Cdd:COG3638 84 MIFQQ-------F--NLVPRlsvltnvlagrlgrtstwrsllGLFPPEDRERALealERVGLADKAYQRADQL------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1339 gyvlSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHRIE-AMLDCQRFLVIEQG 1415
Cdd:COG3638 148 ----SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDlARRYADRIIGLRDG 223
|
..
gi 91982740 1416 NV 1417
Cdd:COG3638 224 RV 225
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
437-637 |
1.11e-23 |
|
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: 101.47 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII------KHSGRVSFSSQISwIMPG--------TI 502
Cdd:COG4555 13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedVRKEPREARRQIG-VLPDerglydrlTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENI-----IFGVSYDEYRYK--SVVKACQLQEDITKFAEqdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:COG4555 92 RENIryfaeLYGLFDEELKKRieELIELLGLEEFLDRRVG-----------ELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 576 GYLDVLTEEQIFEScVCKLMASKTRILVTSK-MEQLKK-ADKILILHEGSSYFYGTFSELQSLR 637
Cdd:COG4555 161 NGLDVMARRLLREI-LRALKKEGKTVLFSSHiMQEVEAlCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1206-1417 |
1.30e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 100.89 E-value: 1.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVDDGNA--ILENISFSISPGQRVGLLGRTGSGKSTLlsaflrmLNI--------KGEIQIDGVSWNSMT- 1274
Cdd:COG1136 5 LELRNLTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTL-------LNIlggldrptSGEVLIDGQDISSLSe 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1275 --LQEWR-KAFGvitqkvFIFSG-------TFRQN----LDPNG---KWRDEEIWKVADQVGLKSVIEQFPGQlnftlvd 1337
Cdd:COG1136 78 reLARLRrRHIG------FVFQFfnllpelTALENvalpLLLAGvsrKERRERARELLERVGLGDRLDHRPSQ------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1338 ggyvLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPIT----YQVIRRVLRQafAGCTVVLCEHRIEAMLDCQRFLVIE 1413
Cdd:COG1136 145 ----LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRE--LGTTIVMVTHDPELAARADRVIRLR 218
|
....
gi 91982740 1414 QGNV 1417
Cdd:COG1136 219 DGRI 222
|
|
| ABC_6TM_MRP7_D1_like |
cd18598 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated protein 7, and ... |
85-294 |
2.29e-23 |
|
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: 101.86 E-value: 2.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 85 GVLLYLGEVTKAVQPVLLGRIIaSYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKT 164
Cdd:cd18598 3 GLLKLLADVLGFAGPLLLNKLV-EFLEDSSEPLSDGYLYALGLVLSSLLGALLSSHYNFQMNKVSLKVRAALVTAVYRKA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 165 LKLSSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMM 244
Cdd:cd18598 82 LRVRSSSLSKFSTGEIVNLMSTDADRIVNFCPSFHDLWSLPLQIIVALYLLYQQVGVAFLAGLVFALVLIPINKWIAKRI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 245 VKY-RDKRAAKiNERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELK 294
Cdd:cd18598 162 GALsEKMMKHK-DARVKLMTEILSGIRVIKLLAWERIFKQKIEELRAKELK 211
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
427-633 |
3.33e-23 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 106.73 E-value: 3.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 427 HLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQ 493
Cdd:TIGR00958 483 DVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGvplvqydhhylhrQVALVGQ 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 494 ISWIMPGTIKENIIFGVSY-DEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLD 572
Cdd:TIGR00958 563 EPVLFSGSVRENIAYGLTDtPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 573 SPFGYLDVLTEEQIFEScvcKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:TIGR00958 643 EATSALDAECEQLLQES---RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQL 700
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
437-633 |
3.45e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.14 E-value: 3.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------------RVSFSSQISWIMPG-TIK 503
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGedvardpaevrrRIGYVPQEPALYPDlTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENI-----IFGVSYDEY--RYKSVVKACQLQEDITKFAEqdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:COG1131 92 ENLrffarLYGLPRKEAreRIDELLELFGLTDAADRKVG-----------TLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 577 YLDVLTEEQIFEsCVCKLMASKTRILVTS----KMEQLkkADKILILHEGSSYFYGTFSEL 633
Cdd:COG1131 161 GLDPEARRELWE-LLRELAAEGKTVLLSThyleEAERL--CDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1208-1417 |
3.96e-23 |
|
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: 99.43 E-value: 3.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQIDGVSWNSMTLQEwRKAFGV-- 1284
Cdd:cd03224 3 VENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRsGSIRFDGRDITGLPPHE-RARAGIgy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSG-TFRQNL--------DPNGKWRDEEIWkvadqvGLKSVIEQFPGQLnftlvdgGYVLSHGHKQLMCLARS 1355
Cdd:cd03224 80 VPEGRRIFPElTVEENLllgayarrRAKRKARLERVY------ELFPRLKERRKQL-------AGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1356 VLSKAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRV 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1208-1417 |
4.48e-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: 99.58 E-value: 4.48e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAI--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNI-----KGEIQIDGVSWNSMT---LQE 1277
Cdd:cd03258 4 LKNVSKVFGDTGGKVtaLKDVSLSVPKGEIFGIIGRSGAGKSTL----IRCINGlerptSGSVLVDGTDLTLLSgkeLRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 WRKAFGVITQKVFIFSG-TFRQN----LDPNGKWRDEEIWKVAD---QVGLKSVIEQFPGQlnftlvdggyvLSHGHKQL 1349
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSrTVFENvalpLEIAGVPKAEIEERVLElleLVGLEDKADAYPAQ-----------LSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1350 MCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRiCDRVAVMEKGEV 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1208-1417 |
5.98e-23 |
|
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: 104.60 E-value: 5.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGN---AILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMT---LQEWRK 1280
Cdd:COG1123 263 VRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPtSGSILFDGKDLTKLSrrsLRELRR 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVITQ----------KVF-IFSGTFRQNLDPNGKWRDEEIWKVADQVGL-KSVIEQFPGQlnftlvdggyvLSHGHKQ 1348
Cdd:COG1123 343 RVQMVFQdpysslnprmTVGdIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHE-----------LSGGQRQ 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1349 LMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
426-628 |
1.08e-22 |
|
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: 96.74 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHlclVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKhsgrvsfssqiswimpgtiken 505
Cdd:cd03214 3 ENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIL---------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 iIFGVSYDEYRYKSVVKAC----QLQE--DITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03214 58 -LDGKDLASLSPKELARKIayvpQALEllGLAHLADRPFN-------ELSGGERQRVLLARALAQEPPILLLDEPTSHLD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 580 VLTEEQIFEScVCKLMAS--KTRILVTSKMEQ-LKKADKILILHEGSSYFYG 628
Cdd:cd03214 130 IAHQIELLEL-LRRLARErgKTVVMVLHDLNLaARYADRVILLKDGRIVAQG 180
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1208-1417 |
3.40e-22 |
|
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: 97.25 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAiLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMT---LQEWRKAFG 1283
Cdd:cd03256 3 VENLSKTYPNGKKA-LKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGSVLIDGTDINKLKgkaLRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQK--------VF--IFSG------TFRQNLdpnGKWRDEEIWKVA---DQVGLKSVIEQFPGQlnftlvdggyvLSH 1344
Cdd:cd03256 82 MIFQQfnlierlsVLenVLSGrlgrrsTWRSLF---GLFPKEEKQRALaalERVGLLDKAYQRADQ-----------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1345 GHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHRIE-AMLDCQRFLVIEQGNV 1417
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDlAREYADRIVGLKDGRI 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
439-622 |
5.05e-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: 96.02 E-value: 5.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII----------KHSGRVSFS-SQISWIMPG------- 500
Cdd:cd03255 18 QALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgtdisklSEKELAAFRrRHIGFVFQSfnllpdl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENI-----IFGVSYDEY--RYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:cd03255 98 TALENVelpllLAGVPKKERreRAEELLERVGLGDRLNHYPSE-----------LSGGQQQRVAIARALANDPKIILADE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 574 PFGYLDVLTEEQIFEscvckLMAS------KTRILVTSKMEQLKKADKILILHEG 622
Cdd:cd03255 167 PTGNLDSETGKEVME-----LLRElnkeagTTIVVVTHDPELAEYADRIIELRDG 216
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1207-1428 |
5.92e-22 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 96.36 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYvddGNAILeNISFSISPGQRVGLLGRTGSGKSTLLSA---FLRMlnIKGEIQIDGVSWN---------SMT 1274
Cdd:COG3840 3 RLDDLTYRY---GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLiagFLPP--DSGRILWNGQDLTalppaerpvSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1275 LQEWRkafgvitqkvfIFSG-TFRQN----LDPNGKWRDEEIWKV---ADQVGLKSVIEQFPGQLnftlvdggyvlSHGH 1346
Cdd:COG3840 77 FQENN-----------LFPHlTVAQNiglgLRPGLKLTAEQRAQVeqaLERVGLAGLLDRLPGQL-----------SGGQ 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1347 KQLMCLARSVLSKAKIILLDEPSANLDPI----TYQVIRRVLRQafAGCTVVLCEHRIEAMLD-CQRFLVIEQGNVWQYE 1421
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPAlrqeMLDLVDELCRE--RGLTVLMVTHDPEDAARiADRVLLVADGRIAADG 212
|
....*..
gi 91982740 1422 SLQALLS 1428
Cdd:COG3840 213 PTAALLD 219
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
437-622 |
9.73e-22 |
|
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: 93.62 E-value: 9.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASegiikhSGRVSFSSQISWIMPGTIKENIifGVSYDE-- 514
Cdd:cd03230 12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD------SGEIKVLGKDIKKEPEEVKRRI--GYLPEEps 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 515 -YRYKSVvkacqlqeditkfaeQDNtvlgeggVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVcK 593
Cdd:cd03230 84 lYENLTV---------------REN-------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLR-E 140
|
170 180 190
....*....|....*....|....*....|.
gi 91982740 594 LMASKTRILVTS-KMEQLKK-ADKILILHEG 622
Cdd:cd03230 141 LKKEGKTILLSShILEEAERlCDRVAILNNG 171
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
437-648 |
1.28e-21 |
|
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: 95.45 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPG-TI 502
Cdd:cd03295 13 GKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGedireqdpvelrrKIGYVIQQIGLFPHmTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIFGVS---YDEYRYKSVVKacQLQE----DITKFAEQdntVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:cd03295 93 EENIALVPKllkWPKEKIRERAD--ELLAlvglDPAEFADR---YPHE----LSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 576 GYLDVLTEEQIFESCV-CKLMASKTRILVTSKM-EQLKKADKILILHEGSSYFYGTFSE-LQSLRPDFSSKLMGYD 648
Cdd:cd03295 164 GALDPITRDQLQEEFKrLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEiLRSPANDFVAEFVGAD 239
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
428-622 |
1.30e-21 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 94.50 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV--GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSS 492
Cdd:COG4619 1 LELEGLSFRvgGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGkplsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 493 QISWIMPGTIKENIIFGVSYDEYRYKsvvkacqlQEDITKFAEQ---DNTVLGEGGVTLSGGQRARISLARAVYKDADLY 569
Cdd:COG4619 81 QEPALWGGTVRDNLPFPFQLRERKFD--------RERALELLERlglPPDILDKPVERLSGGERQRLALIRALLLQPDVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 570 LLDSPFGYLDVLTeEQIFESCVCKLMASKTR--ILVTSKMEQLKK-ADKILILHEG 622
Cdd:COG4619 153 LLDEPTSALDPEN-TRRVEELLREYLAEEGRavLWVSHDPEQIERvADRVLTLEAG 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1179-1417 |
1.46e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 100.81 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1179 HSEDSPNALVIKNehVKkcdtwpsgGEMVVKDLTVKYVDDGNAIlENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN 1258
Cdd:PRK13657 318 DVRDPPGAIDLGR--VK--------GAVEFDDVSFSYDNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1259 IK-GEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNL---DPNGKwrDEEIWKVADQVGLKSVIEQFPGQLNFT 1334
Cdd:PRK13657 387 PQsGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIrvgRPDAT--DEEMRAAAERAQAHDFIERKPDGYDTV 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1335 LVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQ 1414
Cdd:PRK13657 465 VGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDN 544
|
...
gi 91982740 1415 GNV 1417
Cdd:PRK13657 545 GRV 547
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1208-1417 |
1.63e-21 |
|
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: 94.52 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-NIKGEIQIDGVSwnsmtLQEWRKAFGVIT 1286
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkPTSGSIRVFGKP-----LEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QK----------VFIFSGTFRQNLDPNGKWRDEEIWKVADQ----VGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCL 1352
Cdd:cd03235 75 QRrsidrdfpisVRDVVLMGLYGHKGLFRRLSKADKAKVDEalerVGLSELADRQIGE-----------LSGGQQQRVLL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| ABC_6TM_SUR1_D1_like |
cd18591 |
Six-transmembrane helical domain 1 (TMD1) of the sulphonylurea receptors SUR1/2; This group ... |
85-342 |
2.26e-21 |
|
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: 96.54 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 85 GVLLYLGEVTKAVQPVLLGRII----ASYDPDNTEERSIAIYL---------GIGLCLLFIVRTLLLHPAIFGLHHI--- 148
Cdd:cd18591 3 GILKLLGDLLGFVGPLCISGIVdyveENTYSSSNSTDKLSVSYvtveeffsnGYVLAVILFLALLLQATFSQASYHIvir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 149 -GMQMRIAMFSLIYKKTLKLSSRVLD--KISIGQLISLLS---NNLNKFdegLALAHFIWIAPLQVVLLMGLLWDLLQFS 222
Cdd:cd18591 83 eGIRLKTALQAMIYEKALRLSSWNLSsgSMTIGQITNHMSedaNNIMFF---FWLIHYLWAIPLKIIVGLILLYLKLGVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 223 AFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYM 302
Cdd:cd18591 160 ALIGAALILVMTPLQYLIARKLSKNQKSTLEYSDERLKKTNEMLQGIKLLKLYAWENIFLDKIQEARRKELKLLLKDAVY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 91982740 303 RFFTSSAFFFSGFFVVFLSVLPYTVINGIVLR--KIFTTISF 342
Cdd:cd18591 240 WSLMTFLTQASPILVTLVTFGLYPYLEGEPLTaaKAFSSLAL 281
|
|
| ABC_6TM_MRP5_8_9_D1 |
cd18592 |
Six-transmembrane helical domain 1 (TMD1) of multidrug resistance-associated proteins (MRPs) 5, ... |
114-365 |
2.41e-21 |
|
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: 96.09 E-value: 2.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 114 TEERSIAIYLGIGLCLLF----IVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSrvLDKISIGQLISLLSNNLN 189
Cdd:cd18592 28 LEDSDSSVWYGILLVLGLflteLLRSLFFSLTWAISYRTGIRLRGAVLGLLYKKILRLRS--LGDKSVGELINIFSNDGQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 190 KFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNI 269
Cdd:cd18592 106 RLFDAAVFGPLVIGGPVVLILGIVYSTYLLGPWALLGMLVFLLFYPLQAFIAKLTGKFRRKAIVITDKRVRLMNEILNSI 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 270 YSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSVLPYTVI-NGIVLRKIFTTISFCIVLRM 348
Cdd:cd18592 186 KLIKMYAWEKPFAKKIADIRKEERKILEKAGYLQSISISLAPIVPVIASVVTFLAHVALgNDLTAAQAFTVIAVFNSMRF 265
|
250
....*....|....*..
gi 91982740 349 SVtRQFPTAVQIWYDSL 365
Cdd:cd18592 266 SL-RMLPYAVKALAEAK 281
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1208-1412 |
2.63e-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: 94.08 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNA--ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSwnsmtLQEWRKAFGV 1284
Cdd:cd03293 3 VRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPtSGEVLVDGEP-----VTGPGPDRGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFS-GTFRQN----LDPNGKWRDEEIWKVA---DQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSV 1356
Cdd:cd03293 78 VFQQDALLPwLTVLDNvalgLELQGVPKAEARERAEellELVGLSGFENAYPHQ-----------LSGGMRQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1357 LSKAKIILLDEPSANLDPIT----YQVIRRVLRQafAGCTVVLCEHRI-EAMLDCQRFLVI 1412
Cdd:cd03293 147 AVDPDVLLLDEPFSALDALTreqlQEELLDIWRE--TGKTVLLVTHDIdEAVFLADRVVVL 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
426-622 |
4.19e-21 |
|
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: 93.30 E-value: 4.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHlclvGN---PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG-------------IIKHSGRVS 489
Cdd:cd03225 3 KNLSFSY----PDgarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGevlvdgkdltklsLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 490 F-----SSQIswIMPgTIKENIIFG-----VSYDEyRYKSVVKACQLQeDITKFAEQDNTvlgeggvTLSGGQRARISLA 559
Cdd:cd03225 79 LvfqnpDDQF--FGP-TVEEEVAFGlenlgLPEEE-IEERVEEALELV-GLEGLRDRSPF-------TLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 560 RAVYKDADLYLLDSPFGYLDVLTEEQIFEScVCKLMAS-KTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLEL-LKKLKAEgKTIIIVTHDLDLLLElADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
428-633 |
4.77e-21 |
|
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: 93.55 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV---GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSF- 490
Cdd:COG1122 1 IELENLSFSypgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkknlrelrrKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 491 ----SSQIswIMPgTIKENIIFG-----VSYDEYRyKSVVKAcqLQE-DITKFAEQDntVLgeggvTLSGGQRARISLAR 560
Cdd:COG1122 81 fqnpDDQL--FAP-TVEEDVAFGpenlgLPREEIR-ERVEEA--LELvGLEHLADRP--PH-----ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 561 AVYKDADLYLLDSPFGYLDVLTEEQIFEscvckLMAS-----KTRILVTSKMEQL-KKADKILILHEGSSYFYGTFSEL 633
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLE-----LLKRlnkegKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1201-1425 |
6.94e-21 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.73 E-value: 6.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1201 PSGGEMVVKDLTVkYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN-----IKGEIQIDgvswnsmtl 1275
Cdd:COG4178 358 SEDGALALEDLTL-RTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLL----RAIAglwpyGSGRIARP--------- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1276 QEWRKAFgvITQKVFIFSGTFRQNL---DPNGKWRDEEIWKVADQVGLksviEQFPGQLNfTLVDGGYVLSHGHKQLMCL 1352
Cdd:COG4178 424 AGARVLF--LPQRPYLPLGTLREALlypATAEAFSDAELREALEAVGL----GHLAERLD-EEADWDQVLSLGEQQRLAF 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQA 1425
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQLLPAEA 569
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
437-622 |
1.19e-20 |
|
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: 91.81 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRvsfssQISWIMPG---------------- 500
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-----DVTGVPPErrnigmvfqdyalfph 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -TIKENIIFGVsydeyrYKSVVKACQLQEDITKFAEQdntvLGEGGV------TLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:cd03259 87 lTVAENIAFGL------KLRGVPKAEIRARVRELLEL----VGLEGLlnryphELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 574 PFGYLDVLTEEQIFEScVCKLMAS--KTRILVTSKM-EQLKKADKILILHEG 622
Cdd:cd03259 157 PLSALDAKLREELREE-LKELQRElgITTIYVTHDQeEALALADRIAVMNEG 207
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1209-1427 |
1.29e-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: 92.75 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1209 KDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDGVSWNSMTLQEWRKAFG 1283
Cdd:cd03295 4 ENVTKRY-GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTT----MKMINrliepTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKVFIFSG-TFRQN--LDPN-GKWRDEEIWKVADQ----VGL--KSVIEQFPGQlnftlvdggyvLSHGHKQLMCLA 1353
Cdd:cd03295 79 YVIQQIGLFPHmTVEENiaLVPKlLKWPKEKIRERADEllalVGLdpAEFADRYPHE-----------LSGGQQQRVGVA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1354 RSVLSKAKIILLDEPSANLDPITyqviRRVLRQAFA------GCTVVLCEHRI-EAMLDCQRFLVIEQGNVWQYESLQAL 1426
Cdd:cd03295 148 RALAADPPLLLMDEPFGALDPIT----RDQLQEEFKrlqqelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
.
gi 91982740 1427 L 1427
Cdd:cd03295 224 L 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
438-633 |
1.45e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 97.78 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIKE 504
Cdd:PRK11176 356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlrdytlaslrnQVALVSQNVHLFNDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVSyDEYRYKSVVKACQL---QEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvl 581
Cdd:PRK11176 436 NIAYART-EQYSREQIEEAARMayaMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALD-- 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 582 TE-EQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK11176 513 TEsERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1208-1417 |
2.36e-20 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 91.73 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMlnIKGEIQIDGVSWNSMTLQEwRKAFGV 1284
Cdd:cd03219 3 VRGLTKRF--GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLfnlISGFLRP--TSGSVLFDGEDITGLPPHE-IARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 I-T-QKVFIFSG-TFRQNL-----------DPNGKWRDEE------IWKVADQVGLKSVIEQFPGQLnftlvdggyvlSH 1344
Cdd:cd03219 78 GrTfQIPRLFPElTVLENVmvaaqartgsgLLLARARREErearerAEELLERVGLADLADRPAGEL-----------SY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 1345 GHKQLMCLARSVLSKAKIILLDEPSANLDPI-TYQVIRRVLRQAFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEeTEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1208-1417 |
2.56e-20 |
|
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: 91.58 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQIDGVSWNSMTLQE-WRKAFGVI 1285
Cdd:COG0410 6 VENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRsGSIRFDGEDITGLPPHRiARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1286 TQKVFIFSG-TFRQNL---------DPNGKWRDEEIWkvadqvglksviEQFP------GQLnftlvdGGYvLSHGHKQL 1349
Cdd:COG0410 84 PEGRRIFPSlTVEENLllgayarrdRAEVRADLERVY------------ELFPrlkerrRQR------AGT-LSGGEQQM 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1350 MCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRlNREGVTILLVEQNARFALEiADRAYVLERGRI 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
428-605 |
3.12e-20 |
|
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: 90.62 E-value: 3.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV--GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------RVSFSSQISWIMP 499
Cdd:COG4133 3 LEAENLSCRrgERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGepirdaREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 G-------TIKENIIF-----GVSYDEYRYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDAD 567
Cdd:COG4133 83 AdglkpelTVRENLRFwaalyGLRADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLLLSPAP 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 91982740 568 LYLLDSPFGYLDVLTEEqIFESCVCKLMASKTRILVTS 605
Cdd:COG4133 152 LWLLDEPFTALDAAGVA-LLAELIAAHLARGGAVLLTT 188
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
422-582 |
5.68e-20 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 91.30 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 422 SNGENHLSFSHLCLV------GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRV--SFSSQ 493
Cdd:COG1116 2 SAAAPALELRGVSKRfptgggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPvtGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 494 ISWI------MP-GTIKENIIFGVsydeyRYKSVVKAcQLQEDITKFAEQdntvLGEGGV------TLSGGQRARISLAR 560
Cdd:COG1116 82 RGVVfqepalLPwLTVLDNVALGL-----ELRGVPKA-ERRERARELLEL----VGLAGFedayphQLSGGMRQRVAIAR 151
|
170 180
....*....|....*....|..
gi 91982740 561 AVYKDADLYLLDSPFGYLDVLT 582
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALT 173
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
437-622 |
6.14e-20 |
|
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: 88.78 E-value: 6.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII---------------KHSGRVSFSSQISWIMPG- 500
Cdd:cd03229 12 QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgedltdledelpPLRRRIGMVFQDFALFPHl 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENIIFGvsydeyryksvvkacqlqeditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03229 92 TVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 91982740 581 LTeEQIFESCVCKLMAS--KTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:cd03229 134 IT-RREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDG 177
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1219-1417 |
7.32e-20 |
|
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: 89.77 E-value: 7.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1219 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM-LNIKGEIQIDGVSWNSM---TLQEWRKAFGVITQKV-FIFS 1293
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEeLPTSGTIRVNGQDVSDLrgrAIPYLRRKIGVVFQDFrLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1294 GTFRQNL--------DPNGKWRdEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:cd03292 93 RNVYENVafalevtgVPPREIR-KRVPAALELVGLSHKHRALPAEL-----------SGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1366 DEPSANLDPITYQVIRRVLRQA-FAGCTVVLCEHRIEAMLDCQ-RFLVIEQGNV 1417
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
82-361 |
8.89e-20 |
|
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: 91.79 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 82 VFYGVLLYLGevtkavqPVLLGRIIASYDPDNTEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIY 161
Cdd:cd18596 7 VLSSVLSFAP-------PFFLNRLLRYLEDPGEDATVRPWVWVLLLFLGPLLSSLLDQQYLWIGRRLSVRLRAILTQLIF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 162 KKTLKL-------------------SSRVLDKISIGQLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFS 222
Cdd:cd18596 80 EKALRRrdksgssksseskkkdkeeDEDEKSSASVGKINNLMSVDANRISEFAAFLHLLVSAPLQIVIAIVFLYRLLGWS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 223 AFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINERLVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYM 302
Cdd:cd18596 160 ALVGLAVMVLLLPLNGYLAKRYSRAQKELMKARDARVQLVTEVLQGIRMIKFFAWERKWEERILEAREEELKWLRKRFLL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 303 RFFTSSAFFFSGFFVVFLSVLPYTVINGIVLR--KIFTTISFCIVLRMSVTR---QFPTAVQIW 361
Cdd:cd18596 240 DLLLSLLWFLIPILVTVVTFATYTLVMGQELTasVAFTSLALFNMLRGPLNVlpeLITQLLQAK 303
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
428-619 |
1.19e-19 |
|
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: 89.07 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV------GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG--------IIKHSGRVSFSSQ 493
Cdd:cd03293 1 LEVRNVSKTygggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGevlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 494 ISWIMP-GTIKENIIFGVsydeyRYKSVVKAcQLQEDITKFAEQdntvLGEGGV------TLSGGQRARISLARAVYKDA 566
Cdd:cd03293 81 QDALLPwLTVLDNVALGL-----ELQGVPKA-EARERAEELLEL----VGLSGFenayphQLSGGMRQRVALARALAVDP 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 567 DLYLLDSPFGYLDVLTEEQIFEScvckLMA-----SKTRILVT-SKMEQLKKADKILIL 619
Cdd:cd03293 151 DVLLLDEPFSALDALTREQLQEE----LLDiwretGKTVLLVThDIDEAVFLADRVVVL 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
439-622 |
2.31e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 88.56 E-value: 2.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII----------KHSGRVSF-SSQISWI------MPG- 500
Cdd:COG1136 22 TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgqdisslSERELARLrRRHIGFVfqffnlLPEl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENI-----IFGVSYDEY--RYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:COG1136 102 TALENValpllLAGVSRKERreRARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILADE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 574 PFGYLDVLTEEQIFEscvckLMAS------KTRILVTSKMEQLKKADKILILHEG 622
Cdd:COG1136 171 PTGNLDSKTGEEVLE-----LLRElnrelgTTIVMVTHDPELAARADRVIRLRDG 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1208-1417 |
2.47e-19 |
|
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: 89.41 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDGVSW-NSMTLQEWRKA 1281
Cdd:TIGR04520 3 VENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTL----AKLLNglllpTSGKVTVDGLDTlDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVitqkVF------IFSGTFR---------QNLDPngkwrdEEIWK----VADQVGLKSVIEQFPGQlnftlvdggyvL 1342
Cdd:TIGR04520 79 VGM----VFqnpdnqFVGATVEddvafglenLGVPR------EEMRKrvdeALKLVGMEDFRDREPHL-----------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1343 SHGHKQLMCLArSVLS-KAKIILLDEPSANLDPIT----YQVIRRVLRQafAGCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:TIGR04520 138 SGGQKQRVAIA-GVLAmRPDIIILDEATSMLDPKGrkevLETIRKLNKE--EGITVISITHDMEEAVLADRVIVMNKGKI 214
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1222-1417 |
2.53e-19 |
|
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: 88.68 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNL 1300
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPqGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1301 DPN-GKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQV 1379
Cdd:cd03248 109 AYGlQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQ 188
|
170 180 190
....*....|....*....|....*....|....*...
gi 91982740 1380 IRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:cd03248 189 VQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
427-588 |
2.67e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 89.54 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 427 HLSFSHLCLV------GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR----------VSF 490
Cdd:COG4525 3 MLTVRHVSVRypgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVpvtgpgadrgVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 491 ssQISWIMPG-TIKENIIFGVsydeyRYKSVVKACQLQEditkfAEQDNTVLGEGGV------TLSGGQRARISLARAVY 563
Cdd:COG4525 83 --QKDALLPWlNVLDNVAFGL-----RLRGVPKAERRAR-----AEELLALVGLADFarrriwQLSGGMRQRVGIARALA 150
|
170 180
....*....|....*....|....*
gi 91982740 564 KDADLYLLDSPFGYLDVLTEEQIFE 588
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREQMQE 175
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
428-588 |
2.70e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.37 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLC--LVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR----------VSFssQIS 495
Cdd:PRK11248 2 LQISHLYadYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKpvegpgaergVVF--QNE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 496 WIMP-GTIKENIIFG-----VSYDEYRYKS--VVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDAD 567
Cdd:PRK11248 80 GLLPwRNVQDNVAFGlqlagVEKMQRLEIAhqMLKKVGLEGAEKRYIWQ-----------LSGGQRQRVGIARALAANPQ 148
|
170 180
....*....|....*....|.
gi 91982740 568 LYLLDSPFGYLDVLTEEQIFE 588
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQT 169
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1206-1417 |
7.09e-19 |
|
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: 87.74 E-value: 7.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSM---TLQEWRKA 1281
Cdd:TIGR02315 2 LEVENLSKVY-PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPsSGSILLEGTDITKLrgkKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVITQK------------VFI----FSGTFRQNLdpnGKWRDEEIWK---VADQVGLKSVIEQFPGQLnftlvdggyvl 1342
Cdd:TIGR02315 81 IGMIFQHynlierltvlenVLHgrlgYKPTWRSLL---GRFSEEDKERalsALERVGLADKAYQRADQL----------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1343 SHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLR---QAFaGCTVVLCEHRIE-AMLDCQRFLVIEQGNV 1417
Cdd:TIGR02315 147 SGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKrinKED-GITVIINLHQVDlAKKYADRIVGLKAGEI 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1208-1395 |
8.27e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 87.84 E-value: 8.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNA--ILENISFSISPGQRVGLLGRTGSGKSTLlsafLRML-----NIKGEIQIDGVSWN------SMT 1274
Cdd:COG1116 10 LRGVSKRFPTGGGGvtALDDVSLTVAAGEFVALVGPSGCGKSTL----LRLIaglekPTSGEVLVDGKPVTgpgpdrGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1275 LQE-----WRK-----AFGVITQKVfifsgtfrqnldpNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSH 1344
Cdd:COG1116 86 FQEpallpWLTvldnvALGLELRGV-------------PKAERRERARELLELVGLAGFEDAYPHQ-----------LSG 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 1345 GHKQLMCLARSVLSKAKIILLDEPSANLDPIT----YQVIRRVLRQafAGCTVVL 1395
Cdd:COG1116 142 GMRQRVAIARALANDPEVLLMDEPFGALDALTrerlQDELLRLWQE--TGKTVLF 194
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
437-588 |
9.28e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 86.64 E-value: 9.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII----KHSGRVSFSS------------QISWIMPG 500
Cdd:COG2884 14 GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVlvngQDLSRLKRREipylrrrigvvfQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -TIKENIIF-----GVSYDEYRYK--SVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG2884 94 rTVYENVALplrvtGKSRKEIRRRvrEVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIARALVNRPELLLAD 162
|
170
....*....|....*.
gi 91982740 573 SPFGYLDVLTEEQIFE 588
Cdd:COG2884 163 EPTGNLDPETSWEIME 178
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
426-642 |
1.00e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.95 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHlclvGN--PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG----RVSFSS------- 492
Cdd:PRK13657 338 DDVSFSY----DNsrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirTVTRASlrrniav 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 493 --QISWIMPGTIKENIIFG---VSYDEYRykSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDAD 567
Cdd:PRK13657 414 vfQDAGLFNRSIEDNIRVGrpdATDEEMR--AAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 568 LYLLDSPFGYLDVLTEEQIFESCVCkLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSS 642
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDE-LMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAA 565
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
413-633 |
1.06e-18 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 92.09 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 413 QLNNDDRKTSNGE---NHLSFSHLclVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-- 487
Cdd:PRK10790 328 QYGNDDRPLQSGRidiDNVSFAYR--DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRpl 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 488 -----------VSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARI 556
Cdd:PRK10790 406 sslshsvlrqgVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 557 SLARAVYKDADLYLLDSPFGYLDVLTEEQIfESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAI-QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
436-647 |
1.33e-18 |
|
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: 86.62 E-value: 1.33e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 436 VGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-----------RVSFSSQISWIMPG-TIK 503
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkditnlppekrDISYVPQNYALFPHmTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFGVsydeyRYKSVVKAcQLQEDITKFAEQDNT--VLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 581
Cdd:cd03299 90 KNIAYGL-----KKRKVDKK-EIERKVLEIAEMLGIdhLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 582 TEEQIFESC-VCKLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSE-LQSLRPDFSSKLMGY 647
Cdd:cd03299 164 TKEKLREELkKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEvFKKPKNEFVAEFLGF 232
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
382-1411 |
1.37e-18 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 92.78 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 382 VLEYNLMFTgLVMENVTAFWE--EGFQELLEKVQL-----NNDDRKTSNGENHLSFSHLCLVGNP-----VLKNINLNIK 449
Cdd:PTZ00265 331 VLISMFMLT-IILPNITEYMKslEATNSLYEIINRkplveNNDDGKKLKDIKKIQFKNVRFHYDTrkdveIYKDLNFTLT 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 450 KGEMLAITGSTGAGKTSLLMLILGELEASEG--IIKHS------------GRVSFSSQISWIMPGTIKENIIFGV----- 510
Cdd:PTZ00265 410 EGKTYAFVGESGCGKSTILKLIERLYDPTEGdiIINDShnlkdinlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkd 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 511 --------------SYDEYRYK---------------------------------------SVVKACQLQEDITKFAEQD 537
Cdd:PTZ00265 490 lealsnyynedgndSQENKNKRnscrakcagdlndmsnttdsneliemrknyqtikdsevvDVSKKVLIHDFVSALPDKY 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 538 NTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVlTEEQIFESCVCKLMASKTRI--LVTSKMEQLKKADK 615
Cdd:PTZ00265 570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN-KSEYLVQKTINNLKGNENRItiIIAHRLSTIRYANT 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 616 ILILhegssyfygtfselqslrpdfSSKLMGYDTFDQFTEERRSSILTETLRRFSVDDASTTWNKAKQSFRQTGEF---- 691
Cdd:PTZ00265 649 IFVL---------------------SNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSYiieq 707
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 692 GE-----KRKNSILSSFSSVKKISivqkTPLSIEGESDDLQERRLSLVPDSEHGeaalprsnmitagptfpgrrrqsvld 766
Cdd:PTZ00265 708 GThdalmKNKNGIYYTMINNQKVS----SKKSSNNDNDKDSDMKSSAYKDSERG-------------------------- 757
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 767 lmtFTPSSVSSSLQRtrasirkislaprislKEEDIYSRRLSQDSTLNITEeiNEEDLKECFFDDMVKIPTVTTWNTYLR 846
Cdd:PTZ00265 758 ---YDPDEMNGNSKH----------------ENESASNKKSCKMSDENASE--NNAGGKLPFLRNLFKRKPKAPNNLRIV 816
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 847 YftlhRGLFAVLIWCVLVFL-VEVAASLFVLWLLknNPVNGGNNGTKIANTSYvvvitsSSFYYIFYIYVgvadtlLALS 925
Cdd:PTZ00265 817 Y----REIFSYKKDVTIIALsILVAGGLYPVFAL--LYAKYVSTLFDFANLEA------NSNKYSLYILV------IAIA 878
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 926 LFRGLPL---VHTLI--TASKILHRKMLHSILHAPMSTFNKLK-AGGILN-RFSKDIAILDDFLPLTIFDFIQllFIVvg 998
Cdd:PTZ00265 879 MFISETLknyYNNVIgeKVEKTMKRRLFENILYQEISFFDQDKhAPGLLSaHINRDVHLLKTGLVNNIVIFTH--FIV-- 954
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 999 aIIVVSALQPYIF---LATVPGLAVFILLRAYF----LHTSQQLKQLESEGRSPIFTH-------------LVTSLKGLW 1058
Cdd:PTZ00265 955 -LFLVSMVMSFYFcpiVAAVLTGTYFIFMRVFAirarLTANKDVEKKEINQPGTVFAYnsddeifkdpsflIQEAFYNMN 1033
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1059 TLRAFRRQTYFETLFHKALNLHTANwfmylatlrwfQMRidmifvlffivVTFISILTTGEGEGTTGIILTLAMNIMSTL 1138
Cdd:PTZ00265 1034 TVIIYGLEDYFCNLIEKAIDYSNKG-----------QKR-----------KTLVNSMLWGFSQSAQLFINSFAYWFGSFL 1091
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1139 qwAVNSSIDTDSLMRSVsrvFKFIdiqTEESICTKIMKelHSEDSPNA---------LVIK--------NEHVKKCDTWP 1201
Cdd:PTZ00265 1092 --IRRGTILVDDFMKSL---FTFL---FTGSYAGKLMS--LKGDSENAklsfekyypLIIRksnidvrdNGGIRIKNKND 1161
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1202 SGGEMVVKDLTVKYVDDGNA-ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-------------------- 1260
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqd 1241
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1261 -----------------------------------GEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDpNGK 1305
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGK 1320
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1306 WRD--EEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRV 1383
Cdd:PTZ00265 1321 EDAtrEDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1400
|
1210 1220 1230
....*....|....*....|....*....|
gi 91982740 1384 LR--QAFAGCTVVLCEHRIEAMLDCQRFLV 1411
Cdd:PTZ00265 1401 IVdiKDKADKTIITIAHRIASIKRSDKIVV 1430
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1417 |
1.62e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.35 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKST---LLSAFLRMLniKGEIQIDGVSWNSMTLQEWRKAFGV 1284
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTiskILTGLLKPQ--SGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQ---KVFIFS--------GTFRQNLDPNGKWRdeEIWKVADQVGLKSVIEQFPgqLNftlvdggyvLSHGHKQLMCLA 1353
Cdd:PRK13632 88 IFQnpdNQFIGAtveddiafGLENKKVPPKKMKD--IIDDLAKKVGMEDYLDKEP--QN---------LSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1354 rSVLS-KAKIILLDEPSANLDPI----TYQVIRRVLRQAFAgcTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:PRK13632 155 -SVLAlNPEIIIFDESTSMLDPKgkreIKKIMVDLRKTRKK--TLISITHDMDEAILADKVIVFSEGKL 220
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
936-1433 |
1.98e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 91.32 E-value: 1.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 936 LITASKI---LHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFL 1012
Cdd:TIGR00958 226 NYTMARInlrIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTM 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1013 ATVPGLAVFILLRAYF--LHTSQQLKQLESEGRSpifTHLV-TSLKGLWTLRAFRRQTYFETLFHKALN-LHTANW---- 1084
Cdd:TIGR00958 306 VTLINLPLVFLAEKVFgkRYQLLSEELQEAVAKA---NQVAeEALSGMRTVRSFAAEEGEASRFKEALEeTLQLNKrkal 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1085 --FMYLATLRWFQMRIDMIfVLFF---IVVT-------FISILTTGEGEGTTGIILtlaMNIMSTLQWAVNSSidtdslm 1152
Cdd:TIGR00958 383 ayAGYLWTTSVLGMLIQVL-VLYYggqLVLTgkvssgnLVSFLLYQEQLGEAVRVL---SYVYSGMMQAVGAS------- 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1153 rsvSRVFKFIDIQTEesictkimkelhsedSPNALVIKNEHVKkcdtwpsgGEMVVKDLTVKYVDDGNA-ILENISFSIS 1231
Cdd:TIGR00958 452 ---EKVFEYLDRKPN---------------IPLTGTLAPLNLE--------GLIEFQDVSFSYPNRPDVpVLKGLTFTLH 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1232 PGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNLDPN-GKWRDE 1309
Cdd:TIGR00958 506 PGEVVALVGPSGSGKSTVAALLQNLYQpTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGlTDTPDE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1310 EIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDpityQVIRRVLRQ--A 1387
Cdd:TIGR00958 586 EIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQEsrS 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 91982740 1388 FAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVF 1433
Cdd:TIGR00958 662 RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCY 707
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
441-628 |
2.47e-18 |
|
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: 85.42 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIK---KGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPG----------------- 500
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkiglvfqqyalfph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -TIKENIIFGVSydeyRYKSVVKACQLQEDITKFAEQDntVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03297 90 lNVRENLAFGLK----RKRNREDRISVDELLDLLGLDH--LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 580 VLTEEQIfESCVCKLMAS--KTRILVTSKMEQLKK-ADKILILHEGSSYFYG 628
Cdd:cd03297 164 RALRLQL-LPELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
428-633 |
2.51e-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: 85.25 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV----GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG---IIKHSGR---------VSFS 491
Cdd:cd03263 1 LQIRNLTKTykkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtayINGYSIRtdrkaarqsLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 492 SQISWIMPG-TIKENIIF-----GVSYDEYRYKS--VVKACQLQEDITKFAeqdntvlgeggVTLSGGQRARISLARAVY 563
Cdd:cd03263 81 PQFDALFDElTVREHLRFyarlkGLPKSEIKEEVelLLRVLGLTDKANKRA-----------RTLSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 564 KDADLYLLDSPFGYLDVLTEEQIFEsCVCKLMASKTRILVTSKM---EQLkkADKILILHEGSSYFYGTFSEL 633
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWD-LILEVRKGRSIILTTHSMdeaEAL--CDRIAIMSDGKLRCIGSPQEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1201-1421 |
3.53e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.74 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1201 PSGGEMV-VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNikGEIQIDG--VSWNSmTLQe 1277
Cdd:COG0488 310 RLGKKVLeLEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL----LKLLA--GELEPDSgtVKLGE-TVK- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 wrkaFGVITQKvfifsgtfRQNLDPNGK-WrdEEIWKVADQVGLKSVIeQFPGQLNF------TLVDggyVLSHGHKQLM 1350
Cdd:COG0488 380 ----IGYFDQH--------QEELDPDKTvL--DELRDGAPGGTEQEVR-GYLGRFLFsgddafKPVG---VLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1351 CLARSVLSKAKIILLDEPSANLDPITyqviRRVLRQA---FAGcTVVLCEH-RieAMLD--CQRFLVIEQGNVWQYE 1421
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEAlddFPG-TVLLVSHdR--YFLDrvATRILEFEDGGVREYP 511
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1448 |
4.28e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 86.33 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM-LNIKGEIQIDGVSWNSMTLQEWRKAFGVIT 1286
Cdd:PRK13647 7 VEDLHFRY-KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREVNAENEKWVRSKVGLVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKV--FIFSGTF-------RQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCLARSVL 1357
Cdd:PRK13647 86 QDPddQVFSSTVwddvafgPVNMGLDKDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1358 SKAKIILLDEPSANLDPITYQVIRRVL-RQAFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNVWQYESLQALLSEKSVFQR 1435
Cdd:PRK13647 155 MDPDVIVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIVEQA 234
|
250
....*....|...
gi 91982740 1436 ALSSSEKMKLFHG 1448
Cdd:PRK13647 235 GLRLPLVAQIFED 247
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1208-1417 |
5.08e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 85.84 E-value: 5.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:PRK13635 8 VEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTL----AKLLNglllpEAGTITVGGMVLSEETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKV-FIFSGTFRQN-----LDPNGKWRDEEIWKV---ADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLA 1353
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDdvafgLENIGVPREEMVERVdqaLRQVGMEDFLNREPHR-----------LSGGQKQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1354 RSVLSKAKIILLDEPSANLDPITYQ----VIRRVLRQafAGCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRRevleTVRQLKEQ--KGITVLSITHDLDEAAQADRVIVMNKGEI 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1227-1428 |
5.28e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 84.63 E-value: 5.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1227 SFSISPGQRVGLLGRTGSGKSTLLS---AFLRMlnIKGEIQIDGVSWN---------SMTLQEWRkafgvitqkvfIFSG 1294
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNliaGFLTP--ASGSLTLNGQDHTttppsrrpvSMLFQENN-----------LFSH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 -TFRQN----LDPNGKWRDEE---IWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:PRK10771 86 lTVAQNiglgLNPGLKLNAAQrekLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1367 EPSANLDPITYQVIRRVLRQAfagC-----TVVLCEHRIE-AMLDCQRFLVIEQGNVWQYESLQALLS 1428
Cdd:PRK10771 155 EPFSALDPALRQEMLTLVSQV---CqerqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1218-1401 |
7.10e-18 |
|
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: 83.24 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1218 DGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDG--VSWNSMTLQEWRKAFGVITQKV--FIF 1292
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRpQSGAVLIDGepLDYSRKGLLERRQRVGLVFQDPddQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1293 SGTFRQNLD--P-NGKWRDEEIWKVADQ----VGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:TIGR01166 83 AADVDQDVAfgPlNLGLSEAEVERRVREaltaVGASGLRERPTHCL-----------SGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982740 1366 DEPSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRIE 1401
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAeGMTVVISTHDVD 188
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1208-1398 |
8.27e-18 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 83.73 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTllsaFLRMLNI-----KGEIQIDGVSWNSmTLQEWRKaf 1282
Cdd:cd03262 3 IKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKST----LLRCINLleepdSGTIIIDGLKLTD-DKKNINE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 gvITQKV-FIFsgtfrQ--NLDPN--------------GKWRDEEIWKVA----DQVGLKSVIEQFPGQlnftlvdggyv 1341
Cdd:cd03262 74 --LRQKVgMVF-----QqfNLFPHltvlenitlapikvKGMSKAEAEERAlellEKVGLADKADAYPAQ----------- 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1342 LSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEH 1398
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTH 193
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1219-1398 |
8.74e-18 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 83.84 E-value: 8.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1219 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMT---LQEWRKAFGVITQKVFIFSG 1294
Cdd:TIGR02673 14 GVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTpSRGQVRIAGEDVNRLRgrqLPLLRRRIGVVFQDFRLLPD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 -TFRQNL--------DPNGKWRdEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:TIGR02673 94 rTVYENValplevrgKKEREIQ-RRVGAALRQVGLEHKADAFPEQL-----------SGGEQQRVAIARAIVNSPPLLLA 161
|
170 180 190
....*....|....*....|....*....|....
gi 91982740 1366 DEPSANLDPITYQVIRRVLRQA-FAGCTVVLCEH 1398
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLnKRGTTVIVATH 195
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1221-1440 |
1.06e-17 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 84.86 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1221 AILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTlQEWRKAFGVITQKVF--------- 1290
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKpAQGTVSFRGQDLYQLD-RKQRRAFRRDVQLVFqdspsavnp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 ------IFSGTFRQNLDPNGKWRDEEIWKVADQVGLKS-VIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKII 1363
Cdd:TIGR02769 104 rmtvrqIIGEPLRHLTSLDESEQKARIAELLDMVGLRSeDADKLPRQL-----------SGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1364 LLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSS 1440
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFKHPAGRNLQSA 252
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
428-579 |
1.41e-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: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV--GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVsfssqISWIMPG----- 500
Cdd:COG3839 4 LELENVSKSygGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLPPKdrnia 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 ------------TIKENIIFG-----VSYDEY--RYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARA 561
Cdd:COG3839 79 mvfqsyalyphmTVYENIAFPlklrkVPKAEIdrRVREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVALGRA 147
|
170
....*....|....*...
gi 91982740 562 VYKDADLYLLDSPFGYLD 579
Cdd:COG3839 148 LVREPKVFLLDEPLSNLD 165
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1206-1426 |
1.44e-17 |
|
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: 83.32 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSmTLQEWRKAFGV 1284
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSG-TFRQNLD-------PNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSV 1356
Cdd:cd03263 80 CPQFDALFDElTVREHLRfyarlkgLPKSEIKEEVELLLRVLGLTDKANKRART-----------LSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1357 LSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRI-EAMLDCQRFLVIEQGNVWQYESLQAL 1426
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMdEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
440-628 |
1.69e-17 |
|
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: 82.97 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSfssqiSWIMPG-------TIKENIIF---- 508
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS-----SLLGLGggfnpelTGRENIYLngrl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 509 -GVSYDEYRYKSvvkacqlqEDITKFAEqdntvLGEGG----VTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:cd03220 112 lGLSRKEIDEKI--------DEIIEFSE-----LGDFIdlpvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 91982740 584 EQIFESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYG 628
Cdd:cd03220 179 EKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
428-622 |
1.89e-17 |
|
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: 82.90 E-value: 1.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-------------VSFSSQI 494
Cdd:cd03248 17 VTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKpisqyehkylhskVSLVGQE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 495 SWIMPGTIKENIIFGVSYDEYryKSVVKACQ---LQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLL 571
Cdd:cd03248 97 PVLFARSLQDNIAYGLQSCSF--ECVKEAAQkahAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLIL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 572 DSPFGYLDVLTEEQIFESCVCKLmASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:cd03248 175 DEATSALDAESEQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGG 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1208-1417 |
2.03e-17 |
|
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: 82.80 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAI--LENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGEIQIDGVSWNSMTlQEWRK 1280
Cdd:cd03266 4 ADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTL----RMLAGllepdAGFATVDGFDVVKEP-AEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVITQKVFIFSG-TFRQNL----DPNGKWRDE---EIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCL 1352
Cdd:cd03266 79 RLGFVSDSTGLYDRlTARENLeyfaGLYGLKGDEltaRLEELADRLGMEELLDRRVGGF-----------STGMRQKVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRI-EAMLDCQRFLVIEQGNV 1417
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMqEVERLCDRVVVLHRGRV 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
437-622 |
2.09e-17 |
|
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: 82.69 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----------VSFSSQISWIMPG-TIKE 504
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtdlppkdrdIAMVFQNYALYPHmTVYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFG-----VSYDEY--RYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03301 92 NIAFGlklrkVPKDEIdeRVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVREPKVFLMDEPLSN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 91982740 578 LDVLTEEQIFESCVcKLMA--SKTRILVT-SKMEQLKKADKILILHEG 622
Cdd:cd03301 161 LDAKLRVQMRAELK-RLQQrlGTTTIYVThDQVEAMTMADRIAVMNDG 207
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
426-622 |
2.37e-17 |
|
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: 80.19 E-value: 2.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHLclvGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSsqiswimpgtiken 505
Cdd:cd03221 4 ENLSKTYG---GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIG-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 iifgvsydeyryksvvkacqlqeditkFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQ 585
Cdd:cd03221 67 ---------------------------YFEQ-----------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 91982740 586 I------FESCVcklmasktrILVTSKMEQLKK-ADKILILHEG 622
Cdd:cd03221 109 LeealkeYPGTV---------ILVSHDRYFLDQvATKIIELEDG 143
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1208-1415 |
2.63e-17 |
|
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: 82.26 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSmTLQEWRKAFGVIT 1286
Cdd:cd03268 3 TNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPdSGEITFDGKSYQK-NIEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSGTFRQNLDPNGK---WRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKII 1363
Cdd:cd03268 80 APGFYPNLTARENLRLLARllgIRKKRIDEVLDVVGLKDSAKKKVKG-----------FSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1364 LLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIEAM-LDCQRFLVIEQG 1415
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSlRDQGITVLISSHLLSEIqKVADRIGIINKG 202
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
437-619 |
3.99e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.13 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG--RVSFSSQIS---WIMPGTIKENIIFGV- 510
Cdd:NF040873 4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgaRVAYVPQRSevpDSLPLTVRDLVAMGRw 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 511 -------SYDEYRYKSVVKACQlQEDITKFAEQDntvLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:NF040873 84 arrglwrRLTRDDRAAVDDALE-RVGLADLAGRQ---LGE----LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 91982740 584 EQIFESCVCKLMASKTRILVTSKMEQLKKADKILIL 619
Cdd:NF040873 156 ERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1203-1417 |
4.41e-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: 4.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1203 GGEMVVKDLTV----KYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAF---LRMLNIKGEIQIDGVswnSMTL 1275
Cdd:cd03213 1 GVTLSFRNLTVtvksSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEVLINGR---PLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1276 QEWRKAFGVITQK-VFIFSGTFRQNLDPNGKwrdeeiwkvadqvgLKSvieqfpgqlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:cd03213 78 RSFRKIIGYVPQDdILHPTLTVRETLMFAAK--------------LRG-------------------LSGGERKRVSIAL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1355 SVLSKAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHR----IEAMLDcqRFLVIEQGNV 1417
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQpsseIFELFD--KLLLLSQGRV 190
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1225-1420 |
4.99e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 81.57 E-value: 4.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1225 NISFSIsPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSW----NSMTLQEWRKAFGVITQKVFIFSG-TFRQ 1298
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPdGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPHlNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1299 NL------DPNGKWRDEEIwKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPSANL 1372
Cdd:cd03297 95 NLafglkrKRNREDRISVD-ELLDLLGLDHLLNRYPAQ-----------LSGGEKQRVALARALAAQPELLLLDEPFSAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1373 DPITYQVIRRVLRQAFA--GCTVVLCEHRI-EAMLDCQRFLVIEQGNVWQY 1420
Cdd:cd03297 163 DRALRLQLLPELKQIKKnlNIPVIFVTHDLsEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
439-622 |
5.12e-17 |
|
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: 82.00 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----------VSFSSQISWIMPG-TIKENI 506
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEdatdvpvqernVGFVFQHYALFRHmTVFDNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IFGV---------SYDEYRYK--SVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:cd03296 96 AFGLrvkprserpPEAEIRAKvhELLKLVQLDWLADRYPAQ-----------LSGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 91982740 576 GYLDVLTEEQIfESCVCKLM--ASKTRILVTSKMEQ-LKKADKILILHEG 622
Cdd:cd03296 165 GALDAKVRKEL-RRWLRRLHdeLHVTTVFVTHDQEEaLEVADRVVVMNKG 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1220-1443 |
8.40e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 86.95 E-value: 8.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1220 NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLrmlnikGEIqidgvSWNSMTLQEWRKAFGVITQKVFIFSGTFRQN 1299
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAML------GEL-----SHAETSSVVIRGSVAYVPQVSWIFNATVREN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1300 LDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDP-ITYQ 1378
Cdd:PLN03232 699 ILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQ 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 1379 VIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSSEKM 1443
Cdd:PLN03232 779 VFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLMENAGKM 843
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
437-660 |
9.49e-17 |
|
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: 82.21 E-value: 9.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILgELEASEGIIKHSGrVSFSS--------------QISWIMPGTI 502
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDG-VSWNSvplqkwrkafgvipQKVFIFSGTF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENI-IFGVSYDEYRYKsVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 581
Cdd:cd03289 94 RKNLdPYGKWSDEEIWK-VAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 582 TeEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTFDQFTEERRSS 660
Cdd:cd03289 173 T-YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLFPRRNSSK 250
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1208-1384 |
9.76e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 81.75 E-value: 9.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDdgNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDG-VSWNSMTLQ-------EWR 1279
Cdd:PRK14239 8 VSDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGsIVYNGHNIYsprtdtvDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1280 KAFGVITQKVFIFSGTFRQN----LDPNGKwRDEEIWKVADQVGLK--SVIEQFPGQLNftlvDGGYVLSHGHKQLMCLA 1353
Cdd:PRK14239 86 KEIGMVFQQPNPFPMSIYENvvygLRLKGI-KDKQVLDEAVEKSLKgaSIWDEVKDRLH----DSALGLSGGQQQRVCIA 160
|
170 180 190
....*....|....*....|....*....|.
gi 91982740 1354 RSVLSKAKIILLDEPSANLDPITYQVIRRVL 1384
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
438-622 |
1.38e-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: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRV----------SFSSQISWIM--PG----- 500
Cdd:cd03257 18 VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDllklsrrlrkIRRKEIQMVFqdPMsslnp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 --TIKENIIFGVsydeYRYKSVVKACQLQEDITKFAEQ---DNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:cd03257 98 rmTIGEQIAEPL----RIHGKLSKKEARKEAVLLLLVGvglPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 576 GYLDVLTEEQIFEscvckLMAS------KTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:cd03257 174 SALDVSVQAQILD-----LLKKlqeelgLTLLFITHDLGVVAKiADRVAVMYAG 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1209-1417 |
1.46e-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: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1209 KDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSaflrMLNikGEI-QIDGvswNSMTL----------QE 1277
Cdd:COG1119 7 RNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS----LIT--GDLpPTYG---NDVRLfgerrggedvWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 WRKAFGVIT----------QKVF--IFSGTFrqnlDPNGKWR--DEEIWKVADQ----VGLKSVIEQFPGQlnftlvdgg 1339
Cdd:COG1119 76 LRKRIGLVSpalqlrfprdETVLdvVLSGFF----DSIGLYRepTDEQRERAREllelLGLAHLADRPFGT--------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1340 yvLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHRIEAMLDC-QRFLVIEQGN 1416
Cdd:COG1119 143 --LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGR 220
|
.
gi 91982740 1417 V 1417
Cdd:COG1119 221 V 221
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
440-629 |
2.12e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVS--------FSSQISwimpGtiKENIIF--- 508
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPELT----G--RENIYLngr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 509 --GVSYDEYRYKsvvkacqlQEDITKFAEqdntvLGE------GgvTLSGGQRARISLARAVYKDADLYLLDspfgylDV 580
Cdd:COG1134 115 llGLSRKEIDEK--------FDEIVEFAE-----LGDfidqpvK--TYSSGMRARLAFAVATAVDPDILLVD------EV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 581 LT----------EEQIFEscvcKLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYGT 629
Cdd:COG1134 174 LAvgdaafqkkcLARIRE----LRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
440-623 |
2.63e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 82.44 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-----------RVSFSSQ-ISWIMPGTIKENII 507
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvsrlhardrKVGFVFQhYALFRHMTVFDNIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 508 FGV---------SYDEYRYK--SVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK10851 97 FGLtvlprrerpNAAAIKAKvtQLLEMVQLAHLADRYPAQ-----------LSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 577 YLDV------------LTEEQIFescvcklmaskTRILVTSKMEQ-LKKADKILILHEGS 623
Cdd:PRK10851 166 ALDAqvrkelrrwlrqLHEELKF-----------TSVFVTHDQEEaMEVADRVVVMSQGN 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
439-622 |
2.68e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.12 E-value: 2.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSS------QISWI---------MpgTIK 503
Cdd:COG1118 16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNlpprerRVGFVfqhyalfphM--TVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFG-----VSYDEYRYKsvVKAcQLQE-DITKFAE----QdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:COG1118 94 ENIAFGlrvrpPSKAEIRAR--VEE-LLELvQLEGLADrypsQ-----------LSGGQRQRVALARALAVEPEVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 574 PFGYLD-------------VLTEEQIfescvcklmaskTRILVTSKMEQ-LKKADKILILHEG 622
Cdd:COG1118 160 PFGALDakvrkelrrwlrrLHDELGG------------TTVFVTHDQEEaLELADRVVVMNQG 210
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
440-622 |
3.55e-16 |
|
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: 79.15 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLL-----MLILGELEASEGIIKHSGRVSFSSQISWI-------M--------P 499
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLrllnrLNDLIPGAPDEGEVLLDGKDIYDLDVDVLelrrrvgMvfqkpnpfP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 GTIKENIIFGVSYDEYRYKSVVKAcqLQEDITKFAEQDNTVLGE-GGVTLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:cd03260 95 GSIYDNVAYGLRLHGIKLKEELDE--RVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 91982740 579 DVLTEEQIfESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:cd03260 173 DPISTAKI-EELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNG 216
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
441-638 |
4.61e-16 |
|
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: 79.05 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR----------VSFS--SQISWImpgTIKENIIF 508
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKqitepgpdrmVVFQnySLLPWL---TVRENIAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 509 GVsydeyryKSVVKACQLQEDITKFAEQDNTV-LGEGG----VTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:TIGR01184 78 AV-------DRVLPDLSKSERRAIVEEHIALVgLTEAAdkrpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 584 EQIFEscvcKLM-----ASKTRILVTSKM-EQLKKADKILILHEGSSYFYGTFSELQSLRP 638
Cdd:TIGR01184 151 GNLQE----ELMqiweeHRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIGQILEVPFPRP 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1208-1373 |
8.91e-16 |
|
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: 80.10 E-value: 8.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAI--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML----NIKGEIQIDGVSWNSMTLQEWRKA 1281
Cdd:COG0444 4 VRNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppgITSGEILFDGEDLLKLSEKELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVITQKVFifsgtfrQN----LDP--------------NGKWRDEEIWKVA----DQVGL---KSVIEQFPGQlnftlv 1336
Cdd:COG0444 84 RGREIQMIF-------QDpmtsLNPvmtvgdqiaeplriHGGLSKAEARERAiellERVGLpdpERRLDRYPHE------ 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982740 1337 dggyvLSHGHKQLMCLARSVLSKAKIILLDEPSANLD 1373
Cdd:COG0444 151 -----LSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
428-629 |
9.10e-16 |
|
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: 78.93 E-value: 9.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV--GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII-------KHSGRVSFSSQISWI- 497
Cdd:COG1120 2 LEAENLSVGygGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgrdlASLSRRELARRIAYVp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 498 ------MPGTIKENIIFGvsydeyRY-------------KSVVKACqLQE-DITKFAEQDNTvlgeggvTLSGGQRARIS 557
Cdd:COG1120 82 qeppapFGLTVRELVALG------RYphlglfgrpsaedREAVEEA-LERtGLEHLADRPVD-------ELSGGERQRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 558 LARAVYKDADLYLLDSPFGYLDV------------LTEEQifescvcklmaSKTRILVTSKMEQ-LKKADKILILHEGSS 624
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLahqlevlellrrLARER-----------GRTVVMVLHDLNLaARYADRLVLLKDGRI 216
|
....*
gi 91982740 625 YFYGT 629
Cdd:COG1120 217 VAQGP 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1208-1374 |
1.01e-15 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 78.11 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGEIQIDG--VSWNSMTLQEWRK 1280
Cdd:COG1126 4 IENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLL----RCINLleepdSGTITVDGedLTDSKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVitqkVFifsgtfrQ--NLDPN--------------GKWRDEEIWKVA----DQVGLKSVIEQFPGQLnftlvdggy 1340
Cdd:COG1126 78 KVGM----VF-------QqfNLFPHltvlenvtlapikvKKMSKAEAEERAmellERVGLADKADAYPAQL--------- 137
|
170 180 190
....*....|....*....|....*....|....
gi 91982740 1341 vlSHGHKQLMCLARSVLSKAKIILLDEPSANLDP 1374
Cdd:COG1126 138 --SGGQQQRVAIARALAMEPKVMLFDEPTSALDP 169
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
447-598 |
1.42e-15 |
|
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: 78.22 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 447 NIKKGEMLAITGSTGAGKTSLLMLILGELEASEG-IIKHSGRVSFSSQ-ISWIMPGTIKE---NIIFGVSYDEYRYKSVV 521
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGdIEIELDTVSYKPQyIKADYEGTVRDllsSITKDFYTHPYFKTEIA 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 522 KACQLqEDITkfaeqDNTVLgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVlteEQifescvcKLMASK 598
Cdd:cd03237 101 KPLQI-EQIL-----DREVP-----ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV---EQ-------RLMASK 156
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1219-1432 |
1.44e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.01 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1219 GNAILENISFSISPGQRVGLLGRTGSGKSTllsAFLRMLNI----KGEIQIDGVSWNSMTLQE-WRKAFGVITQKVFIFS 1293
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIvprdAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1294 G-TFRQNLDPNGKWRDEeIWKVADQVGLKSVIEQFP-GQLNFTLvdgGYVLSHGHKQLMCLARSVLSKAKIILLDEPSAN 1371
Cdd:PRK10895 92 RlSVYDNLMAVLQIRDD-LSAEQREDRANELMEEFHiEHLRDSM---GQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1372 LDPITYQVIRRVLRQAF-AGCTVVLCEHRIEAMLD-CQRFLVIEQGNVWQYESLQALLSEKSV 1432
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
424-634 |
1.59e-15 |
|
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: 77.71 E-value: 1.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 424 GENHLSFSHLCLV--GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG--------------- 486
Cdd:COG1127 2 SEPMIEVRNLTKSfgDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqditglsekelyelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 487 -RVS--------FSSqiswiMpgTIKENIIF------GVSYDEYRykSVVKAC----QLQEDITKF-AEqdntvlgeggv 546
Cdd:COG1127 82 rRIGmlfqggalFDS-----L--TVFENVAFplrehtDLSEAEIR--ELVLEKlelvGLPGAADKMpSE----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 547 tLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFE---SCVCKLMAskTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:COG1127 142 -LSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDElirELRDELGL--TSVVVTHDLDSAFAiADRVAVLADG 218
|
250
....*....|..
gi 91982740 623 SSYFYGTFSELQ 634
Cdd:COG1127 219 KIIAEGTPEELL 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
437-634 |
1.65e-15 |
|
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: 77.54 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG----------------RVS--------FSS 492
Cdd:cd03261 12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGedisglseaelyrlrrRMGmlfqsgalFDS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 493 qiswiMpgTIKENIIFGVSydEYRYKSvvkacqlQEDITKFAEQdntVLGEGGVT---------LSGGQRARISLARAVY 563
Cdd:cd03261 92 -----L--TVFENVAFPLR--EHTRLS-------EEEIREIVLE---KLEAVGLRgaedlypaeLSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 564 KDADLYLLDSPFGYLDVLTEEQIfESCVCKLMASK--TRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSELQ 634
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVI-DDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELR 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1208-1417 |
2.34e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 79.35 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAI--LENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGEIQIDGVSWNSMT---LQE 1277
Cdd:COG1135 4 LENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLI----RCINLlerptSGSVLVDGVDLTALSereLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 WRKAFGVITQKvfiF----SGTFRQN------LDpngKWRDEEIW-KVA---DQVGLKSVIEQFPGQLnftlvdggyvlS 1343
Cdd:COG1135 80 ARRKIGMIFQH---FnllsSRTVAENvalpleIA---GVPKAEIRkRVAellELVGLSDKADAYPSQL-----------S 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1344 HGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEH------RIeamldCQRFLVIEQG 1415
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHemdvvrRI-----CDRVAVLENG 217
|
..
gi 91982740 1416 NV 1417
Cdd:COG1135 218 RI 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
437-634 |
2.66e-15 |
|
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: 77.22 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRV----------SFSSQISWIMPG------ 500
Cdd:cd03256 13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDinklkgkalrQLRRQIGMIFQQfnlier 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -TIKENIIFG--------------VSYDEYRyksvvKACQLQE--DITKFAEQ--DntvlgeggvTLSGGQRARISLARA 561
Cdd:cd03256 93 lSVLENVLSGrlgrrstwrslfglFPKEEKQ-----RALAALErvGLLDKAYQraD---------QLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 562 VYKDADLYLLDSPFGYLDVLTEEQIFEscvckLMASKTR---ILVTSKMEQL----KKADKILILHEGSSYFYGTFSELQ 634
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMD-----LLKRINReegITVIVSLHQVdlarEYADRIVGLKDGRIVFDGPPAELT 233
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1222-1415 |
2.78e-15 |
|
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: 76.17 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-MLNIKGEIQIDGvswNSMTLqEWRKAFG-------------VITQ 1287
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGiILPDSGEVLFDG---KPLDI-AARNRIGylpeerglypkmkVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 KVFIFSgtfRQNLDPNGKWRDEEIWkvADQVGL----KSVIEQfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKII 1363
Cdd:cd03269 91 LVYLAQ---LKGLKKEEARRRIDEW--LERLELseyaNKRVEE---------------LSKGNQQKVQFIAAVIHDPELL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1364 LLDEPSANLDPITYQVIRRVLR-QAFAGCTVVLCEHRIEAMLD-CQRFLVIEQG 1415
Cdd:cd03269 151 ILDEPFSGLDPVNVELLKDVIReLARAGKTVILSTHQMELVEElCDRVLLLNKG 204
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
438-633 |
3.64e-15 |
|
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: 80.33 E-value: 3.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIikhSGRVSF-------------SSQISWIM------ 498
Cdd:COG1123 19 VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRI---SGEVLLdgrdllelsealrGRRIGMVFqdpmtq 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 499 --PGTIKENIIF-----GVSYDEYRYKsvVKACQLQEDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG1123 96 lnPVTVGDQIAEalenlGLSRAEARAR--VLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMALALDPDLLIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 572 DSPFGYLDVLTEEQIFEscvckLMASKTR------ILVTSKMEQ-LKKADKILILHEGSSYFYGTFSEL 633
Cdd:COG1123 167 DEPTTALDVTTQAEILD-----LLRELQRergttvLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1223-1435 |
3.67e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMT----LQEWRKAFGVITQ--KVFIFSGT 1295
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAGYHITPETgnknLKKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1296 FRQ-------NLDPNGKWRDEEIWKVADQVGLK-SVIEQFPgqlnftlvdggYVLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:PRK13641 103 VLKdvefgpkNFGFSEDEAKEKALKWLKKVGLSeDLISKSP-----------FELSGGQMRRVAIAGVMAYEPEILCLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1368 PSANLDPITyqviRRVLRQAF-----AGCTVVLCEHRIEAMLD-CQRFLVIEQGNVWQYESLQALLSEKSVFQR 1435
Cdd:PRK13641 172 PAAGLDPEG----RKEMMQLFkdyqkAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDKEWLKK 241
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
437-622 |
4.20e-15 |
|
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: 74.39 E-value: 4.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRvsfssqiswimpgtikeniifgvsydEYR 516
Cdd:cd03216 12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK--------------------------EVS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 517 YKSVVKACQLqeditkfaeqdntvlgegGVT----LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFEsCVC 592
Cdd:cd03216 66 FASPRDARRA------------------GIAmvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK-VIR 126
|
170 180 190
....*....|....*....|....*....|..
gi 91982740 593 KLMAS-KTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:cd03216 127 RLRAQgVAVIFISHRLDEVFEiADRVTVLRDG 158
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1223-1417 |
4.48e-15 |
|
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: 77.11 E-value: 4.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN--IK---GEIQIDGVSWNSMT---LQEWRKAFGVitqkVF---- 1290
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLI----QHLNglLKptsGTVTIDGRDITAKKkkkLKDLRKKVGL----VFqfpe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 --IFSGTFR-------QNLdpngKWRDEEIWKVA----DQVGL-KSVIEQFPgqlnFTLvdggyvlSHGHKQLMCLArSV 1356
Cdd:TIGR04521 93 hqLFEETVYkdiafgpKNL----GLSEEEAEERVkealELVGLdEEYLERSP----FEL-------SGGQMRRVAIA-GV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1357 LS-KAKIILLDEPSANLDPIT----YQVIRRVLRQafAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:TIGR04521 157 LAmEPEVLILDEPTAGLDPKGrkeiLDLFKRLHKE--KGLTVILVTHSMEDVAEyADRVIVMHKGKI 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
439-622 |
4.51e-15 |
|
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: 75.53 E-value: 4.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIKEN 505
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGidistipledlrsSLTIIPQDPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 IIfgvSYDEYRYKSVVKACQLQeditkfaeqdntvlgEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQ 585
Cdd:cd03369 102 LD---PFDEYSDEEIYGALRVS---------------EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982740 586 IFEScVCKLMASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:cd03369 164 IQKT-IREEFTNSTILTIAHRLRTIIDYDKILVMDAG 199
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1207-1417 |
5.66e-15 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 78.26 E-value: 5.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTvKYVDDGNAiLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMlnI-------KGEIQIDGVSWNS-MTLQEW 1278
Cdd:COG1118 4 EVRNIS-KRFGSFTL-LDDVSLEIASGELVALLGPSGSGKTTLL----RI--IagletpdSGRIVLNGRDLFTnLPPRER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1279 RKAFgvitqkVFifsgtfrQN--LDPN-------------GKWRDEEIWKVADQ----VGLKSVIEQFPGQLnftlvdgg 1339
Cdd:COG1118 76 RVGF------VF-------QHyaLFPHmtvaeniafglrvRPPSKAEIRARVEEllelVQLEGLADRYPSQL-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1340 yvlSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEH-RIEAMLDCQRFLVIEQGN 1416
Cdd:COG1118 135 ---SGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDelGGTTVFVTHdQEEALELADRVVVMNQGR 211
|
.
gi 91982740 1417 V 1417
Cdd:COG1118 212 I 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1221-1440 |
5.78e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.65 E-value: 5.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1221 AILENISFSISPGQRVGLLGRTGSGKSTLlsafLRML-----NIKGEiqidgVSWNSMTL----QEWRKAFGVITQKVF- 1290
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTL----ARLLvglesPSQGN-----VSWRGEPLaklnRAQRKAFRRDIQMVFq 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 --------------IFSGTFRQNLDPNGKWRDEEIWKVADQVGLK-SVIEQFPGQlnftlvdggyvLSHGHKQLMCLARS 1355
Cdd:PRK10419 97 dsisavnprktvreIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQ-----------LSGGQLQRVCLARA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1356 VLSKAKIILLDEPSANLD-PITYQVIRRV--LRQAFaGCTVVLCEHRIEAMLD-CQRFLVIEQGNVWQYESLQALLSEKS 1431
Cdd:PRK10419 166 LAVEPKLLILDEAVSNLDlVLQAGVIRLLkkLQQQF-GTACLFITHDLRLVERfCQRVMVMDNGQIVETQPVGDKLTFSS 244
|
....*....
gi 91982740 1432 VFQRALSSS 1440
Cdd:PRK10419 245 PAGRVLQNA 253
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1222-1419 |
6.80e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.82 E-value: 6.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRMLNiKGEIQIDGVSWNSMTLQEWRKAFgvitqkVFIFSGTFRQ- 1298
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRiiAGLEHQT-SGHIRFHGTDVSRLHARDRKVGF------VFQHYALFRHm 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1299 ----NLD-----------PNGKWRDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKII 1363
Cdd:PRK10851 90 tvfdNIAfgltvlprrerPNAAAIKAKVTQLLEMVQLAHLADRYPAQL-----------SGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1364 LLDEPSANLDPITYQVIRRVLRQ-----AFagcTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQlheelKF---TSVFVTHdQEEAMEVADRVVVMSQGNIEQ 217
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
437-632 |
7.99e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 7.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFS--SQ--------------ISWIMPG 500
Cdd:COG0488 327 DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGyfDQhqeeldpdktvldeLRDGAPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENII-----FGVSYDeyryksvvkacqlqeDITKFAEqdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:COG0488 407 GTEQEVRgylgrFLFSGD---------------DAFKPVG-----------VLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 576 GYLDVLTEEQI------FESCVcklmasktrILVTSKMEQLKK-ADKILILHEGS-SYFYGTFSE 632
Cdd:COG0488 461 NHLDIETLEALeealddFPGTV---------LLVSHDRYFLDRvATRILEFEDGGvREYPGGYDD 516
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1219-1437 |
8.47e-15 |
|
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: 76.43 E-value: 8.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1219 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDG-VSWNSmtlqewrkafgvitQKVFIFSGTF 1296
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEpSEGKIKHSGrISFSS--------------QFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1297 RQNLdPNGKWRDEEIWK-VADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPI 1375
Cdd:cd03291 115 KENI-IFGVSYDEYRYKsVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1376 T-YQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRAL 1437
Cdd:cd03291 194 TeKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
439-622 |
9.52e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 75.45 E-value: 9.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFS----------------SQISWIMP--- 499
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKrrkkflrrigvvfgqkTQLWWDLPvid 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 --GTIKEniIFGVSYDEYRyKSVVKACQLQeDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:cd03267 115 sfYLLAA--IYDLPPARFK-KRLDELSELL-DLEELLDTPVR-------QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 578 LDVLTEEQI--FESCVCKLmaSKTRILVTS----KMEQLkkADKILILHEG 622
Cdd:cd03267 184 LDVVAQENIrnFLKEYNRE--RGTTVLLTShymkDIEAL--ARRVLVIDKG 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
435-622 |
1.11e-14 |
|
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: 73.62 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 435 LVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-VSFSSQISWIMPGtikeniIFGVSYD 513
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKpVTRRSPRDAIRAG------IAYVPED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 514 eyRYKSvvkACQLQEDITkfaeqDNTVLGeggVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFEscVCK 593
Cdd:cd03215 84 --RKRE---GLVLDLSVA-----ENIALS---SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYR--LIR 148
|
170 180 190
....*....|....*....|....*....|..
gi 91982740 594 LMAS--KTRILVTSKMEQL-KKADKILILHEG 622
Cdd:cd03215 149 ELADagKAVLLISSELDELlGLCDRILVMYEG 180
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1208-1417 |
1.14e-14 |
|
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: 74.54 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQrVGLLGRTGSGKSTL---LSAFLRMlnIKGEIQIDGVSWNSMTlQEWRKAFGV 1284
Cdd:cd03264 3 LENLTKRY--GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLmriLATLTPP--SSGTIRIDGQDVLKQP-QKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSG-TFRQNLD-------PNGKWRDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSV 1356
Cdd:cd03264 77 LPQEFGVYPNfTVREFLDyiawlkgIPSKEVKARVDEVLELVNLGDRAKKKIGSL-----------SGGMRRRVGIAQAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1357 LSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:cd03264 146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKL 207
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
437-622 |
1.32e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 77.06 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVsfssqISWIMPG---------------- 500
Cdd:COG3842 17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRD-----VTGLPPEkrnvgmvfqdyalfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -TIKENIIFG-----VSYDEYRYK--SVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG3842 92 lTVAENVAFGlrmrgVPKAEIRARvaELLELVGLEGLADRYPHQ-----------LSGGQQQRVALARALAPEPRVLLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 573 SPFGYLDV-LTEEQIFEscVCKLMAS--KTRILVT-SKMEQLKKADKILILHEG 622
Cdd:COG3842 161 EPLSALDAkLREEMREE--LRRLQRElgITFIYVThDQEEALALADRIAVMNDG 212
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1206-1375 |
1.63e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.07 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM------LNIKGEIQIDG--VSWNSMTLQE 1277
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgARVEGEILLDGedIYDPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 WRKAFGVITQKVFIFSGTFRQN----LDPNGKWRDEEI-------------WK-VADQvgLKsvieqfpgqlnftlvDGG 1339
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNvaygLRLHGIKSKSELdeiveeslrkaalWDeVKDR--LK---------------KSA 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 91982740 1340 YVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPI 1375
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPI 188
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1222-1420 |
1.64e-14 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 74.66 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGEIQIDGVSW------NSMTLQEWRKAFGVITQKVF 1290
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLL----RVLNLletpdSGQLNIAGHQFdfsqkpSEKAIRLLRQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 IFSG-TFRQNL--------DPNGKWRDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAK 1361
Cdd:COG4161 93 LWPHlTVMENLieapckvlGLSKEQAREKAMKLLARLRLTDKADRFPLHL-----------SGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1362 IILLDEPSANLDP-ITYQVIRRVLRQAFAGCTVVLCEHRIE-AMLDCQRFLVIEQGNVWQY 1420
Cdd:COG4161 162 VLLFDEPTAALDPeITAQVVEIIRELSQTGITQVIVTHEVEfARKVASQVVYMEKGRIIEQ 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
1208-1399 |
1.76e-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: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVkYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN-----IKGEIQIDGVSwNSMtlqewrkaF 1282
Cdd:cd03223 3 LENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLF----RALAglwpwGSGRIGMPEGE-DLL--------F 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 gvITQKVFIFSGTFRQnldpngkwrdeeiwkvadqvglksvieqfpgQLNFTLVDggyVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:cd03223 69 --LPQRPYLPLGTLRE-------------------------------QLIYPWDD---VLSGGEQQRLAFARLLLHKPKF 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982740 1363 ILLDEPSANLDPITYQVIRRVLRQafAGCTVVLCEHR 1399
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1222-1428 |
1.96e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.74 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNI-----KGEIQIDGVSWN--SMTLQEWRKAFGVITQKVFIFSG 1294
Cdd:PRK09493 16 VLHNIDLNIDQGEVVVIIGPSGSGKSTLL----RCINKleeitSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 -TFRQN-----LDPNGKWRdEEIWKVA----DQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:PRK09493 92 lTALENvmfgpLRVRGASK-EEAEKQArellAKVGLAERAHHYPSEL-----------SGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1365 LDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIE-AMLDCQRFLVIEQGNVWQYESLQALLS 1428
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1208-1415 |
1.99e-14 |
|
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: 74.39 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTvKYVDDGNA---ILENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRmLNIKGEIQIDGVSWNSMTlQEWRKAF 1282
Cdd:COG4181 11 LRGLT-KTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGllAGLD-RPTSGTVRLAGQDLFALD-EDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 -GvitQKV-FIF-------SGTFRQNL--------DPNGKWRDEEIwkvADQVGLKSVIEQFPGQlnftlvdggyvLSHG 1345
Cdd:COG4181 88 rA---RHVgFVFqsfqllpTLTALENVmlplelagRRDARARARAL---LERVGLGHRLDHYPAQ-----------LSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1346 HKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEHRIEAMLDCQRFLVIEQG 1415
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAG 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1223-1432 |
2.01e-14 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 74.53 E-value: 2.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RMLNIKGEIQIDG---VSWNsmTLQEWRKAFGVITQKVFIFSG-TFR 1297
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCgDPRATSGRIVFDGkdiTDWQ--TAKIMREAVAIVPEGRRVFSRmTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1298 QNLDPNGKWRDEEIWkvadQVGLKSVIEQFPgQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITY 1377
Cdd:PRK11614 99 ENLAMGGFFAERDQF----QERIKWVYELFP-RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1378 QVIRRVLRQAFA-GCTVVLCEHRI-EAMLDCQRFLVIEQGNVWQYESLQALLSEKSV 1432
Cdd:PRK11614 174 QQIFDTIEQLREqGMTIFLVEQNAnQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1206-1400 |
2.85e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 74.75 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVddGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRM------LNIKGEIQIDGVS-WNSMTLQEW 1278
Cdd:PRK14271 22 MAAVNLTLGFA--GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMndkvsgYRYSGDVLLGGRSiFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1279 RKAFGVITQKVFIF---------SGTFRQNLDPNGKWRDEEIWKVAdQVGLKSVIEQfpgqlnfTLVDGGYVLSHGHKQL 1349
Cdd:PRK14271 100 RRRVGMLFQRPNPFpmsimdnvlAGVRAHKLVPRKEFRGVAQARLT-EVGLWDAVKD-------RLSDSPFRLSGGQQQL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1350 MCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRI 1400
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNL 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
437-623 |
2.88e-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: 73.81 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----------VSFSSQISWIMPG-TIKE 504
Cdd:cd03300 12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKditnlpphkrpVNTVFQNYALFPHlTVFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVsydeyRYKSVVKACQLQE-----DITKFAEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03300 92 NIAFGL-----RLKKLPKAEIKERvaealDLVQLEGYANRKPSQ----LSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 91982740 580 V-LTEEQIFESCVCKLMASKTRILVTSKMEQ-LKKADKILILHEGS 623
Cdd:cd03300 163 LkLRKDMQLELKRLQKELGITFVFVTHDQEEaLTMSDRIAVMNKGK 208
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1222-1417 |
3.19e-14 |
|
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: 73.73 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLlsaFLRMLNI----KGEIQIDGVSWNSMTL-QEWRKAFGVITQKVFIFSG-T 1295
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTT---FYMIVGLvkpdSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1296 FRQNL--------DPNGKWRDEeiwkvadqvgLKSVIEQFpgQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03218 92 VEENIlavleirgLSKKEREEK----------LEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1368 PSANLDPITYQVIRRVLRQ-AFAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSiTDRAYIIYEGKV 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1225-1419 |
3.37e-14 |
|
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: 74.60 E-value: 3.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1225 NISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN--IK---GEIQIDGVSWNSMT---LQEWR-KAFGVITQKVFIFSG- 1294
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTL----LRCINrlIEptsGKVLIDGQDIAAMSrkeLRELRrKKISMVFQSFALLPHr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 TFRQN----LDPNG---KWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03294 118 TVLENvafgLEVQGvprAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1368 PSANLDPItyqvIRR-----VLR-QAFAGCTVVLCEHR-IEAMLDCQRFLVIEQGNVWQ 1419
Cdd:cd03294 187 AFSALDPL----IRRemqdeLLRlQAELQKTIVFITHDlDEALRLGDRIAIMKDGRLVQ 241
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1201-1417 |
3.44e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 74.33 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1201 PSGGEMVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN----------IKG-----EIQI 1265
Cdd:PRK11247 8 NQGTPLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLL----RLLAgletpsagelLAGtaplaEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1266 DgvswNSMTLQE-----WRKafgVITQkvfifsgtfrQNLDPNGKWRDEEIwKVADQVGLKSVIEQFPGqlnftlvdggy 1340
Cdd:PRK11247 82 D----TRLMFQDarllpWKK---VIDN----------VGLGLKGQWRDAAL-QALAAVGLADRANEWPA----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1341 VLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPIT----YQVIRRVLRQafAGCTVVLCEHRI-EAMLDCQRFLVIEQG 1415
Cdd:PRK11247 133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTriemQDLIESLWQQ--HGFTVLLVTHDVsEAVAMADRVLLIEEG 210
|
..
gi 91982740 1416 NV 1417
Cdd:PRK11247 211 KI 212
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1205-1417 |
3.47e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 74.28 E-value: 3.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1205 EMVVKDLTVKYVDDgnAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQIDGVSWNSMTLQEWRKAFG 1283
Cdd:PRK11231 2 TLRTENLTVGYGTK--RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKVFIFSGTFRQNLDPNGK------W-----RDEEIWKVADQvglKSVIEQFPGQLnftLVDggyvLSHGHKQLMCL 1352
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAYGRspwlslWgrlsaEDNARVNQAME---QTRINHLADRR---LTD----LSGGQRQRAFL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDpITYQV-IRRVLRQ-AFAGCTVVLCEHRI-EAMLDCQRFLVIEQGNV 1417
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLD-INHQVeLMRLMRElNTQGKTVVTVLHDLnQASRYCDHLVVLANGHV 216
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
1206-1398 |
3.79e-14 |
|
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: 73.20 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLqewrKAFGV 1284
Cdd:TIGR03740 1 LETKNLSKRF--GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRpTSGEIIFDGHPWTRKDL----HKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSG-TFRQNLDPNGKWR---DEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKA 1360
Cdd:TIGR03740 75 LIESPPLYENlTARENLKVHTTLLglpDSRIDEVLNIVDLTNTGKKKAKQF-----------SLGMKQRLGIAIALLNHP 143
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 91982740 1361 KIILLDEPSANLDPITYQVIRRVLRqAFA--GCTVVLCEH 1398
Cdd:TIGR03740 144 KLLILDEPTNGLDPIGIQELRELIR-SFPeqGITVILSSH 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1208-1415 |
4.23e-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: 71.69 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAflrmlnIKGEIQIDGvswnsmtlqewrkafGVITq 1287
Cdd:cd03216 3 LRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKI------LSGLYKPDS---------------GEIL- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 kvfiFSGTFRQNLDPngkwRDeeiwkvADQVGLKSVieqfpgqlnftlvdggYVLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03216 59 ----VDGKEVSFASP----RD------ARRAGIAMV----------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 91982740 1368 PSANLDPI-TYQVIRRVLRQAFAGCTVVLCEHRI-EAMLDCQRFLVIEQG 1415
Cdd:cd03216 109 PTAALTPAeVERLFKVIRRLRAQGVAVIFISHRLdEVFEIADRVTVLRDG 158
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
858-1109 |
4.31e-14 |
|
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: 74.51 E-value: 4.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 858 LIWCVLVFLVEVAASLFVLWLLKnnpvnggnngtkiantsYVV--VITSSSFYYIFYIYVGVADTLLALSLFRGLPLVHT 935
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTK-----------------LLIddVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 936 LITASKILH---RKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFL 1012
Cdd:cd07346 64 ARLGQRVVFdlrRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1013 ATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHTANWFMYLATLR 1092
Cdd:cd07346 144 VALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA 223
|
250
....*....|....*..
gi 91982740 1093 WFQMRIDMIFVLFFIVV 1109
Cdd:cd07346 224 LFSPLIGLLTALGTALV 240
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1208-1415 |
5.21e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 70.56 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAflrmlnIKGEIQIDGvswnsmtlqewrkafGVITQ 1287
Cdd:cd03221 3 LENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKL------IAGELEPDE---------------GIVTW 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 KVFIFSGTFRQnldpngkwrdeeiwkvadqvglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03221 60 GSTVKIGYFEQ-------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1368 PSANLDPITYQVIRRVLrQAFAGcTVVLCEH-RieAMLD--CQRFLVIEQG 1415
Cdd:cd03221 97 PTNHLDLESIEALEEAL-KEYPG-TVILVSHdR--YFLDqvATKIIELEDG 143
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1205-1419 |
5.84e-14 |
|
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: 73.14 E-value: 5.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1205 EMVVKDLTVKYvddGNAI-LENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRMLNiKGEIQIDGVSWNSMTLQEwrKA 1281
Cdd:cd03296 2 SIEVRNVSKRF---GDFVaLDDVSLDIPSGELVALLGPSGSGKTTLLRliAGLERPD-SGTILFGGEDATDVPVQE--RN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVITQKVFIFSG-TFRQNL-----------DPNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQL 1349
Cdd:cd03296 76 VGFVFQHYALFRHmTVFDNVafglrvkprseRPPEAEIRAKVHELLKLVQLDWLADRYPAQ-----------LSGGQRQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1350 MCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAF--AGCTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:cd03296 145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHdeLHVTTVFVTHdQEEALEVADRVVVMNKGRIEQ 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1436 |
6.55e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.11 E-value: 6.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDG--VSWNSMTLQEWRKAFGV 1284
Cdd:PRK13636 8 VEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGkpIDYSRKGLMKLRESVGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKV--FIFSGTFRQNLD---PNGKWRDEEIWKVADQVGLKSVIEQFPGQLNftlvdggYVLSHGHKQLMCLARSVLSK 1359
Cdd:PRK13636 87 VFQDPdnQLFSASVYQDVSfgaVNLKLPEDEVRKRVDNALKRTGIEHLKDKPT-------HCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1360 AKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHRIEAM-LDCQRFLVIEQGNVWQYESLQALLSEKSVFQRA 1436
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKV 239
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1227-1417 |
1.13e-13 |
|
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: 71.76 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1227 SFSISPGQRVGLLGRTGSGKSTLL---SAFLrmLNIKGEIQIDGVSWNSMTLQEwrKAFGVITQKVFIFSG-TFRQNLD- 1301
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLnliAGFE--TPQSGRVLINGVDVTAAPPAD--RPVSMLFQENNLFAHlTVEQNVGl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1302 ---PNGKWRDEE---IWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPSANLDPI 1375
Cdd:cd03298 94 glsPGLKLTAEDrqaIEVALARVGLAGLEKRLPGEL-----------SGGERQRVALARVLVRDKPVLLLDEPFAALDPA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 91982740 1376 ----TYQVIRRVLRQafAGCTVVLCEHRIE--AMLDcQRFLVIEQGNV 1417
Cdd:cd03298 163 lraeMLDLVLDLHAE--TKMTVLMVTHQPEdaKRLA-QRVVFLDNGRI 207
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
433-621 |
1.50e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 71.36 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 433 LCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASegiIKHSGRVSFSSQISWIMP------G------ 500
Cdd:COG4136 9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPA---FSASGEVLLNGRRLTALPaeqrriGilfqdd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 ------TIKENIIFGVSYD---EYRYKSVVKAcqLQE-DITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYL 570
Cdd:COG4136 86 llfphlSVGENLAFALPPTigrAQRRARVEQA--LEEaGLAGFADRDPA-------TLSGGQRARVALLRALLAEPRALL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 571 LDSPFGYLDVLTEEQIFESCVCKLmasKTR----ILVTSKMEQLKKADKILILHE 621
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVFEQI---RQRgipaLLVTHDEEDAPAAGRVLDLGN 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1203-1437 |
1.59e-13 |
|
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: 76.14 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1203 GGEMVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RMLNIKGEIQIDGvswnsmtlqewrkA 1281
Cdd:TIGR00957 634 GNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLaEMDKVEGHVHMKG-------------S 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVITQKVFIFSGTFRQNLdPNGKWRDEEIWK-VADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKA 1360
Cdd:TIGR00957 701 VAYVPQQAWIQNDSLRENI-LFGKALNEKYYQqVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNA 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1361 KIILLDEPSANLDP-ITYQVIRRVL--RQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRAL 1437
Cdd:TIGR00957 780 DIYLFDDPLSAVDAhVGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFL 859
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
448-599 |
1.64e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 75.23 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 448 IKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQ-ISWIMPGTIKENI-----IFGVSYdeyrYKS-V 520
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISYKPQyIKPDYDGTVEDLLrsitdDLGSSY----YKSeI 437
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 521 VKACQLqEDITkfaeqDNTVlgeggVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVlteEQifescvcKLMASKT 599
Cdd:PRK13409 438 IKPLQL-ERLL-----DKNV-----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV---EQ-------RLAVAKA 495
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1223-1443 |
1.67e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.93 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLrmlnikGEIQidGVSWNSMTLqewRKAFGVITQKVFIFSGTFRQNLDP 1302
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAML------GELP--PRSDASVVI---RGTVAYVPQVSWIFNATVRDNILF 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1303 NGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDP-ITYQVIR 1381
Cdd:PLN03130 702 GSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFD 781
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1382 RVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRALSSSEKM 1443
Cdd:PLN03130 782 KCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKM 843
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1208-1446 |
1.75e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 1.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDG--------VSWNSMTLQEWR 1279
Cdd:PRK14258 10 VNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGrveffnqnIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1280 KAFGVITQKVFIFSGTFRQNLDPNGK---WR--------------DEEIWKVADQVGLKSVIEqfpgqlnftlvdggyvL 1342
Cdd:PRK14258 88 RQVSMVHPKPNLFPMSVYDNVAYGVKivgWRpkleiddivesalkDADLWDEIKHKIHKSALD----------------L 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1343 SHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAF--AGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQY 1420
Cdd:PRK14258 152 SGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGNENRI 231
|
250 260
....*....|....*....|....*.
gi 91982740 1421 ESLQALLSEKSVFQRALSSSEKMKLF 1446
Cdd:PRK14258 232 GQLVEFGLTKKIFNSPHDSRTREYVL 257
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
437-579 |
1.76e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----------VSFSSQISWIMPG-TIKE 504
Cdd:PRK09452 26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQdithvpaenrhVNTVFQSYALFPHmTVFE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFG-----VSYDEY--RYKSVVKACQLQEditkFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK09452 106 NVAFGlrmqkTPAAEItpRVMEALRMVQLEE----FAQRKPH-------QLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
..
gi 91982740 578 LD 579
Cdd:PRK09452 175 LD 176
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
427-580 |
1.79e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 70.99 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 427 HLSFSHL-CLVGNPVL-KNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIK------HSGRVSFSSQISWI- 497
Cdd:PRK13538 1 MLEARNLaCERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepiRRQRDEYHQDLLYLg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 498 -MPGtIK------ENIIFgvsydeyryksvvkACQLQEDITKFAEQDntVLGEGGV---------TLSGGQRARISLARA 561
Cdd:PRK13538 81 hQPG-IKteltalENLRF--------------YQRLHGPGDDEALWE--ALAQVGLagfedvpvrQLSAGQQRRVALARL 143
|
170
....*....|....*....
gi 91982740 562 VYKDADLYLLDSPFGYLDV 580
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDK 162
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1208-1401 |
1.79e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 72.42 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsaFLRMLNI----KGEIQIDG--VSWNSMTLQEWRKA 1281
Cdd:PRK13639 4 TRDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTL---FLHFNGIlkptSGEVLIKGepIKYDKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVITQKV--FIFSGTFRQNL--DP-NGKWRDEEIWK-VAD---QVGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCL 1352
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVafGPlNLGLSKEEVEKrVKEalkAVGMEGFENKPP-----------HHLSGGQKKRVAI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAF-AGCTVVLCEHRIE 1401
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkEGITIIISTHDVD 198
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
431-632 |
1.81e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 72.77 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 431 SHLCLVGNP----VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII------------------KHSGRV 488
Cdd:PRK13637 9 THIYMEGTPfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvklsdirKKVGLV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 489 sFSSQISWIMPGTIKENIIFGVS----YDEYRYKSVVKACQLQE-DITKFAEQDNtvlgeggVTLSGGQRARISLARAVY 563
Cdd:PRK13637 89 -FQYPEYQLFEETIEKDIAFGPInlglSEEEIENRVKRAMNIVGlDYEDYKDKSP-------FELSGGQKRRVAIAGVVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 564 KDADLYLLDSPFGYLDVLTEEQIFEScvCKLMASK---TRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSE 632
Cdd:PRK13637 161 MEPKILILDEPTAGLDPKGRDEILNK--IKELHKEynmTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1218-1432 |
1.97e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 72.33 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1218 DGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLniKGEIQIDGVSWNSMT-LQEWRKAFGVITQKVFI-F 1292
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLalhLNGLLRPQ--KGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPETqF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1293 SG-TFRQNL---DPNGKWRDEEIWKVAD----QVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:PRK13644 91 VGrTVEEDLafgPENLCLPPIEIRKRVDralaEIGLEKYRHRSPKT-----------LSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1365 LDEPSANLDPITYQ-VIRRVLRQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSV 1432
Cdd:PRK13644 160 FDEVTSMLDPDSGIaVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSL 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1220-1430 |
2.26e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 2.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1220 NAILENISFSISPGQRVGLLGRTGSGKSTLLSaflrmlNIKGEIQIDGVSWNSMTL---------------QEWRKAFGV 1284
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLR------HLSGLITGDKSAGSHIELlgrtvqregrlardiRKSRANTGY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQ------KVFIFSGTFRQNLDPNGKWRDEEIW--KVADQVGLKSVIEQFPGQLNFTLVDggyVLSHGHKQLMCLARSV 1356
Cdd:PRK09984 91 IFQqfnlvnRLSVLENVLIGALGSTPFWRTCFSWftREQKQRALQALTRVGMVHFAHQRVS---TLSGGQQQRVAIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1357 LSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEHRIE-AMLDCQRFLVIEQGNVWQYESLQALLSEK 1430
Cdd:PRK09984 168 MQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
428-633 |
2.29e-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: 71.65 E-value: 2.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV--GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG-----------------IIKHSGRV 488
Cdd:COG1119 4 LELRNVTVRrgGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvrlfgerrggedvweLRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 489 SfSSQISWIMPGTIKENII----FGVS--YDEYRYKSVVKACQLQE--DITKFAEQDntvLGeggvTLSGGQRARISLAR 560
Cdd:COG1119 84 S-PALQLRFPRDETVLDVVlsgfFDSIglYREPTDEQRERARELLEllGLAHLADRP---FG----TLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 561 AVYKDADLYLLDSPFGYLDVLTEEQIFEScVCKLMAS--KTRILVTSKMEQLKKA-DKILILHEGSSYFYGTFSEL 633
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLAL-LDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPKEEV 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
437-662 |
2.35e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 73.72 E-value: 2.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----------VSFSSQISWIMPG-TIKE 504
Cdd:PRK11607 31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVdlshvppyqrpINMMFQSYALFPHmTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVSYDEY-------RYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK11607 111 NIAFGLKQDKLpkaeiasRVNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 578 LDVLTEEQIFESCVCKL-MASKTRILVTSKMEQ-LKKADKILILHEGSSYFYGTFSELQSlRPD--FSSKLMG-YDTFDQ 652
Cdd:PRK11607 180 LDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEIYE-HPTtrYSAEFIGsVNVFEG 258
|
250
....*....|
gi 91982740 653 FTEERRSSIL 662
Cdd:PRK11607 259 VLKERQEDGL 268
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1208-1419 |
2.59e-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: 73.21 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMlnI-------KGEIQIDGVSWNSmtLQEWRK 1280
Cdd:COG3842 8 LENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRM--IagfetpdSGRILLDGRDVTG--LPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVitqkVFifsgtfrQN--LDPN-------------GKWRDEEIW-KVA---DQVGLKSVIEQFPGQlnftlvdggyv 1341
Cdd:COG3842 78 NVGM----VF-------QDyaLFPHltvaenvafglrmRGVPKAEIRaRVAellELVGLEGLADRYPHQ----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1342 LSHGHKQLMCLARSVLSKAKIILLDEPSANLDP----ITYQVIRRVLRQafAGCTVVLCEH-RIEAMLDCQRFLVIEQGN 1416
Cdd:COG3842 136 LSGGQQQRVALARALAPEPRVLLLDEPLSALDAklreEMREELRRLQRE--LGITFIYVTHdQEEALALADRIAVMNDGR 213
|
...
gi 91982740 1417 VWQ 1419
Cdd:COG3842 214 IEQ 216
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
437-580 |
3.00e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 74.33 E-value: 3.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG-IIKHSG-RVSFSSQISWIMPG-TIKENIIFGVS-- 511
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGeVSIPKGlRIGYLPQEPPLDDDlTVLDTVLDGDAel 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 512 ---YDEYRY------KSVVKACQLQEDITKFAEQD--------NTVLGEGGV----------TLSGGQRARISLARAVYK 564
Cdd:COG0488 90 ralEAELEEleaklaEPDEDLERLAELQEEFEALGgweaearaEEILSGLGFpeedldrpvsELSGGWRRRVALARALLS 169
|
170
....*....|....*.
gi 91982740 565 DADLYLLDSPFGYLDV 580
Cdd:COG0488 170 EPDLLLLDEPTNHLDL 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1206-1398 |
3.76e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 71.10 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvddGNA-ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN------IKGEIQIDGVSWNSMTLQEW 1278
Cdd:PRK14247 4 IEIRDLKVSF---GQVeVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1279 RKAFGVITQ------KVFIFSG-TFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDggyvLSHGHKQLMC 1351
Cdd:PRK14247 81 RRRVQMVFQipnpipNLSIFENvALGLKLNRLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGK----LSGGQQQRLC 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 91982740 1352 LARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEH 1398
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTH 203
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1223-1417 |
3.87e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 71.62 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGV--SWNSMTLQEWRKAFGVITQ--KVFIFSGTFR 1297
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVdiTDKKVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1298 QNLD---PNGKWRDEEI----WKVADQVGLKsvIEQFPGQLNFTlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPSA 1370
Cdd:PRK13637 103 KDIAfgpINLGLSEEEIenrvKRAMNIVGLD--YEDYKDKSPFE-------LSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1371 NLDP-----ITYQVirRVLRQAFaGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:PRK13637 174 GLDPkgrdeILNKI--KELHKEY-NMTIILVSHSMEDVAKlADRIIVMNKGKC 223
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1206-1417 |
3.90e-13 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 70.77 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKST---LLSAFLRmlNIKGEIQIDGVSWNSMTLQE-WRKA 1281
Cdd:TIGR04406 2 LVAENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsfyMIVGLVR--PDAGKILIDGQDITHLPMHErARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVITQKVFIFSG-TFRQNL--------DPNGKWRDEEIWKVADQVGLKSVIEQfpgqlnftlvdGGYVLSHGHKQLMCL 1352
Cdd:TIGR04406 78 IGYLPQEASIFRKlTVEENImavleirkDLDRAEREERLEALLEEFQISHLRDN-----------KAMSLSGGERRRVEI 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDPITYQVIRRV---LRQafAGCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:TIGR04406 147 ARALATNPKFILLDEPFAGVDPIAVGDIKKIikhLKE--RGIGVLITDHNVRETLDiCDRAYIISDGKV 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1219-1415 |
4.34e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1219 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTlQEWRKAFGVITQkvfiFSG--- 1294
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPdAGKITVLGVPVPARA-RLARARIGVVPQ----FDNldl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 --TFRQNLDPNGKW---RDEEIWKVadqvgLKSVIE--QFPGQLNFTLVDggyvLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:PRK13536 128 efTVRENLLVFGRYfgmSTREIEAV-----IPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 91982740 1368 PSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRI-EAMLDCQRFLVIEQG 1415
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLArGKTILLTTHFMeEAERLCDRLCVLEAG 248
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
440-628 |
5.34e-13 |
|
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: 69.62 E-value: 5.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWI--MPG--------TIKENIIF- 508
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgyLPEerglypkmKVIDQLVYl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 509 ----GVSYDEYRYksvvkacQLQEDITKF--AEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03269 95 aqlkGLKKEEARR-------RIDEWLERLelSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 91982740 583 EEqIFESCVCKLMAS-KTRILVTSKMEQLKK-ADKILILHEGSSYFYG 628
Cdd:cd03269 164 VE-LLKDVIRELARAgKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1208-1417 |
6.28e-13 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 73.30 E-value: 6.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSaFLRML----NIKGEI----------------QIDG 1267
Cdd:TIGR03269 3 VKNLTKKF--DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMH-VLRGMdqyePTSGRIiyhvalcekcgyverpSKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1268 ----VSWNSMTLQE---W----------RKAFGVITQKVFIFSGTFR------QNLDPNGKWRDEEIWKVADqvglksVI 1324
Cdd:TIGR03269 80 epcpVCGGTLEPEEvdfWnlsdklrrriRKRIAIMLQRTFALYGDDTvldnvlEALEEIGYEGKEAVGRAVD------LI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1325 EQFpgQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAF--AGCTVVLCEHRIEA 1402
Cdd:TIGR03269 154 EMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEV 231
|
250
....*....|....*.
gi 91982740 1403 MLD-CQRFLVIEQGNV 1417
Cdd:TIGR03269 232 IEDlSDKAIWLENGEI 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1220-1417 |
6.72e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 70.04 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1220 NAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNI-----KGEIQIDGVSW------NSMTLQEWRKAFGVITQK 1288
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSL----LRVLNLlemprSGTLNIAGNHFdfsktpSDKAIRELRRNVGMVFQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1289 VFIFSG-TFRQNL-----------DPNGKWRDEEIWKvadQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSV 1356
Cdd:PRK11124 91 YNLWPHlTVQQNLieapcrvlglsKDQALARAEKLLE---RLRLKPYADRFPLH-----------LSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1357 LSKAKIILLDEPSANLDP-ITYQVIRRVLRQAFAGCTVVLCEHRIE-AMLDCQRFLVIEQGNV 1417
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPeITAQIVSIIRELAETGITQVIVTHEVEvARKTASRVVYMENGHI 219
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
439-633 |
6.90e-13 |
|
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: 69.92 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGeLEA-SEGIIKHSGR----------VSFSSQISWIMPG------- 500
Cdd:cd03258 19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCING-LERpTSGSVLVDGTdltllsgkelRKARRRIGMIFQHfnllssr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENI-----IFGVSyDEYRYKSV---VKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:cd03258 98 TVFENValpleIAGVP-KAEIEERVlelLELVGLEDKADAYPAQ-----------LSGGQKQRVGIARALANNPKVLLCD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 573 SPFGYLDVLTEEQIFE---SCVCKLmaSKTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:cd03258 166 EATSALDPETTQSILAllrDINREL--GLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
404-588 |
7.45e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 72.92 E-value: 7.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 404 GFQELLEKVQLNNDD--RKTSNGENHLSFSHLCLV---GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEAS 478
Cdd:COG4178 337 GFEEALEAADALPEAasRIETSEDGALALEDLTLRtpdGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 479 EGIIKH--SGRVSFSSQISWIMPGTIKENIIF---GVSYDEYRYKSVVKACQLQEDITKFAEQDNTvlgegGVTLSGGQR 553
Cdd:COG4178 417 SGRIARpaGARVLFLPQRPYLPLGTLREALLYpatAEAFSDAELREALEAVGLGHLAERLDEEADW-----DQVLSLGEQ 491
|
170 180 190
....*....|....*....|....*....|....*
gi 91982740 554 ARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFE 588
Cdd:COG4178 492 QRLAFARLLLHKPDWLFLDEATSALDEENEAALYQ 526
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
440-628 |
7.56e-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: 69.32 E-value: 7.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------------RVSFSSQISWIMPG-TIKENI 506
Cdd:cd03266 20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkepaearrRLGFVSDSTGLYDRlTARENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IF-----GVSYDEY--RYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03266 100 EYfaglyGLKGDELtaRLEELADRLGMEELLDRRVGG-----------FSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 91982740 580 VLTEEQIFESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYG 628
Cdd:cd03266 169 VMATRALREFIRQLRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1206-1428 |
8.36e-13 |
|
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: 69.67 E-value: 8.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvddGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVswNSMTLQEWRKAFGV 1284
Cdd:cd03299 1 LKVENLSKDW---KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKpDSGKILLNGK--DITNLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSG-TFRQNLD-------PNGKWRDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSV 1356
Cdd:cd03299 76 VPQNYALFPHmTVYKNIAyglkkrkVDKKEIERKVLEIAEMLGIDHLLNRKPETL-----------SGGEQQRVAIARAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 1357 LSKAKIILLDEPSANLDPITYQVIRRVLRQAF--AGCTVVLCEHR-IEAMLDCQRFLVIEQGNVWQYESLQALLS 1428
Cdd:cd03299 145 VVNPKILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDfEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1214-1373 |
9.32e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.82 E-value: 9.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1214 KYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVS---WNSMTLQEWRKAFGVITQ--- 1287
Cdd:PRK15134 293 KRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPlhnLNRRQLLPVRHRIQVVFQdpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 ---------KVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQ-FPGQlnftlvdggyvLSHGHKQLMCLARSVL 1357
Cdd:PRK15134 373 sslnprlnvLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAE-----------FSGGQRQRIAIARALI 441
|
170
....*....|....*.
gi 91982740 1358 SKAKIILLDEPSANLD 1373
Cdd:PRK15134 442 LKPSLIILDEPTSSLD 457
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1210-1398 |
9.60e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.87 E-value: 9.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1210 DLTVKYVDdgNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN------IKGEIQIDGVSWNSMTLQ--EWRKA 1281
Cdd:PRK14267 9 NLRVYYGS--NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRNIYSPDVDpiEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 FGVitqkVFIFSGTF---------------------RQNLDPNGKW--RDEEIWkvaDQVglKSVIEQFPGQLnftlvdg 1338
Cdd:PRK14267 87 VGM----VFQYPNPFphltiydnvaigvklnglvksKKELDERVEWalKKAALW---DEV--KDRLNDYPSNL------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1339 gyvlSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEH 1398
Cdd:PRK14267 151 ----SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1213-1373 |
9.63e-13 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 72.79 E-value: 9.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1213 VKYVDDgnailenISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMT---LQEWRKAFgvitQKV 1289
Cdd:COG4172 299 VKAVDG-------VSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQDLDGLSrraLRPLRRRM----QVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1290 FifsgtfrQN----LDP-------------------NGKWRDEEIWKVADQVGLK-SVIEQFPGQlnftlvdggyvLSHG 1345
Cdd:COG4172 368 F-------QDpfgsLSPrmtvgqiiaeglrvhgpglSAAERRARVAEALEEVGLDpAARHRYPHE-----------FSGG 429
|
170 180
....*....|....*....|....*....
gi 91982740 1346 HKQLMCLARSVLSKAKIILLDEP-SAnLD 1373
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPtSA-LD 457
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
440-628 |
1.27e-12 |
|
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: 68.84 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEaSEGIIkhSGRVSFSSQISwiMPGTIKENIIFGVSYD------ 513
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE-GGGTT--SGQILFNGQPR--KPDQFQKCVAYVRQDDillpgl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 514 ---EYRYKSVVkaCQLQEDITKFAEQ---DNTVLGEGGVT---------LSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:cd03234 97 tvrETLTYTAI--LRLPRKSSDAIRKkrvEDVLLRDLALTriggnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 579 DVLTEEQIFEscVCKLMASKTRILVTS----KMEQLKKADKILILHEGSSYFYG 628
Cdd:cd03234 175 DSFTALNLVS--TLSQLARRNRIVILTihqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
441-622 |
1.45e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLML------------ILGELEASEGI--IKHSGRVSFSSQISWIMP------G 500
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliisetgqtIVGDYAIPANLkkIKEVKRLRKEIGLVFQFPeyqlfqE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENIIFGVSY----DEYRYKSV---VKACQLQEDITKfaeqdntvlgEGGVTLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK13645 107 TIEKDIAFGPVNlgenKQEAYKKVpelLKLVQLPEDYVK----------RSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 574 PFGYLDVLTEEQiFESCVCKLMASKTR--ILVTSKMEQ-LKKADKILILHEG 622
Cdd:PRK13645 177 PTGGLDPKGEED-FINLFERLNKEYKKriIMVTHNMDQvLRIADEVIVMHEG 227
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
440-642 |
1.54e-12 |
|
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: 72.67 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIKENI 506
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGlniakiglhdlrfKITIIPQDPVLFSGSLRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQI 586
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 587 -------FESCvcklmaskTRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSS 642
Cdd:TIGR00957 1461 qstirtqFEDC--------TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
428-622 |
1.70e-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: 68.61 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCL-VGNP-----VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG--------------- 486
Cdd:COG4181 9 IELRGLTKtVGTGageltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGqdlfaldedararlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 487 --RVSFSSQISWIMPG-TIKENI-----IFGVSYDEYRYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISL 558
Cdd:COG4181 89 arHVGFVFQSFQLLPTlTALENVmlpleLAGRRDARARARALLERVGLGHRLDHYPAQ-----------LSGGEQQRVAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 559 ARAVYKDADLYLLDSPFGYLDVLTEEQIFEscvckLMASKTR------ILVTSKMEQLKKADKILILHEG 622
Cdd:COG4181 158 ARAFATEPAILFADEPTGNLDAATGEQIID-----LLFELNRergttlVLVTHDPALAARCDRVLRLRAG 222
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
448-586 |
1.71e-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: 72.12 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 448 IKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQ-ISWIMPGTIKENI------IFGVSYdeyrYKS- 519
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKISYKPQyISPDYDGTVEEFLrsantdDFGSSY----YKTe 438
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 520 VVKACQLQeditKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVltEEQI 586
Cdd:COG1245 439 IIKPLGLE----KLLDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRL 492
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
439-633 |
1.72e-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: 68.72 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR--------------VSFSSQISWIMPG-TIK 503
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarlgIGYLPQEASIFRKlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENI-----IFGVSYDEYRYKsvvkACQLQED--ITKFAEQDntvlgegGVTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:cd03218 94 ENIlavleIRGLSKKEREEK----LEELLEEfhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 577 YLDVLTEEQIfESCVCKLMASKTRILVTSK--MEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:cd03218 163 GVDPIAVQDI-QKIIKILKDRGIGVLITDHnvRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1222-1398 |
1.83e-12 |
|
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: 68.45 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML----NIKGEIQIDGVswnSMTLQEWRKAFGVITQKVFIFSG-TF 1296
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVegggTTSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGlTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1297 RQNLD-------PNgKWRDEEIWKVADQVGLKsvieqfpgQLNFTLVDGGYV--LSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03234 99 RETLTytailrlPR-KSSDAIRKKRVEDVLLR--------DLALTRIGGNLVkgISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190
....*....|....*....|....*....|..
gi 91982740 1368 PSANLDPIT-YQVIRRVLRQAFAGCTVVLCEH 1398
Cdd:cd03234 170 PTSGLDSFTaLNLVSTLSQLARRNRIVILTIH 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
437-588 |
2.38e-12 |
|
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: 67.82 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG----------------RVSFSSQISWIMPG 500
Cdd:cd03292 13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraipylrrKIGVVFQDFRLLPD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -TIKENIIF-----GVSYDEY--RYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:cd03292 93 rNVYENVAFalevtGVPPREIrkRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIAD 161
|
170
....*....|....*.
gi 91982740 573 SPFGYLDVLTEEQIFE 588
Cdd:cd03292 162 EPTGNLDPDTTWEIMN 177
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
437-646 |
2.62e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG----------------RVSFSSQISWIMPG 500
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGidtgdfsklqgirklvGIVFQNPETQFVGR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENIIFGVSydeyryksvvKACQLQEDITKFAEQdntVLGEGGV---------TLSGGQRARISLARAVYKDADLYLL 571
Cdd:PRK13644 94 TVEEDLAFGPE----------NLCLPPIEIRKRVDR---ALAEIGLekyrhrspkTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 572 DSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKKADKILILHEGSSYFYGtfsELQSLRPDFSSKLMG 646
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEG---EPENVLSDVSLQTLG 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
439-622 |
2.74e-12 |
|
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: 71.09 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII----------KHSGRVSFSSQISWIM--PG------ 500
Cdd:COG1123 279 RAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIlfdgkdltklSRRSLRELRRRVQMVFqdPYsslnpr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -TIKENIIFGVsydeyRYKSVVKACQLQEDITKFAEQ---DNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:COG1123 359 mTVGDIIAEPL-----RLHGLLSRAERRERVAELLERvglPPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTS 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 577 YLDVLTEEQIFEscvckLMAS------KTRILVT---SKMEQLkkADKILILHEG 622
Cdd:COG1123 434 ALDVSVQAQILN-----LLRDlqrelgLTYLFIShdlAVVRYI--ADRVAVMYDG 481
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1206-1417 |
2.81e-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: 2.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTlQEWRKAFGV 1284
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPtSGRATVAGHDVVREP-REVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSG-TFRQNLD--------PNGKWRdEEIWKVADQVGLKSVIEQfpgqlnftLVdGGYvlSHGHKQLMCLARS 1355
Cdd:cd03265 78 VFQDLSVDDElTGWENLYiharlygvPGAERR-ERIDELLDFVGLLEAADR--------LV-KTY--SGGMRRRLEIARS 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 1356 VLSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEHRI-EAMLDCQRFLVIEQGNV 1417
Cdd:cd03265 146 LVHRPEVLFLDEPTIGLDPQTRAHVWEYIEklKEEFGMTILLTTHYMeEAEQLCDRVAIIDHGRI 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
440-633 |
2.97e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 69.45 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------------RVSFSSQISWIMPG-TIKENI 506
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpsrarharqRVGVVPQFDNLDPDfTVRENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 -IFGvsydeyRY--KSVVKACQLQEDITKFAEQDNTVLGEGGvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:PRK13537 102 lVFG------RYfgLSAAAARALVPPLLEFAKLENKADAKVG-ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 584 EQIFESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13537 175 HLMWERLRSLLARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
439-622 |
3.53e-12 |
|
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: 68.40 E-value: 3.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIKEN 505
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGidisklplhtlrsRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 IIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTeEQ 585
Cdd:cd03288 115 LDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT-EN 193
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982740 586 IFESCVCKLMASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:cd03288 194 ILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRG 230
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
99-355 |
3.84e-12 |
|
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: 68.78 E-value: 3.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 99 PVLLGRIIASYDPDNTEERSIAIYLgIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIG 178
Cdd:cd18559 17 PSNLWLLLWFDDPVNGPQEHGQVYL-SVLGALAILQGITVFQYSMAVSIGGIFASRAVHLDLYHKALRSPISFFERTPSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 179 QLISLLSNNLNKFDEGLALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMMVKYRDKRAAKINER 258
Cdd:cd18559 96 ELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGPMAAVGIPLGLLYVPVNRVYAASSRQLKRLESVSKDPR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 259 LVITSEVIDNIYSVKAYCWESAMEKIIESLREEELKMTRRSAYMRFFTSSAFFFSGFFVVFLSVLPYTVI---NGIVLRK 335
Cdd:cd18559 176 YKLFNETLLGISVIKAFEWEEAFIRQVDAKRDNELAYLPSIVYLRALAVRLWCVGPCIVLFASFFAYVSRhslAGLVALK 255
|
250 260
....*....|....*....|
gi 91982740 336 IFTTISFCIVLRMSVtRQFP 355
Cdd:cd18559 256 VFYSLALTTYLNWPL-NMSP 274
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1208-1436 |
4.14e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTlLSAFLRML-----NIKGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:PRK13640 8 FKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKST-ISKLINGLllpddNPNSKITVDGITLTAKTVWDIREKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQ---KVFIfSGTFRQN----LDPNGKWRDEEIWKVADqvglksVIEQFpGQLNFTLVDGGYvLSHGHKQLMCLARS 1355
Cdd:PRK13640 87 GIVFQnpdNQFV-GATVGDDvafgLENRAVPRPEMIKIVRD------VLADV-GMLDYIDSEPAN-LSGGQKQRVAIAGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1356 VLSKAKIILLDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLSEKSVF 1433
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
...
gi 91982740 1434 QRA 1436
Cdd:PRK13640 238 KEI 240
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
426-622 |
4.29e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.09 E-value: 4.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHLCLVgNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWI-------- 497
Cdd:PRK13632 11 ENVSFSYPNSE-NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIrkkigiif 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 498 -------MPGTIKENIIFGVS---YDEYRYKSVVKACQLQEDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDAD 567
Cdd:PRK13632 90 qnpdnqfIGATVEDDIAFGLEnkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQ-------NLSGGQKQRVAIASVLALNPE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 568 LYLLDSPFGYLDVLTEEQIFescvcKLM------ASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIK-----KIMvdlrktRKKTLISITHDMDEAILADKVIVFSEG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1223-1417 |
4.39e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.44 E-value: 4.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLNI-----KGEIQIDGV---SWNSMTLQEWRKAFGVITQKVFIFSG 1294
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTL----IRCINLlerptSGRVLVDGQdltALSEKELRKARRQIGMIFQHFNLLSS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 -TFRQN----LDPNGKWRDEEIWKVA---DQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:PRK11153 97 rTVFDNvalpLELAGTPKAEIKARVTellELVGLSDKADRYPAQ-----------LSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1367 EPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHRIEAMLD-CQRFLVIEQGNV 1417
Cdd:PRK11153 166 EATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRL 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1222-1415 |
5.19e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 68.68 E-value: 5.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEwRKAFGVITQkvfiFSgtfrqNL 1300
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHpDAGSISLCGEPVPSRARHA-RQRVGVVPQ----FD-----NL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1301 DPNGKWRdEEIWKVADQVGLKS--VIEQFPGQLNFTLVDGGY-----VLSHGHKQLMCLARSVLSKAKIILLDEPSANLD 1373
Cdd:PRK13537 92 DPDFTVR-ENLLVFGRYFGLSAaaARALVPPLLEFAKLENKAdakvgELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 91982740 1374 PITYQVIRRVLRQAFA-GCTVVLCEHRI-EAMLDCQRFLVIEQG 1415
Cdd:PRK13537 171 PQARHLMWERLRSLLArGKTILLTTHFMeEAERLCDRLCVIEEG 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
437-635 |
8.02e-12 |
|
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: 66.30 E-value: 8.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR--------------VSFSSQISWIMPG-T 501
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRditglppheraragIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENIIFGvsydEYRYKSVVKACQLQEDITKFaeqdnTVLGE-----GGvTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:cd03224 92 VEENLLLG----AYARRRAKRKARLERVYELF-----PRLKErrkqlAG-TLSGGEQQMLAIARALMSRPKLLLLDEPSE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 577 YLDVLTEEQIFEsCVCKLMASKTRILVTskmEQ-----LKKADKILILHEGSSYFYGTFSELQS 635
Cdd:cd03224 162 GLAPKIVEEIFE-AIRELRDEGVTILLV---EQnarfaLEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_6TM_ABCC |
cd18559 |
Six-transmembrane helical domain of the ABC transporters, subfamily C; This group represents ... |
937-1162 |
8.78e-12 |
|
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: 67.62 E-value: 8.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 937 ITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPyIFLATVP 1016
Cdd:cd18559 67 IFASRAVHLDLYHKALRSPISFFERTPSGELVNLFSKDLDRVDSMAPQVIKMWMGPLQNVIGLYLLILLAGP-MAAVGIP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1017 GLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRrqtyFETLFHKALNLHTANWFMYL---ATLRW 1093
Cdd:cd18559 146 LGLLYVPVNRVYAASSRQLKRLESVSKDPRYKLFNETLLGISVIKAFE----WEEAFIRQVDAKRDNELAYLpsiVYLRA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1094 FQMRIDMIFVLFFIVVTFISILTTGEGEGTTGIILTLAMNIMSTLQWAVNSSIDTDSLMRSVSRVFKFI 1162
Cdd:cd18559 222 LAVRLWCVGPCIVLFASFFAYVSRHSLAGLVALKVFYSLALTTYLNWPLNMSPEVITNIVAAEVSLERS 290
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1208-1417 |
9.96e-12 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 66.72 E-value: 9.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDGVSWNSMTLQEWRKAF 1282
Cdd:PRK13548 5 ARNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALSgelspDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKV---FIFS-------GtfrqnLDPNGKWRDEE---IWKVADQVGLksviEQFPGQLnftlvdggY-VLSHGHKQ 1348
Cdd:PRK13548 79 AVLPQHSslsFPFTveevvamG-----RAPHGLSRAEDdalVAAALAQVDL----AHLAGRD--------YpQLSGGEQQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1349 LMCLARsVL-------SKAKIILLDEPSANLDPITYQVIRRVLRQaFA---GCTVVLCEHRIE-AMLDCQRFLVIEQGNV 1417
Cdd:PRK13548 142 RVQLAR-VLaqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQ-LAherGLAVIVVLHDLNlAARYADRIVLLHQGRL 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
434-622 |
1.15e-11 |
|
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: 66.90 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 434 CLVGnpvLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-----------------RVSFSSQISW 496
Cdd:cd03294 36 QTVG---VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrrkKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 497 IMPG-TIKENIIFGVSydeyryksvVKACQLQEDITKFAEQDNTVLGEGGVT-----LSGGQRARISLARAVYKDADLYL 570
Cdd:cd03294 113 LLPHrTVLENVAFGLE---------VQGVPRAEREERAAEALELVGLEGWEHkypdeLSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 571 LDSPFGYLDVLTEEQIFESCVcKLMAS--KTRILVTSKM-EQLKKADKILILHEG 622
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELL-RLQAElqKTIVFITHDLdEALRLGDRIAIMKDG 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
437-622 |
1.16e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKhSGRVSFSS---------QISWIMP-GTIKENI 506
Cdd:PRK11247 24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-AGTAPLAEaredtrlmfQDARLLPwKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IFGVSYDeYRyksvVKACQLQEDItKFAEQDNtvlgEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE--- 583
Cdd:PRK11247 103 GLGLKGQ-WR----DAALQALAAV-GLADRAN----EWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRiem 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 91982740 584 EQIFEScvckLMASK--TRILVTSKM-EQLKKADKILILHEG 622
Cdd:PRK11247 173 QDLIES----LWQQHgfTVLLVTHDVsEAVAMADRVLLIEEG 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1207-1420 |
1.35e-11 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 67.79 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRML----NI-KGEIQIDGVSWN---------S 1272
Cdd:COG3839 5 ELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRMIagleDPtSGEILIGGRDVTdlppkdrniA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1273 MTLQEW--------RK--AFGVITQKVfifsgtfrqnldpNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvL 1342
Cdd:COG3839 79 MVFQSYalyphmtvYEniAFPLKLRKV-------------PKAEIDRRVREAAELLGLEDLLDRKPKQ-----------L 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1343 SHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrlGTTTIYVTHdQVEAMTLADRIAVMNDGRIQQ 214
|
.
gi 91982740 1420 Y 1420
Cdd:COG3839 215 V 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
418-622 |
1.36e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.89 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 418 DRKTSNGENHLSFSHLClvGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-VSFSSQISW 496
Cdd:COG1129 247 KRAAAPGEVVLEVEGLS--VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpVRIRSPRDA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 497 I-----------------MPGTIKENIIFgVSYDEYRYKSVVKACQLQEDITKFAEQ--------DNTVlgeggVTLSGG 551
Cdd:COG1129 325 IragiayvpedrkgeglvLDLSIRENITL-ASLDRLSRGGLLDRRRERALAEEYIKRlriktpspEQPV-----GNLSGG 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 552 QRARISLARAVYKDADLYLLDSPF-GyLDVLTEEQIFescvcKLMASKTR-----ILVTSKMEQLKK-ADKILILHEG 622
Cdd:COG1129 399 NQQKVVLAKWLATDPKVLILDEPTrG-IDVGAKAEIY-----RLIRELAAegkavIVISSELPELLGlSDRILVMREG 470
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
438-622 |
1.46e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 66.65 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-VSFSSQ---ISWI-------MPGT----- 501
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKdVTKLPEykrAKYIgrvfqdpMMGTapsmt 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENII------------FGVSYDEY-RYKSVVKACQLQ-EDitkfaeQDNTVLGeggvTLSGGQRARISLARAVYKDAD 567
Cdd:COG1101 99 IEENLAlayrrgkrrglrRGLTKKRReLFRELLATLGLGlEN------RLDTKVG----LLSGGQRQALSLLMATLTKPK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 568 LYLLDSPFGYLD------V--LTEEQIFESCVCKLMasktrilVTSKMEQ-LKKADKILILHEG 622
Cdd:COG1101 169 LLLLDEHTAALDpktaalVleLTEKIVEENNLTTLM-------VTHNMEQaLDYGNRLIMMHEG 225
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1209-1436 |
1.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 66.75 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1209 KDLTVKYVDDGNAiLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQIDGVSWNSMTLQEWRKAFGVITQ 1287
Cdd:PRK13652 7 RDLCYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTsGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 KV--FIFSGTFRQNL--DPNGKWRDEE-----IWKVADQVGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCLARSVLS 1358
Cdd:PRK13652 86 NPddQIFSPTVEQDIafGPINLGLDEEtvahrVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1359 KAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHRIEAMLDCQRFL-VIEQGNVWQYESLQALLSEKSVFQR 1435
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMADYIyVMDKGRIVAYGTVEEIFLQPDLLAR 234
|
.
gi 91982740 1436 A 1436
Cdd:PRK13652 235 V 235
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
437-628 |
1.55e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 66.68 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWI---------------MPGT 501
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrskvglvfqdpddqvFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENIIFG-----VSYDEY--RYKSVVKACQLQEditkFAEQdntvlgeGGVTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK13647 97 VWDDVAFGpvnmgLDKDEVerRVEEALKAVRMWD----FRDK-------PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 575 FGYLDVLTEEQIFESCVCKLMASKTRILVTSKME-QLKKADKILILHEGSSYFYG 628
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEG 220
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
439-628 |
1.62e-11 |
|
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: 64.88 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELeasegiikHSGRVSfssqiswimpGTIKENiifGVSYDEYRYK 518
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR--------TGLGVS----------GEVLIN---GRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 519 SvvkacqlqedITKFAEQDNTVLGEGGV-----------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIF 587
Cdd:cd03213 82 K----------IIGYVPQDDILHPTLTVretlmfaaklrGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 91982740 588 EScvCKLMASKTRILVTS----KMEQLKKADKILILHEGSSYFYG 628
Cdd:cd03213 152 SL--LRRLADTGRTIICSihqpSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
446-622 |
1.62e-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: 65.21 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 446 LNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----------VSFSSQISWIMPG-TIKENIIFGVS-- 511
Cdd:cd03298 19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHlTVEQNVGLGLSpg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 512 -----YDEYRYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQI 586
Cdd:cd03298 99 lkltaEDRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 91982740 587 FEsCVCKLMASK--TRILVTSKMEQLKK-ADKILILHEG 622
Cdd:cd03298 168 LD-LVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNG 205
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
441-622 |
1.77e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.78 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-----------------RVSFSSQI--SWIMPGT 501
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitpetgnknlkklrkKVSLVFQFpeAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENIIFG-----VSYDEYRYKSV--VKACQLQEDitkfaeqdntVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK13641 103 VLKDVEFGpknfgFSEDEAKEKALkwLKKVGLSED----------LISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 91982740 575 FGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHG 221
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
428-596 |
2.01e-11 |
|
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: 63.71 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV---GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMlILGEL-EASEG-IIKHSG-RVSFSSQISWIMPGT 501
Cdd:cd03223 1 IELENLSLAtpdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLwPWGSGrIGMPEGeDLLFLPQRPYLPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENIIfgvsydeYRYKSVvkacqlqeditkfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVL 581
Cdd:cd03223 80 LREQLI-------YPWDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEE 125
|
170
....*....|....*
gi 91982740 582 TEEQIFESCVCKLMA 596
Cdd:cd03223 126 SEDRLYQLLKELGIT 140
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1209-1401 |
2.12e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 65.96 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1209 KDLTVKYvddGNAI-LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDG-VSWNSMTLQ-------EWR 1279
Cdd:PRK14243 14 ENLNVYY---GSFLaVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPGFRVEGkVTFHGKNLYapdvdpvEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1280 KAFGVITQKVFIFSGTFRQNLDPNGKWR------DEEIWKVADQVGLKSVIEQfpgqlnfTLVDGGYVLSHGHKQLMCLA 1353
Cdd:PRK14243 91 RRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQAALWDEVKD-------KLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 91982740 1354 RSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRIE 1401
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQ 211
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
440-622 |
2.45e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.29 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPG---------------TIKE 504
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREavaivpegrrvfsrmTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVSY-DEYRYKSVVKacQLQEDITKFAEQDNTVLGeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:PRK11614 100 NLAMGGFFaERDQFQERIK--WVYELFPRLHERRIQRAG----TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 91982740 584 EQIFESCVCKLMASKTRILVTSKMEQ-LKKADKILILHEG 622
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVEQNANQaLKLADRGYVLENG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
440-635 |
2.52e-11 |
|
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: 65.15 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR--------------VSFSSQISWIMPG-TIKE 504
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEditglppheiarlgIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGV------TLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:cd03219 95 NVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLadrpagELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 579 DVLTEEQIFEScVCKLMASKTRILVTS-KMEQLKK-ADKILILHEGSSYFYGTFSELQS 635
Cdd:cd03219 175 NPEETEELAEL-IRELRERGITVLLVEhDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1219-1415 |
2.88e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 64.66 E-value: 2.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1219 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLrmlnikGEIQ-IDG-VSWNSMTLQEW---------RKAFGVITQ 1287
Cdd:cd03290 13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIL------GEMQtLEGkVHWSNKNESEPsfeatrsrnRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 KVFIFSGTFRQNLDPNGKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:cd03290 87 KPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1368 PSANL-----DPITYQVIRRVLRQAFAgcTVVLCEHRIEAMLDCQRFLVIEQG 1415
Cdd:cd03290 167 PFSALdihlsDHLMQEGILKFLQDDKR--TLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1208-1415 |
3.83e-11 |
|
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: 63.61 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVddgnaiLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKA-FGVI 1285
Cdd:cd03215 7 VRGLSVKGA------VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPaSGEITLDGKPVTRRSPRDAIRAgIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1286 TQkvfifsgtfrqnlDPngkwRDEEIwkvadqVGLKSVIEqfpgqlNFTLvdgGYVLSHGHKQLMCLARSVLSKAKIILL 1365
Cdd:cd03215 81 PE-------------DR----KREGL------VLDLSVAE------NIAL---SSLLSGGNQQKVVLARWLARDPRVLIL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1366 DEPSANLDPITYQVIRRVLRQ-AFAGCTVVLcehrI-----EAMLDCQRFLVIEQG 1415
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRElADAGKAVLL----IsseldELLGLCDRILVMYEG 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1208-1419 |
4.20e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.40 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN-----IKGEIQIDGVSWNSMTlqEWRKAF 1282
Cdd:PRK11607 22 IRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLL----RMLAgfeqpTAGQIMLDGVDLSHVP--PYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKVFIFSG-TFRQN----LDPNGKWRDEEIWKVADQVGLKSVIE---QFPGQLnftlvdggyvlSHGHKQLMCLAR 1354
Cdd:PRK11607 94 NMMFQSYALFPHmTVEQNiafgLKQDKLPKAEIASRVNEMLGLVHMQEfakRKPHQL-----------SGGQRQRVALAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1355 SVLSKAKIILLDEPSANLDP-----ITYQVIRRVLRqafAGCTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKklrdrMQLEVVDILER---VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQ 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
432-623 |
4.35e-11 |
|
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: 63.70 E-value: 4.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 432 HLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILG--ELEASEGIIKHSG----------RVSFSSQISWIMP 499
Cdd:cd03217 7 HVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGeditdlppeeRARLGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 GTIKeniifGVSYDEY-RYksvvkacqlqeditkfaeqdntvLGEGgvtLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:cd03217 87 PEIP-----GVKNADFlRY-----------------------VNEG---FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 91982740 579 DVLTEEQIFEScVCKLMASKTRILVTSKMEQL---KKADKILILHEGS 623
Cdd:cd03217 136 DIDALRLVAEV-INKLREEGKSVLIITHYQRLldyIKPDRVHVLYDGR 182
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
437-622 |
4.56e-11 |
|
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: 64.09 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWI------------------M 498
Cdd:cd03262 12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelrqkvgmvfqqfnlfphL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 499 pgTIKENIIF------GVSYDEYRYKS--VVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYL 570
Cdd:cd03262 92 --TVLENITLapikvkGMSKAEAEERAleLLEKVGLADKADAYPAQ-----------LSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 571 LDSPFGYLDvltEEQIFEscVCKLMAS-----KTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:cd03262 159 FDEPTSALD---PELVGE--VLDVMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDG 211
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
445-579 |
4.88e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.22 E-value: 4.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 445 NLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----------VSFSSQISWIMPG-TIKENIIFGV-- 510
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpVSMLFQENNLFSHlTVAQNIGLGLnp 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 511 -----SYDEYRYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK10771 99 glklnAAQREKLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1206-1420 |
5.06e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.03 E-value: 5.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVDDgnAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMlnikgeiQIDGVSWNSMTLQEWRKAF 1282
Cdd:PRK13638 2 LATSDLWFRYQDE--PVLKGLNLDFSLSPVTGLVGANGCGKSTLfmnLSGLLRP-------QKGAVLWQGKPLDYSKRGL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVITQKV-FIFSG----TFRQNLDPNGKWR-------DEEIWKVADQVglksvieqfpgqlnFTLVDGGY-------VLS 1343
Cdd:PRK13638 73 LALRQQVaTVFQDpeqqIFYTDIDSDIAFSlrnlgvpEAEITRRVDEA--------------LTLVDAQHfrhqpiqCLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1344 HGHKQLMCLARSVLSKAKIILLDEPSANLDPI----TYQVIRRVLRQafaGCTVVLCEHRIEAMLDCQRFL-VIEQGNVW 1418
Cdd:PRK13638 139 HGQKKRVAIAGALVLQARYLLLDEPTAGLDPAgrtqMIAIIRRIVAQ---GNHVIISSHDIDLIYEISDAVyVLRQGQIL 215
|
..
gi 91982740 1419 QY 1420
Cdd:PRK13638 216 TH 217
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
439-614 |
5.38e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 5.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------RVSFSSQI------SWIMPG-TIKEN 505
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERqsikkdLCTYQKQLcfvghrSGINPYlTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 IIFGVSYDEyryksvvKACQLQEDITKFAEQDNTVLGEGgvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvlteEQ 585
Cdd:PRK13540 95 CLYDIHFSP-------GAVGITELCRLFSLEHLIDYPCG--LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD----EL 161
|
170 180 190
....*....|....*....|....*....|...
gi 91982740 586 IFESCVCKLMASKTR---ILVTSKME-QLKKAD 614
Cdd:PRK13540 162 SLLTIITKIQEHRAKggaVLLTSHQDlPLNKAD 194
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
437-586 |
5.58e-11 |
|
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: 64.44 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG-------IIKHSGRVSFSSQISWIM--------PG- 500
Cdd:COG1124 17 RVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGevtfdgrPVTRRRRKAFRRRVQMVFqdpyaslhPRh 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENI-----IFGVSYDEYRYKSVVKACQLQEDI-TKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:COG1124 97 TVDRILaeplrIHGLPDREERIAELLEQVGLPPSFlDRYPHQ-----------LSGGQRQRVAIARALILEPELLLLDEP 165
|
170
....*....|..
gi 91982740 575 FGYLDVLTEEQI 586
Cdd:COG1124 166 TSALDVSVQAEI 177
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
426-636 |
6.08e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 6.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHLClvgNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMlILGELEASEGIIKHSGRVSF--------------- 490
Cdd:PRK14258 11 NNLSFYYDT---QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVEFfnqniyerrvnlnrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 491 SSQISWIMPG------TIKENIIFGVSYDEYRYK--------SVVKACQLQEDItkfaeqdNTVLGEGGVTLSGGQRARI 556
Cdd:PRK14258 87 RRQVSMVHPKpnlfpmSVYDNVAYGVKIVGWRPKleiddiveSALKDADLWDEI-------KHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 557 SLARAVYKDADLYLLDSPFGYLDVLTEEQIfESCV--CKLMASKTRILVTSKMEQLKKadkiliLHEGSSYFYGTFSELQ 634
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKV-ESLIqsLRLRSELTMVIVSHNLHQVSR------LSDFTAFFKGNENRIG 232
|
..
gi 91982740 635 SL 636
Cdd:PRK14258 233 QL 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
440-588 |
6.37e-11 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 64.07 E-value: 6.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-----------------RVSFSSQISWIMPG-T 501
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpmsklssaakaelrnqKLGFIYQFHHLLPDfT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENI-----IFGVSYDEYRYKS--VVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK11629 104 ALENVampllIGKKKPAEINSRAleMLAAVGLEHRANHRPSE-----------LSGGERQRVAIARALVNNPRLVLADEP 172
|
170
....*....|....
gi 91982740 575 FGYLDVLTEEQIFE 588
Cdd:PRK11629 173 TGNLDARNADSIFQ 186
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1206-1419 |
6.52e-11 |
|
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: 63.43 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN-----IKGEIQIDGvswNSMT-LQEWR 1279
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTL----RMIAgleepTSGRIYIGG---RDVTdLPPKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1280 KAFGVITQKVFIFSG-TFRQNLDPNGKWR-------DEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMC 1351
Cdd:cd03301 72 RDIAMVFQNYALYPHmTVYDNIAFGLKLRkvpkdeiDERVREVAELLQIEHLLDRKPKQL-----------SGGQRQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1352 LARSVLSKAKIILLDEPSANLDP-ITYQV---IRRVLRQafAGCTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:cd03301 141 LGRAIVREPKVFLMDEPLSNLDAkLRVQMraeLKRLQQR--LGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1208-1399 |
6.81e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 6.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMlnIKGEIQIDGvswNSMTLQEwrkafgviTQ 1287
Cdd:TIGR03719 325 AENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTL----FRM--ITGQEQPDS---GTIEIGE--------TV 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 KVfIFSGTFRQNLDPNGK-WrdEEIWKVADQVGLKSVieQFP-----GQLNFTLVD-----GgyVLSHGHKQLMCLARSV 1356
Cdd:TIGR03719 386 KL-AYVDQSRDALDPNKTvW--EEISGGLDIIKLGKR--EIPsrayvGRFNFKGSDqqkkvG--QLSGGERNRVHLAKTL 458
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 91982740 1357 LSKAKIILLDEPSANLDPITYQVIRRVLrQAFAGCTVVLCEHR 1399
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLDVETLRALEEAL-LNFAGCAVVISHDR 500
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1214-1419 |
7.08e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.64 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1214 KYVDDGN---AILENISFSISPGQRVGLLGRTGSGKSTLLsAFLRMLN--IKGEIQIDGVSWNSMTlQEWRKAF-----G 1283
Cdd:PRK10584 14 KSVGQGEhelSILTGVELVVKRGETIALIGESGSGKSTLL-AILAGLDdgSSGEVSLVGQPLHQMD-EEARAKLrakhvG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKvFIFSGTF--RQNLDPNGKWRDE-------EIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLAR 1354
Cdd:PRK10584 92 FVFQS-FMLIPTLnaLENVELPALLRGEssrqsrnGAKALLEQLGLGKRLDHLPAQL-----------SGGEQQRVALAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1355 SVLSKAKIILLDEPSANLDPITYQVIRRVLrqaFA-----GCTVVLCEHRIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLL---FSlnrehGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1209-1417 |
7.79e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 64.72 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1209 KDLTVKYVDDGNA----ILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLrmLNIKGEIQIDGVSWNSM-TLQEWRK 1280
Cdd:PRK13633 8 KNVSYKYESNEESteklALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL--IPSEGKVYVDGLDTSDEeNLWDIRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVitqkVFifsgtfrQNLD----------------PNGKWRDEEIWKVADQvGLKSV----IEQFPGQLnftlvdggy 1340
Cdd:PRK13633 86 KAGM----VF-------QNPDnqivativeedvafgpENLGIPPEEIRERVDE-SLKKVgmyeYRRHAPHL--------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1341 vLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPI----TYQVIRRVLRQafAGCTVVLCEHRIEAMLDCQRFLVIEQGN 1416
Cdd:PRK13633 145 -LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSgrreVVNTIKELNKK--YGITIILITHYMEEAVEADRIIVMDSGK 221
|
.
gi 91982740 1417 V 1417
Cdd:PRK13633 222 V 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1214-1417 |
8.28e-11 |
|
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: 64.72 E-value: 8.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1214 KYVDDGNAiLENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLNikGEIQIDG----VSWNSMTLQ--EWRKAFGVITQ 1287
Cdd:TIGR01188 1 KVYGDFKA-VDGVNFKVREGEVFGFLGPNGAGKTTTI----RMLT--TLLRPTSgtarVAGYDVVREprKVRRSIGIVPQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 KVFIFSG-TFRQNLDPNG------KW-RDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSK 1359
Cdd:TIGR01188 74 YASVDEDlTGRENLEMMGrlyglpKDeAEERAEELLELFELGEAADRPVGTY-----------SGGMRRRLDIAASLIHQ 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1360 AKIILLDEPSANLDPITYQVIRRVLRqAF--AGCTVVLCEHRI-EAMLDCQRFLVIEQGNV 1417
Cdd:TIGR01188 143 PDVLFLDEPTTGLDPRTRRAIWDYIR-ALkeEGVTILLTTHYMeEADKLCDRIAIIDHGRI 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
441-609 |
8.59e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 64.03 E-value: 8.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLI--LGELEAS---EGIIKHSGR---------VSFSSQISWIM------PG 500
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHniysprtdtVDLRKEIGMVFqqpnpfPM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENIIFGVSYDEYRYKSVVKACQlqEDITKFAEQDNTV---LGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK14239 101 SIYENVVYGLRLKGIKDKQVLDEAV--EKSLKGASIWDEVkdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190
....*....|....*....|....*....|..
gi 91982740 578 LDVLTEEQIfESCVCKLMASKTRILVTSKMEQ 609
Cdd:PRK14239 179 LDPISAGKI-EETLLGLKDDYTMLLVTRSMQQ 209
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
437-586 |
9.05e-11 |
|
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: 62.90 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIK------HSGRVSFSSQISWI--MPG-----TIK 503
Cdd:cd03231 12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLlnggplDFQRDSIARGLLYLghAPGikttlSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFgvsydeYRYKSVVKACQlqediTKFAEQDNTVLGEGGV-TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03231 92 ENLRF------WHADHSDEQVE-----EALARVGLNGFEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAG 160
|
....
gi 91982740 583 EEQI 586
Cdd:cd03231 161 VARF 164
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
441-639 |
9.21e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.62 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEAsegiikHSGRVSFSSQ-ISWIMPG-----------------TI 502
Cdd:COG3840 15 PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPP------DSGRILWNGQdLTALPPAerpvsmlfqennlfphlTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIFGVSydeyryksvvKACQL----QEDITKFAEQdntvLGEGGV------TLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG3840 89 AQNIGLGLR----------PGLKLtaeqRAQVEQALER----VGLAGLldrlpgQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 573 SPFGYLD-------------VLTEEQIfescvcklmaskTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSELQSLRP 638
Cdd:COG3840 155 EPFSALDpalrqemldlvdeLCRERGL------------TVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEP 222
|
.
gi 91982740 639 D 639
Cdd:COG3840 223 P 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
437-634 |
9.61e-11 |
|
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: 63.16 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG--------IIKHSGRVSFSsqISWI--MPG-----T 501
Cdd:cd03265 12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGratvaghdVVREPREVRRR--IGIVfqDLSvddelT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENI-----IFGVSYDEYRYK--SVVKACQLQEDITKFAEqdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:cd03265 90 GWENLyiharLYGVPGAERRERidELLDFVGLLEAADRLVK-----------TYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 575 FGYLDVLTEEQIFEScVCKLMASK--TRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSELQ 634
Cdd:cd03265 159 TIGLDPQTRAHVWEY-IEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEELK 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
428-637 |
1.13e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.59 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLIL----------------------------GELEASE 479
Cdd:PTZ00265 1171 VNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneqdyqGDEEQNV 1250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 480 G--------------------IIKHSGRV-------------------SFSSQISWIMPGTIKENIIFGvsYDEYRYKSV 520
Cdd:PTZ00265 1251 GmknvnefsltkeggsgedstVFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIYENIKFG--KEDATREDV 1328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 521 VKACQ---LQEDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCV-CKLMA 596
Cdd:PTZ00265 1329 KRACKfaaIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdIKDKA 1408
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 91982740 597 SKTRILVTSKMEQLKKADKILILH--EGSSYF---YGTFSELQSLR 637
Cdd:PTZ00265 1409 DKTIITIAHRIASIKRSDKIVVFNnpDRTGSFvqaHGTHEELLSVQ 1454
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1208-1373 |
1.21e-10 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.86 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMlnIKGEIQIDG--VSWNsmtlQEWRkaFGVI 1285
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTL----LKI--LAGELEPDSgeVSIP----KGLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1286 TQKVFIFSG-TFRQN-LDPNGKWR----------------DEEIWKVA------DQVG---LKSVIEQFPGQLNFTLVDG 1338
Cdd:COG0488 67 PQEPPLDDDlTVLDTvLDGDAELRaleaeleeleaklaepDEDLERLAelqeefEALGgweAEARAEEILSGLGFPEEDL 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 91982740 1339 GY---VLSHGHKQLMCLARSVLSKAKIILLDEPSANLD 1373
Cdd:COG0488 147 DRpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
426-584 |
1.25e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFSHL-CLVGN-PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR----VSFSSQISWImp 499
Cdd:PRK13539 1 MMLEGEDLaCVRGGrVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGdiddPDVAEACHYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 G---------TIKENIIFGVSY---DEYRYKSVVKACQLQeDIT--KFAEqdntvlgeggvtLSGGQRARISLARAVYKD 565
Cdd:PRK13539 79 GhrnamkpalTVAENLEFWAAFlggEELDIAAALEAVGLA-PLAhlPFGY------------LSAGQKRRVALARLLVSN 145
|
170
....*....|....*....
gi 91982740 566 ADLYLLDSPFGYLDVLTEE 584
Cdd:PRK13539 146 RPIWILDEPTAALDAAAVA 164
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1223-1415 |
1.28e-10 |
|
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: 63.12 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKST---LLSAFLRmlNIKGEIQIDG-VSWNSMtlQEWRKAFGVI----TQKVF---- 1290
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTtlkILSGLLQ--PTSGEVRVAGlVPWKRR--KKFLRRIGVVfgqkTQLWWdlpv 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 ------------IFSGTFRQNLDpngkwrdeeiwKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLS 1358
Cdd:cd03267 113 idsfyllaaiydLPPARFKKRLD-----------ELSELLDLEELLDTPVRQL-----------SLGQRMRAEIAAALLH 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1359 KAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHR---IEAMldCQRFLVIEQG 1415
Cdd:cd03267 171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRerGTTVLLTSHYmkdIEAL--ARRVLVIDKG 230
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
437-633 |
1.51e-10 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 62.99 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEasegiiKHSGRVSFSSQISWIMPgtIKENIIFGVSY---- 512
Cdd:PRK10895 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP------RDAGNIIIDDEDISLLP--LHARARRGIGYlpqe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 513 -DEYR----YKSVVKACQLQEDITKFAEQD--NTVLGEG---------GVTLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK10895 87 aSIFRrlsvYDNLMAVLQIRDDLSAEQREDraNELMEEFhiehlrdsmGQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 577 YLD---VLTEEQIFEscvcKLMASKTRILVTSK--MEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK10895 167 GVDpisVIDIKRIIE----HLRDSGLGVLITDHnvRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1215-1398 |
1.80e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.14 E-value: 1.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1215 YVDDgNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDG--VSWNSMTLQ----EWRKAFGVITQ 1287
Cdd:PRK14246 19 YIND-KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIyDSKIKVDGkvLYFGKDIFQidaiKLRKEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1288 KVFIFS-----GTFRQNLDPNGKWRDEEIWKVADQ----VGL-KSVIEQfpgqlnftLVDGGYVLSHGHKQLMCLARSVL 1357
Cdd:PRK14246 98 QPNPFPhlsiyDNIAYPLKSHGIKEKREIKKIVEEclrkVGLwKEVYDR--------LNSPASQLSGGQQQRLTIARALA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 91982740 1358 SKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEH 1398
Cdd:PRK14246 170 LKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSH 210
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1208-1374 |
1.86e-10 |
|
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: 61.99 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTvkYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLL---SAFLRMLniKGEIqidgvSWNSMTLQEWRKafgv 1284
Cdd:TIGR01189 3 ARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLrilAGLLRPD--SGEV-----RWNGTPLAEQRD---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQKVFIFSG---------TFRQNLD---PNGKWRDEEIWKVADQVGLKSvIEQFP-GQlnftlvdggyvLSHGHKQLMC 1351
Cdd:TIGR01189 70 EPHENILYLGhlpglkpelSALENLHfwaAIHGGAQRTIEDALAAVGLTG-FEDLPaAQ-----------LSAGQQRRLA 137
|
170 180
....*....|....*....|...
gi 91982740 1352 LARSVLSKAKIILLDEPSANLDP 1374
Cdd:TIGR01189 138 LARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
408-622 |
1.99e-10 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 408 LLEkvqLNNDDRKTSNGENHLSfshlclvgnpVLKNINLNIKKGEMLAITGSTGAGKtSLLMLILGELE-ASEGIIKHSG 486
Cdd:PRK10535 4 LLE---LKDIRRSYPSGEEQVE----------VLKGISLDIYAGEMVAIVGASGSGK-STLMNILGCLDkPTSGTYRVAG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 487 RvSFSSQISWIMPGTIKENiiFGVSYDEYRYKSVVKACQLQEDITKFA--------EQDNTVLGEGGV---------TLS 549
Cdd:PRK10535 70 Q-DVATLDADALAQLRREH--FGFIFQRYHLLSHLTAAQNVEVPAVYAglerkqrlLRAQELLQRLGLedrveyqpsQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 550 GGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFesCVCKLMASK--TRILVTSKMEQLKKADKILILHEG 622
Cdd:PRK10535 147 GGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVM--AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDG 219
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1208-1417 |
2.15e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.59 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRM-LNI----KGEIQIDGvswNSMTlQEWRKAF 1282
Cdd:COG4152 4 LKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTI----RIiLGIlapdSGEVLWDG---EPLD-PEDRRRI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 G-------------VITQKVFIfsGTFRqNLDPNGKWRDEEIWkvADQVGLKSV----IEQfpgqlnftlvdggyvLSHG 1345
Cdd:COG4152 74 GylpeerglypkmkVGEQLVYL--ARLK-GLSKAEAKRRADEW--LERLGLGDRankkVEE---------------LSKG 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1346 HKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLR-QAFAGCTVVLCEHR---IEAMldCQRFLVIEQGNV 1417
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIReLAAKGTTVIFSSHQmelVEEL--CDRIVIINKGRK 207
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
437-580 |
2.92e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-------VSFSSQISWIMPGT-------I 502
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDdvealsaRAASRRVASVPQDTslsfefdV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIFGVSYDEYRY-------KSVVKACQLQEDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:PRK09536 95 RQVVEMGRTPHRSRFdtwtetdRAAVERAMERTGVAQFADRPVT-------SLSGGERQRVLLARALAQATPVLLLDEPT 167
|
....*
gi 91982740 576 GYLDV 580
Cdd:PRK09536 168 ASLDI 172
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
435-622 |
3.08e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.81 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 435 LVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG---------RVSF-SSQISWI------- 497
Cdd:PRK10908 12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGhditrlknrEVPFlRRQIGMIfqdhhll 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 498 MPGTIKEN-----IIFGVSYDEYRYK--SVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYL 570
Cdd:PRK10908 92 MDRTVYDNvaiplIIAGASGDDIRRRvsAALDKVGLLDKAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 571 LDSPFGYLDVLTEEQI---FESC----VCKLMASKTRILVTskmeqlKKADKILILHEG 622
Cdd:PRK10908 161 ADEPTGNLDDALSEGIlrlFEEFnrvgVTVLMATHDIGLIS------RRSYRMLTLSDG 213
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
426-561 |
3.38e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 62.48 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 426 NHLSFShlcLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR------------------ 487
Cdd:PRK13548 6 RNLSVR---LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRpladwspaelarrravlp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 488 ----VSFssqiswimPGTIKENIIFGVS---YDEYRYKSVVKACQLQEDITKFAEQDNTvlgeggvTLSGGQRARISLAR 560
Cdd:PRK13548 83 qhssLSF--------PFTVEEVVAMGRAphgLSRAEDDALVAAALAQVDLAHLAGRDYP-------QLSGGEQQRVQLAR 147
|
.
gi 91982740 561 A 561
Cdd:PRK13548 148 V 148
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
448-648 |
3.54e-10 |
|
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: 60.66 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 448 IKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-RVSFSSQIswimpgtikeniifgvsydeyryksvvkacql 526
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGiTPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 527 qeditkfaeqdntvlgeggVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVltEEQIFESCVCKLM---ASKTRILV 603
Cdd:cd03222 70 -------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDI--EQRLNAARAIRRLseeGKKTALVV 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 91982740 604 TSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYD 648
Cdd:cd03222 129 EHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYL 173
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
441-633 |
3.60e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.73 E-value: 3.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII--------------------KHSGRVsFSSQISWIMPG 500
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVtigervitagkknkklkplrKKVGIV-FQFPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENIIFG-----VSYDE--YRYKSVVKACQLQEDitkfaeqdntVLGEGGVTLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK13634 102 TVEKDICFGpmnfgVSEEDakQKAREMIELVGLPEE----------LLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 574 PFGYLDVLTEEQIFEscvcklMASK-------TRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13634 172 PTAGLDPKGRKEMME------MFYKlhkekglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
437-636 |
3.77e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.50 E-value: 3.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVL-KNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSF--------------SSQISWIM--- 498
Cdd:PLN03073 520 GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMavfsqhhvdgldlsSNPLLYMMrcf 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 499 PGTIKEniifgvsydeyryksvvkacQLQEDITKFAEQDNTVLgEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PLN03073 600 PGVPEQ--------------------KLRAHLGSFGVTGNLAL-QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL 658
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 579 DVLTEEQIFESCVC----KLMASKTRILVTSKMEQLkkadkiLILHEGS-SYFYGTFSELQSL 636
Cdd:PLN03073 659 DLDAVEALIQGLVLfqggVLMVSHDEHLISGSVDEL------WVVSEGKvTPFHGTFHDYKKT 715
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
437-655 |
3.96e-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: 64.05 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILG--ELEASEG-IIKH------SGRVSFSSQISWIMP---GTIKE 504
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGrIIYHvalcekCGYVERPSKVGEPCPvcgGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVSYDEYRYKSVVK--ACQLQEDITKFAEQ---DNTV--LGEGGVT---------------------------LSG 550
Cdd:TIGR03269 92 EEVDFWNLSDKLRRRIRKriAIMLQRTFALYGDDtvlDNVLeaLEEIGYEgkeavgravdliemvqlshrithiardLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 551 GQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQL--KKADKILILHEGSSYFYG 628
Cdd:TIGR03269 172 GEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVieDLSDKAIWLENGEIKEEG 251
|
250 260
....*....|....*....|....*...
gi 91982740 629 TFSELqslrpdfSSKLM-GYDTFDQFTE 655
Cdd:TIGR03269 252 TPDEV-------VAVFMeGVSEVEKECE 272
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1206-1417 |
4.01e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQ-------- 1276
Cdd:PRK15056 7 IVVNDVTVTW-RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLaSGKISILGQPTRQALQKnlvayvpq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1277 ----EWrkAFGVITQKVFIFSGTFRQNLDPNGKWRDEEIWKVA-DQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMC 1351
Cdd:PRK15056 86 seevDW--SFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAAlARVDMVEFRHRQIGE-----------LSGGQKKRVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1352 LARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTV 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1208-1417 |
4.08e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 63.71 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDdgNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVIT 1286
Cdd:PRK09536 6 VSDLSVEFGD--TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTpTAGTVLVAGDDVEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFI-FSGTFRQ-----------NLDPNGKWRDEEIWKVADQVGlksvIEQFPGQlNFTlvdggyVLSHGHKQLMCLAR 1354
Cdd:PRK09536 84 QDTSLsFEFDVRQvvemgrtphrsRFDTWTETDRAAVERAMERTG----VAQFADR-PVT------SLSGGERQRVLLAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1355 SVLSKAKIILLDEPSANLDpITYQV--IRRVLRQAFAGCTVVLCEHRIE-AMLDCQRFLVIEQGNV 1417
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLD-INHQVrtLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRV 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
437-586 |
4.60e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.21 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-------------VSFSSQISWIMPGTIK 503
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQptrqalqknlvayVPQSEEVDWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFG-------VSYDEYRYKSVVKACQLQEDITKFAEQDntvLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK15056 99 DVVMMGryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQ---IGE----LSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170
....*....|
gi 91982740 577 YLDVLTEEQI 586
Cdd:PRK15056 172 GVDVKTEARI 181
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
437-622 |
4.68e-10 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------------RVSFSSQISWIMPG-TIK 503
Cdd:PRK13536 53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpararlaraRIGVVPQFDNLDLEfTVR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 EN-IIFGvsydeyRYKSvVKACQLQEDIT---KFAEQDNTVlgEGGVT-LSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK13536 133 ENlLVFG------RYFG-MSTREIEAVIPsllEFARLESKA--DARVSdLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 91982740 579 DVLTEEQIFESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHFMEEAERlCDRLCVLEAG 248
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
441-609 |
5.05e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.11 E-value: 5.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLL-----MLILGELEASEGIIKHSGRVSFSSQISWI---------------MPG 500
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFHGKNLYAPDVDPVevrrrigmvfqkpnpFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENIIFGV-------SYDEYRYKSVVKACQLQEDITKfaeqdntvLGEGGVTLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK14243 106 SIYDNIAYGAringykgDMDELVERSLRQAALWDEVKDK--------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 91982740 574 PFGYLDVLTEEQIfESCVCKLMASKTRILVTSKMEQ 609
Cdd:PRK14243 178 PCSALDPISTLRI-EELMHELKEQYTIIIVTHNMQQ 212
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
440-628 |
5.28e-10 |
|
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: 61.05 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGeMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------RVSFSSQISWiMPGTikeniiFGV--- 510
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGqdvlkqPQKLRRRIGY-LPQE------FGVypn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 511 --SYDEYRYKSVVKACQlQEDITKFAEQdntVLGEGGV---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:cd03264 87 ftVREFLDYIAWLKGIP-SKEVKARVDE---VLELVNLgdrakkkigSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 580 VltEEQI-FESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYG 628
Cdd:cd03264 163 P--EERIrFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
439-628 |
5.45e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 60.74 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLI---LGELEASEGII------------KHSGRVSFSSQISWIMPG-TI 502
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIhyngipykefaeKYPGEIIYVSEEDVHFPTlTV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIFgvsydeyryksvvkACQLQeditkfaeQDNTVLGeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:cd03233 101 RETLDF--------------ALRCK--------GNEFVRG-----ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 583 EEQIFeSCVcKLMASKTRILVTSKMEQ-----LKKADKILILHEGSSYFYG 628
Cdd:cd03233 154 ALEIL-KCI-RTMADVLKTTTFVSLYQasdeiYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1218-1419 |
6.44e-10 |
|
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: 61.10 E-value: 6.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1218 DGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDGVSWNSmtLQEWRKAFGVITQKVFIF 1292
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTL----LRLIAgfetpTSGEILLDGKDITN--LPPHKRPVNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1293 SG-TFRQN----LDPNGKWRDEEIWKVA---DQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:cd03300 85 PHlTVFENiafgLRLKKLPKAEIKERVAealDLVQLEGYANRKPSQ-----------LSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1365 LDEPSANLDPITYQVIRRVLR--QAFAGCTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKrlQKELGITFVFVTHdQEEALTMSDRIAVMNKGKIQQ 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
438-622 |
8.14e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 61.01 E-value: 8.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLL-----MLILGELEASEGIIKHSGRVSFSSQISWI-----------MPG- 500
Cdd:PRK14267 17 NHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfnrLLELNEEARVEGEVRLFGRNIYSPDVDPIevrrevgmvfqYPNp 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 ----TIKENIIFGVsydeyRYKSVVKACQLQEDITKFAEQDNTV-------LGEGGVTLSGGQRARISLARAVYKDADLY 569
Cdd:PRK14267 97 fphlTIYDNVAIGV-----KLNGLVKSKKELDERVEWALKKAALwdevkdrLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 570 LLDSPFGYLDVLTEEQIfESCVCKLMASKTRILVT-SKMEQLKKADKILILHEG 622
Cdd:PRK14267 172 LMDEPTANIDPVGTAKI-EELLFELKKEYTIVLVThSPAQAARVSDYVAFLYLG 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1206-1429 |
9.41e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.92 E-value: 9.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN---------IK-GEIQIDGvswnSMTL 1275
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTL----LRCINlleqpeagtIRvGDITIDT----ARSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1276 QEWRKAFGVITQKV-FIFSGTfrqNLDPN---------------GKWRDEEIW---KVADQVGLKSVIEQFPGQlnftlv 1336
Cdd:PRK11264 74 SQQKGLIRQLRQHVgFVFQNF---NLFPHrtvleniiegpvivkGEPKEEATArarELLAKVGLAGKETSYPRR------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1337 dggyvLSHGHKQLMCLARSVLSKAKIILLDEPSANLDP-ITYQVIRRVLRQAFAGCTVVLCEHRIEAMLD-CQRFLVIEQ 1414
Cdd:PRK11264 145 -----LSGGQQQRVAIARALAMRPEVILFDEPTSALDPeLVGEVLNTIRQLAQEKRTMVIVTHEMSFARDvADRAIFMDQ 219
|
250
....*....|....*
gi 91982740 1415 GNVWQYESLQALLSE 1429
Cdd:PRK11264 220 GRIVEQGPAKALFAD 234
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1223-1398 |
1.26e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.62 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFGVITQ--------KVFIFSG 1294
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQqqsppfamPVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 TFRQnldpngkwrdeeiwKVADQVGLKSVIEQFPGQLNFTLVDGGYV--LSHGHKQLMCLARSVL-------SKAKIILL 1365
Cdd:COG4138 92 LHQP--------------AGASSEAVEQLLAQLAEALGLEDKLSRPLtqLSGGEWQRVRLAAVLLqvwptinPEGQLLLL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 91982740 1366 DEPSANLDpITYQVI-RRVLRQ-AFAGCTVVLCEH 1398
Cdd:COG4138 158 DEPMNSLD-VAQQAAlDRLLRElCQQGITVVMSSH 191
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1223-1417 |
1.27e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 61.64 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-I----KGEIQIDGvswnsMTLQEWRKAF----GVitqkVFifs 1293
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTT----IKMLTgIlvptSGEVRVLG-----YVPFKRRKEFarriGV----VF--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1294 GTfRQNLdpngkWRD----------EEIWKVADQVgLKSVIEQFPGQLNFtlvdGGYV------LSHGHKQLMCLARSVL 1357
Cdd:COG4586 102 GQ-RSQL-----WWDlpaidsfrllKAIYRIPDAE-YKKRLDELVELLDL----GELLdtpvrqLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 1358 SKAKIILLDEPSANLDPITYQVIRRVLRQ--AFAGCTVVLCEHR---IEAMldCQRFLVIEQGNV 1417
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDmddIEAL--CDRVIVIDHGRI 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
439-633 |
1.28e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.80 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVsFSSQISW----------------IMPGTI 502
Cdd:PRK13635 21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV-LSEETVWdvrrqvgmvfqnpdnqFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIF-----GVSYDEY--RYKSVVKACQLQEditkFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:PRK13635 100 QDDVAFgleniGVPREEMveRVDQALRQVGMED----FLNREPH-------RLSGGQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 576 GYLDVLTEEQIFEscVCKLMASKTRILV---TSKMEQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13635 169 SMLDPRGRREVLE--TVRQLKEQKGITVlsiTHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
438-639 |
1.31e-09 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.80 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLM----LILGE------LEASEGIIKHSGRVSFSSQISWIMPG------- 500
Cdd:PRK09984 17 HQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDksagshIELLGRTVQREGRLARDIRKSRANTGyifqqfn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -----TIKENIIFGVSYDE------YRYKSVVKACQLQEDITK-----FAEQDNTvlgeggvTLSGGQRARISLARAVYK 564
Cdd:PRK09984 97 lvnrlSVLENVLIGALGSTpfwrtcFSWFTREQKQRALQALTRvgmvhFAHQRVS-------TLSGGQQQRVAIARALMQ 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 565 DADLYLLDSPFGYLDVLTEEQIFEScvCKLMASKTRILVTSKMEQ----LKKADKILILHEGSSYFYGTFSELQSLRPD 639
Cdd:PRK09984 170 QAKVILADEPIASLDPESARIVMDT--LRDINQNDGITVVVTLHQvdyaLRYCERIVALRQGHVFYDGSSQQFDNERFD 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
441-633 |
1.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 60.90 E-value: 1.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-RVSFSSQISWIMPGTIKENIIFGVSYDEYRYKS 519
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDiVVSSTSKQKEIKPVRKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 520 VVKACQL--------QEDITKFAEQDNTVLG-------EGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV---L 581
Cdd:PRK13643 102 VLKDVAFgpqnfgipKEKAEKIAAEKLEMVGladefweKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPkarI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 582 TEEQIFESCvckLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13643 182 EMMQLFESI---HQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1222-1270 |
1.67e-09 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 60.10 E-value: 1.67e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDG-VSW 1270
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTL----LKLIAgilepTSGRVEVNGrVSA 91
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
441-636 |
1.83e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 60.15 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII----------------KHSGRVsFSSQISWIMPGTIKE 504
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaitddnfeklrKHIGIV-FQNPDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFG-----VSYDEyrYKSVVKACQLQEDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13648 104 DVAFGlenhaVPYDE--MHRRVSEALKQVDMLERADYEPN-------ALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 580 VLTEEQIFeSCVCKLMASK--TRILVTSKMEQLKKADKILILHEGSSYFYGT----FSELQSL 636
Cdd:PRK13648 175 PDARQNLL-DLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTpteiFDHAEEL 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1223-1398 |
2.30e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 2.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQEWRKAFGVITQK--------VFIFSG 1294
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQqtppfampVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 TFRQNLDPNGKWRDeEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVL-------SKAKIILLDE 1367
Cdd:PRK03695 92 LHQPDKTRTEAVAS-ALNEVAEALGLDDKLGRSVNQ-----------LSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 91982740 1368 PSANLDpIT-----YQVIRRVLRQafaGCTVVLCEH 1398
Cdd:PRK03695 160 PMNSLD-VAqqaalDRLLSELCQQ---GIAVVMSSH 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
438-623 |
2.33e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.72 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLI-------LGEL----------EASEGIIKHSGRVSFssQISWIMPG 500
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkleeitSGDLivdglkvndpKVDERLIRQEAGMVF--QQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 -TIKENIIFGVSydEYRYKSVVKACQLQEDITK---FAEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK09493 92 lTALENVMFGPL--RVRGASKEEAEKQARELLAkvgLAERAHHYPSE----LSGGQQQRVAIARALAVKPKLMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 577 YLDV-LTEEqifescVCKLMAS-----KTRILVTSKMEQLKKA-------DKILILHEGS 623
Cdd:PRK09493 166 ALDPeLRHE------VLKVMQDlaeegMTMVIVTHEIGFAEKVasrlifiDKGRIAEDGD 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
395-589 |
2.44e-09 |
|
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: 61.74 E-value: 2.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 395 ENVTAFWEEGFQEL--LEKVQLNNDDRKTSNgenhLSfSHLCLVGNPVLK---NINLNIKKGEMLAITGSTGAGKTSLLM 469
Cdd:TIGR03269 254 DEVVAVFMEGVSEVekECEVEVGEPIIKVRN----VS-KRYISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 470 LILGELEASegiikhSGRVSFSSQISWI--------MPGTIKENI-IFGVSYDEYRYKSVVKacQLQEDIT-----KFA- 534
Cdd:TIGR03269 329 IIAGVLEPT------SGEVNVRVGDEWVdmtkpgpdGRGRAKRYIgILHQEYDLYPHRTVLD--NLTEAIGlelpdELAr 400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 535 --------------EQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFES 589
Cdd:TIGR03269 401 mkavitlkmvgfdeEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHS 469
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
437-560 |
2.83e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.96 E-value: 2.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPGTIK 503
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGedistlkpeiyrqQVSYCAQTPTLFGDTVY 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 504 ENIIFGVsydEYRYKSVVKAcQLQEDITKFaEQDNTVLGEGGVTLSGGQRARISLAR 560
Cdd:PRK10247 99 DNLIFPW---QIRNQQPDPA-IFLDDLERF-ALPDTILTKNIAELSGGEKQRISLIR 150
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1218-1398 |
3.62e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 3.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1218 DGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLniKGEIQIDG--VSWNSMTLQEWRKAFGvitQKVFiFSG- 1294
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSL----LRIL--AGLARPDAgeVLWQGEPIRRQRDEYH---QDLL-YLGh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 --------TFRQNLDPN----GKWRDEEIWKVADQVGLKSViEQFPGQlnftlvdggyVLSHGHKQLMCLARSVLSKAKI 1362
Cdd:PRK13538 82 qpgiktelTALENLRFYqrlhGPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPL 150
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982740 1363 ILLDEPSANLDPI-TYQVIRRVLRQAFAGCTVVLCEH 1398
Cdd:PRK13538 151 WILDEPFTAIDKQgVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
439-672 |
4.62e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 59.33 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG-----------------IIKHSGRVsFSSQISWIMPGT 501
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvyvdgldtsdeenlwdIRNKAGMV-FQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENIIFG-----VSYDEYRYK--SVVKACQLQEdITKFAEQdntvlgeggvTLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:PRK13633 103 VEEDVAFGpenlgIPPEEIRERvdESLKKVGMYE-YRRHAPH----------LLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 575 FGYLDVLTEEQIFESCvcKLMASK---TRILVTSKMEQLKKADKILILHEGSSYFYGT----FSELQSLrpdfssKLMGY 647
Cdd:PRK13633 172 TAMLDPSGRREVVNTI--KELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTpkeiFKEVEMM------KKIGL 243
|
250 260
....*....|....*....|....*
gi 91982740 648 DTfDQFTEerrssiLTETLRRFSVD 672
Cdd:PRK13633 244 DV-PQVTE------LAYELKKEGVD 261
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1208-1401 |
5.03e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQID-----------GVSWNSMTL 1275
Cdd:PRK11248 4 ISHLYADY--GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDgkpvegpgaerGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1276 QEWRK-----AFGVITQKVfifsgtfrqnldPNGKwRDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLM 1350
Cdd:PRK11248 82 LPWRNvqdnvAFGLQLAGV------------EKMQ-RLEIAHQMLKKVGLEGAEKRYIWQL-----------SGGQRQRV 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1351 CLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA--GCTVVLCEHRIE 1401
Cdd:PRK11248 138 GIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITHDIE 190
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
439-579 |
5.11e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII----KHSGRVSFSSQISWI--MPG-----TIKENII 507
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgKTATRGDRSRFMAYLghLPGlkadlSTLENLH 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 508 FGVSYDEYRYKSVVKACQLqedITKFAEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK13543 105 FLCGLHGRRAKQMPGSALA---IVGLAGYEDTLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
437-579 |
5.11e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.61 E-value: 5.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLI------------LGELE--------ASEGIIKH-SGRVSFSSQIS 495
Cdd:PRK11264 15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITidtarslsQQKGLIRQlRQHVGFVFQNF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 496 WIMPG-TIKENIIFGvsydeyryKSVVKAcQLQEDITKFAEQdntVLGEGGVT---------LSGGQRARISLARAVYKD 565
Cdd:PRK11264 95 NLFPHrTVLENIIEG--------PVIVKG-EPKEEATARARE---LLAKVGLAgketsyprrLSGGQQQRVAIARALAMR 162
|
170
....*....|....
gi 91982740 566 ADLYLLDSPFGYLD 579
Cdd:PRK11264 163 PEVILFDEPTSALD 176
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
440-622 |
5.53e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.83 E-value: 5.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPG------ 500
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlKVADKNQLRLLRTRltmvfq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 --------TIKENI------IFGVSYDEYRYKSVVKACQLqeDITKFAEqdntvlGEGGVTLSGGQRARISLARAVYKDA 566
Cdd:PRK10619 100 hfnlwshmTVLENVmeapiqVLGLSKQEARERAVKYLAKV--GIDERAQ------GKYPVHLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 567 DLYLLDSPFGYLDvltEEQIFEscVCKLMAS-----KTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:PRK10619 172 EVLLFDEPTSALD---PELVGE--VLRIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQG 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1208-1399 |
6.43e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 6.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDdgNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSwnsmtLQEWRKAFgvit 1286
Cdd:PRK13540 4 VIELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPeKGEILFERQS-----IKKDLCTY---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSGtFRQNLDPNGKWRDE---EIWKVADQVGLKSVIEQFpgQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAKII 1363
Cdd:PRK13540 73 QKQLCFVG-HRSGINPYLTLRENclyDIHFSPGAVGITELCRLF--SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982740 1364 LLDEPSANLDPITYQVI-RRVLRQAFAGCTVVLCEHR 1399
Cdd:PRK13540 150 LLDEPLVALDELSLLTIiTKIQEHRAKGGAVLLTSHQ 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1208-1417 |
6.66e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.95 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNA-ILENISFSISPGQRVGLLGRTGSGKST---LLSAFLRmlNIKGEIQIDGVSWNSMTLQEWRKAFG 1283
Cdd:PRK13642 7 VENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFE--EFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKV-FIFSGTFRQN-----LDPNGKWRDEEIWKVADqvGLKSVieqfpGQLNFTLVDGGYvLSHGHKQLMCLARSVL 1357
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDdvafgMENQGIPREEMIKRVDE--ALLAV-----NMLDFKTREPAR-LSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1358 SKAKIILLDEPSANLDPITYQVIRRVLRQAFAG--CTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEI 218
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
438-579 |
7.77e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 59.35 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-VSFSS----------QISWIMPG-TIKEN 505
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdVTHRSiqqrdicmvfQSYALFPHmSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 I-----IFGVSYDEyRYKSVVKACQLQ-----EDitKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPF 575
Cdd:PRK11432 99 VgyglkMLGVPKEE-RKQRVKEALELVdlagfED--RYVDQ-----------ISGGQQQRVALARALILKPKVLLFDEPL 164
|
....
gi 91982740 576 GYLD 579
Cdd:PRK11432 165 SNLD 168
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1222-1417 |
1.07e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 59.68 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRMLNIK--GEIQIDGVSWNSMTLQEwRKAFgVITQKVFI------ 1291
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNalAFRSPKGVKgsGSVLLNGMPIDAKEMRA-ISAY-VQQDDLFIptltvr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1292 ----FSGTFRQNLDPNGKWRDEEIWKVADQVGLKS---VIEQFPGQLNftlvdggyVLSHGHKQLMCLARSVLSKAKIIL 1364
Cdd:TIGR00955 118 ehlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKcanTRIGVPGRVK--------GLSGGERKRLAFASELLTDPPLLF 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1365 LDEPSANLDPIT-YQVIRRVLRQAFAGCTVVLCEHRIEAMLDCQ--RFLVIEQGNV 1417
Cdd:TIGR00955 190 CDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSELFELfdKIILMAEGRV 245
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1199-1417 |
1.15e-08 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 59.74 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1199 TWPSGGEMVvkdltvkyvddgnAILENISFSISPGQRVGLLGRTGSGKSTLLSaFLRMLN--IKGEIQIDG---VSWNSM 1273
Cdd:PRK10535 13 SYPSGEEQV-------------EVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDkpTSGTYRVAGqdvATLDAD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1274 TLQEWRKA-FGVITQKVFIFSG-TFRQNLD-------PNGKWRDEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSH 1344
Cdd:PRK10535 79 ALAQLRREhFGFIFQRYHLLSHlTAAQNVEvpavyagLERKQRLLRAQELLQRLGLEDRVEYQPSQ-----------LSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1345 GHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRIEAMLDCQRFLVIEQGNV 1417
Cdd:PRK10535 148 GQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
440-580 |
1.28e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 57.43 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG--RVSFSSQ-----------ISWIM---PGTIK 503
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGklRIGYVPQklyldttlpltVNRFLrlrPGTKK 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 504 ENIIFGVsydeyryKSVVKACQLQEDITKfaeqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK09544 99 EDILPAL-------KRVQAGHLIDAPMQK---------------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDV 153
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
440-635 |
1.41e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 57.81 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWI--MP---G-----TIKENIIF- 508
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgyLPeerGlypkmKVGEQLVYl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 509 ----GVSydeyryKSVVKAcQLQEDITKF--AEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGYLDV-- 580
Cdd:COG4152 96 arlkGLS------KAEAKR-RADEWLERLglGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPFSGLDPvn 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 581 --LTEEQIFEscvckLMAS-KTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSELQS 635
Cdd:COG4152 165 veLLKDVIRE-----LAAKgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRR 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1213-1386 |
1.46e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1213 VKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFI 1291
Cdd:PRK10247 13 VGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISpTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1292 FSGTFRQNL-----------DPNGKWRDEEIWKVADQVGLKSVIEqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKA 1360
Cdd:PRK10247 93 FGDTVYDNLifpwqirnqqpDPAIFLDDLERFALPDTILTKNIAE----------------LSGGEKQRISLIRNLQFMP 156
|
170 180 190
....*....|....*....|....*....|
gi 91982740 1361 KIILLDEPSANLDP----ITYQVIRRVLRQ 1386
Cdd:PRK10247 157 KVLLLDEITSALDEsnkhNVNEIIHRYVRE 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-633 |
1.68e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.36 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRV-SFSSQISWIMPGTIKENI--IFGVS----- 511
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVlYFGKDIFQIDAIKLRKEVgmVFQQPnpfph 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 512 ---YDEYRYKSVVKACQLQEDITKFAEQDNTVLG----------EGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYL 578
Cdd:PRK14246 105 lsiYDNIAYPLKSHGIKEKREIKKIVEECLRKVGlwkevydrlnSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 579 DVLTEEQIfESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK14246 185 DIVNSQAI-EKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1208-1373 |
1.70e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 56.42 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVkyVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSwnsmtlQEWRKAFGVIT 1286
Cdd:PRK13539 5 GEDLAC--VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPaAGTIKLDGGD------IDDPDVAEACH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 qkvfiFSG---------TFRQNLDpngKWR------DEEIWKVADQVGLKSVIEqfpgqlnftlVDGGYvLSHGHKQLMC 1351
Cdd:PRK13539 77 -----YLGhrnamkpalTVAENLE---FWAaflggeELDIAAALEAVGLAPLAH----------LPFGY-LSAGQKRRVA 137
|
170 180
....*....|....*....|..
gi 91982740 1352 LARSVLSKAKIILLDEPSANLD 1373
Cdd:PRK13539 138 LARLLVSNRPIWILDEPTAALD 159
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1208-1413 |
2.37e-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: 56.65 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvDDGNAILENISFSISPGQRVGLLGRTGSGKSTllsaFLRML--NIK---GEIQIDG--VSWNSMTLqewrK 1280
Cdd:cd03237 1 YTYPTMKK-TLGEFTLEVEGGSISESEVIGILGPNGIGKTT----FIKMLagVLKpdeGDIEIELdtVSYKPQYI----K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVITQKVFIFSGTFRQNLDPngKWRDEeiwkVADQVGLKSVIEQfpgQLNftlvdggyVLSHGHKQLMCLARSVLSKA 1360
Cdd:cd03237 72 ADYEGTVRDLLSSITKDFYTHP--YFKTE----IAKPLQIEQILDR---EVP--------ELSGGELQRVAIAACLSKDA 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1361 KIILLDEPSANLDP----ITYQVIRRVLRQAFAGCTVVlcEHRIeAMLD--CQRFLVIE 1413
Cdd:cd03237 135 DIYLLDEPSAYLDVeqrlMASKVIRRFAENNEKTAFVV--EHDI-IMIDylADRLIVFE 190
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1208-1415 |
2.39e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 56.92 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLNikGEIQIDGVSWNSM----------- 1273
Cdd:PRK11300 8 VSGLMMRF--GGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVfncLTGFYKPTG--GTILLRGQHIEGLpghqiarmgvv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1274 -TLQEWR--KAFGVITQ---------KVFIFSGTF---------RQNLDPNGKWrdeeiwkvADQVGLKSVIEQFPGQLn 1332
Cdd:PRK11300 84 rTFQHVRlfREMTVIENllvaqhqqlKTGLFSGLLktpafrraeSEALDRAATW--------LERVGLLEHANRQAGNL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1333 ftlvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPSANLDP---ITYQVIRRVLRQAFaGCTVVLCEHRIEAMLD-CQR 1408
Cdd:PRK11300 155 ----------AYGQQRRLEIARCMVTQPEILMLDEPAAGLNPketKELDELIAELRNEH-NVTVLLIEHDMKLVMGiSDR 223
|
....*..
gi 91982740 1409 FLVIEQG 1415
Cdd:PRK11300 224 IYVVNQG 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1206-1417 |
2.44e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 56.63 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDG---VSWNSMTLqewrka 1281
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPdSGEVLVDGldvATTPSREL------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 fgviTQKVFIfsgtFRQNLDPNGKWRdeeiwkVADQVGL--------------KSVIEQFPGQLNFTLVDGGYV--LSHG 1345
Cdd:COG4604 74 ----AKRLAI----LRQENHINSRLT------VRELVAFgrfpyskgrltaedREIIDEAIAYLDLEDLADRYLdeLSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1346 HKQL----MCLARSvlskAKIILLDEPSANLDPITYQVIRRVLRQAF--AGCTVVLCEH----------RIEAMLDCQrf 1409
Cdd:COG4604 140 QRQRafiaMVLAQD----TDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHdinfascyadHIVAMKDGR-- 213
|
....*...
gi 91982740 1410 lVIEQGNV 1417
Cdd:COG4604 214 -VVAQGTP 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
441-656 |
2.47e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.03 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR---------------VSFSSQISWIMPGTIKEN 505
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGElltaenvwnlrrkigMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 IIFGVSYDEYRYKSVVKACQ---LQEDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRVDealLAVNMLDFKTREPA-------RLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 583 EEQIFEscVCKLMASK---TRILVTSKMEQLKKADKILILHEGSSYFYGTFSELQSLRPD---------FSSKLM----- 645
Cdd:PRK13642 176 RQEIMR--VIHEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDmveigldvpFSSNLMkdlrk 253
|
250
....*....|..
gi 91982740 646 -GYDTFDQFTEE 656
Cdd:PRK13642 254 nGFDLPEKYLSE 265
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
441-633 |
2.51e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.10 E-value: 2.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-----------------RVSFSSQI--SWIMPGT 501
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvrkRIGMVFQFpeSQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 502 IKENIIFGVSYDEYRYKSV-VKACQLQEDItKFAEQdntVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK13646 103 VEREIIFGPKNFKMNLDEVkNYAHRLLMDL-GFSRD---VMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 581 LTEEQIFESC-VCKLMASKTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13646 179 QSKRQVMRLLkSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1206-1398 |
2.56e-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: 55.58 E-value: 2.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKyvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLniKGEIQIDG--VSWNSMTLQEWRKafg 1283
Cdd:cd03231 1 LEADELTCE--RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTL----LRIL--AGLSPPLAgrVLLNGGPLDFQRD--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 vITQKVFIFSG---------TFRQNLDpngKWR----DEEIWKVADQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLM 1350
Cdd:cd03231 70 -SIARGLLYLGhapgikttlSVLENLR---FWHadhsDEQVEEALARVGLNGFEDRPVAQ-----------LSAGQQRRV 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 91982740 1351 CLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEH 1398
Cdd:cd03231 135 ALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGhCARGGMVVLTTH 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
437-637 |
2.79e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.01 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----------------VSFSSQISWIMP 499
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpikydkksllevrktvgIVFQNPDDQLFA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 GTIKENIIFG-----VSYDEY--RYKSVVKACQLqEDITKFAEQDntvlgeggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:PRK13639 94 PTVEEDVAFGplnlgLSKEEVekRVKEALKAVGM-EGFENKPPHH----------LSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 573 SPFGYLDVLTEEQIFescvcKLM-----ASKTRILVTSKMEQLKK-ADKILILHEGSSYFYGT----FSELQSLR 637
Cdd:PRK13639 163 EPTSGLDPMGASQIM-----KLLydlnkEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTpkevFSDIETIR 232
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1209-1398 |
2.81e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 58.44 E-value: 2.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1209 KDLTVKYVDDGNAiLENISFSISPGQRVGLLGRTGSGKSTlLSAFLRMLN--IKGEIQIDGVSWNSMTLQEWRKAFGVIT 1286
Cdd:PRK10522 326 RNVTFAYQDNGFS-VGPINLTIKRGELLFLIGGNGSGKST-LAMLLTGLYqpQSGEILLDGKPVTAEQPEDYRKLFSAVF 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSgtfrQNLDPNGKWRDEEIwkvadqvgLKSVIEQFPGQLNFTLVDGGYV---LSHGHKQLMCLARSVLSKAKII 1363
Cdd:PRK10522 404 TDFHLFD----QLLGPEGKPANPAL--------VEKWLERLKMAHKLELEDGRISnlkLSKGQKKRLALLLALAEERDIL 471
|
170 180 190
....*....|....*....|....*....|....*....
gi 91982740 1364 LLDEPSANLDP----ITYQVIRRVLRQafAGCTVVLCEH 1398
Cdd:PRK10522 472 LLDEWAADQDPhfrrEFYQVLLPLLQE--MGKTIFAISH 508
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
441-633 |
3.23e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 57.74 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-----------------RVSFSSQISWIMPG-TI 502
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaelrevrrkKIAMVFQSFALMPHmTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIFGVSYdeyrykSVVKACQLQE---DITKFAEQDNTVLGEGGvTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:PRK10070 124 LDNTAFGMEL------AGINAEERREkalDALRQVGLENYAHSYPD-ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 580 VLTEEQIFESCVcKLMASKTRILVTSKM---EQLKKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK10070 197 PLIRTEMQDELV-KLQAKHQRTIVFISHdldEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
424-622 |
4.11e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 57.71 E-value: 4.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 424 GENHLSFSHLClvgNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR--VSFSSQ------IS 495
Cdd:PRK10762 254 GEVRLKVDNLS---GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHevVTRSPQdglangIV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 496 WIMPGTIKENIIFGVSYDE------YRYKSvVKACQLQEDITKFAEQD------------NTVLGEggvtLSGGQRARIS 557
Cdd:PRK10762 331 YISEDRKRDGLVLGMSVKEnmsltaLRYFS-RAGGSLKHADEQQAVSDfirlfniktpsmEQAIGL----LSGGNQQKVA 405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 558 LARAVYKDADLYLLDSPFGYLDVLTEEQIFEsCVCKLMASK-TRILVTSKM-EQLKKADKILILHEG 622
Cdd:PRK10762 406 IARGLMTRPKVLILDEPTRGVDVGAKKEIYQ-LINQFKAEGlSIILVSSEMpEVLGMSDRILVMHEG 471
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
441-644 |
4.38e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 57.75 E-value: 4.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEAS---EGIIKHSGRVSFSSQISWI----------MPG-TIKENI 506
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIsayvqqddlfIPTlTVREHL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IF--------GVSYDEYRYKsvVKACQLQEDITKFAeqdNTVLGEGGVT--LSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:TIGR00955 121 MFqahlrmprRVTKKEKRER--VDEVLQALGLRKCA---NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 577 YLDVLTEEQIFEscVCKLMASKTRILVTS-------KMEQLkkaDKILILHEGSSYFYGTFSELqslrPDFSSKL 644
Cdd:TIGR00955 196 GLDSFMAYSVVQ--VLKGLAQKGKTIICTihqpsseLFELF---DKIILMAEGRVAYLGSPDQA----VPFFSDL 261
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1207-1386 |
5.03e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 55.42 E-value: 5.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsaFlRMLN--IK---GEIQIDGVSWNSMTL-QEWRK 1280
Cdd:COG1137 5 EAENLVKSY--GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT---F-YMIVglVKpdsGRIFLDGEDITHLPMhKRARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVITQKVFIFSG-TFRQNL-------DPNGKWRDEEIWKVADQVGLKSVIEQFpgqlnftlvdgGYVLSHGHKQLMCL 1352
Cdd:COG1137 79 GIGYLPQEASIFRKlTVEDNIlavlelrKLSKKEREERLEELLEEFGITHLRKSK-----------AYSLSGGERRRVEI 147
|
170 180 190
....*....|....*....|....*....|....
gi 91982740 1353 ARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQ 1386
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIIRH 181
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
437-633 |
5.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 56.01 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASegiikhSGRVSFSSQ-ISWIMPGTIK------------ 503
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPS------SGRILFDGKpIDYSRKGLMKlresvgmvfqdp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFGVS-YDEYRYKSVvkACQLQEDitKFAEQDNTVLGEGGVT---------LSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK13636 92 DNQLFSASvYQDVSFGAV--NLKLPED--EVRKRVDNALKRTGIEhlkdkpthcLSFGQKKRVAIAGVLVMEPKVLVLDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 574 PFGYLDVLTEEQIFEscVCKLMASK---TRILVTSKMEQLK-KADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13636 168 PTAGLDPMGVSEIMK--LLVEMQKElglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEV 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1223-1419 |
5.69e-08 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 56.97 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWR-----------KAFGVITQKVF 1290
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELRevrrkkiamvfQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 IFSGTFRQNL-DPNGKWRDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPS 1369
Cdd:PRK10070 124 LDNTAFGMELaGINAEERREKALDALRQVGLENYAHSYPDEL-----------SGGMRQRVGLARALAINPDILLMDEAF 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1370 ANLDPITYQVIRRVL--RQAFAGCTVVLCEHRI-EAMLDCQRFLVIEQGNVWQ 1419
Cdd:PRK10070 193 SALDPLIRTEMQDELvkLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQ 245
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
437-622 |
5.71e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.58 E-value: 5.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG---I-------IKHSGR-VSFSSQISWIMPG-TIKE 504
Cdd:PRK11000 15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGdlfIgekrmndVPPAERgVGMVFQSYALYPHlSVAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVSYdeyrykSVVKACQLQEDITKFAE--QDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLT 582
Cdd:PRK11000 95 NMSFGLKL------AGAKKEEINQRVNQVAEvlQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 91982740 583 EEQIfESCVCKLMA--SKTRILVT-SKMEQLKKADKILILHEG 622
Cdd:PRK11000 169 RVQM-RIEISRLHKrlGRTMIYVThDQVEAMTLADKIVVLDAG 210
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
437-629 |
5.88e-08 |
|
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: 57.72 E-value: 5.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-----VSFSSQISWIMPG--------TIK 503
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKdietnLDAVRQSLGMCPQhnilfhhlTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 504 ENIIFgvsYDEYRYKSVVKAcQLQEDitkfAEQDNTVL----GEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLD 579
Cdd:TIGR01257 1022 EHILF---YAQLKGRSWEEA-QLEME----AMLEDTGLhhkrNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 91982740 580 VLTEEQIFEsCVCKLMASKTRILVTSKMEQLK-KADKILILHEGSSYFYGT 629
Cdd:TIGR01257 1094 PYSRRSIWD-LLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
441-619 |
6.04e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSlLMLIL-GELEASEGIIKHSGR-VSFSSqiswimPG------------------ 500
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKST-LMKILyGLYQPDSGEILIDGKpVRIRS------PRdaialgigmvhqhfmlvp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 --TIKENIIFGVsydEYRYKSVVKACQLQEDITKFAEQ-------DNTVlgeggVTLSGGQRARISLARAVYKDADLYLL 571
Cdd:COG3845 94 nlTVAENIVLGL---EPTKGGRLDRKAARARIRELSERygldvdpDAKV-----EDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 572 DSPFGyldVLTEEQI---FEscVCKLMAS--KTRILVTSKMEQLKK-ADKILIL 619
Cdd:COG3845 166 DEPTA---VLTPQEAdelFE--ILRRLAAegKSIIFITHKLREVMAiADRVTVL 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
425-623 |
6.55e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.96 E-value: 6.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 425 ENHLSFSHLCLV----GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGEL---EASEGIIKHSGrVSFSSQISW- 496
Cdd:PRK13640 3 DNIVEFKHVSFTypdsKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDG-ITLTAKTVWd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 497 ---------------IMPGTIKENIIFGVsydEYR------YKSVVKACQLQEDITKFAEQDNTvlgeggvTLSGGQRAR 555
Cdd:PRK13640 82 irekvgivfqnpdnqFVGATVGDDVAFGL---ENRavprpeMIKIVRDVLADVGMLDYIDSEPA-------NLSGGQKQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 556 ISLARAVYKDADLYLLDSPFGYLDVLTEEQIFeSCVCKLMASK--TRILVTSKMEQLKKADKILILHEGS 623
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQIL-KLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGK 220
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1218-1419 |
7.08e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.49 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1218 DGNAILENISFSISPGQRVGLLGRTGSGKSTLLS--AFLRMLNiKGEIQIDGVSWNS--------------------MTL 1275
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRliAGFETPD-SGRIMLDGQDITHvpaenrhvntvfqsyalfphMTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1276 QEwRKAFGVITQKVfifsgtfrqnldPNgkwrdEEIWK-VAD---QVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMC 1351
Cdd:PRK09452 104 FE-NVAFGLRMQKT------------PA-----AEITPrVMEalrMVQLEEFAQRKPHQ-----------LSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1352 LARSVLSKAKIILLDEPSANLDpitYQV-------IRRVLRQafAGCTVVLCEHRIE---AMLDcqRFLVIEQGNVWQ 1419
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALD---YKLrkqmqneLKALQRK--LGITFVFVTHDQEealTMSD--RIVVMRDGRIEQ 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1223-1415 |
7.21e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.72 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLsaflRMLN-----IKGEIQIDGVSWNSMTLQEWRK-AFGVITQKV-FIFSGT 1295
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLM----KVLSgihepTKGTITINNINYNKLDHKLAAQlGIGIIYQELsVIDELT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1296 FRQNLDPnGKWRDEEIWKV---------------ADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKA 1360
Cdd:PRK09700 97 VLENLYI-GRHLTKKVCGVniidwremrvraammLLRVGLKVDLDEKVANL-----------SISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1361 KIILLDEPSANL--DPITYQ-VIRRVLRQafAGCTVVLCEHRIEAMLD-CQRFLVIEQG 1415
Cdd:PRK09700 165 KVIIMDEPTSSLtnKEVDYLfLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDG 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1208-1428 |
8.01e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.51 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKY-VDDGNAILENISFSISPGQRVGLLGRTGSGKST---LLSAFLRMLNikGEIQIDGVSWNSMTLQEWRKAFG 1283
Cdd:PRK13650 7 VKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAES--GQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1284 VITQKV-FIFSGTFRQN-----LDPNGKWRDEEIWKVA---DQVGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLAR 1354
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDdvafgLENKGIPHEEMKERVNealELVGMQDFKEREPAR-----------LSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1355 SVLSKAKIILLDEPSANLDPI----TYQVIRRVlRQAFaGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQYESLQALLS 1428
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEgrleLIKTIKGI-RDDY-QMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1223-1412 |
8.32e-08 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 56.57 E-value: 8.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsaflrmlnIK----------GEIQIDG--VSWNSmTLQEWRKAFGVITQKVF 1290
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTL---------MKilsgvyqpdsGEILLDGepVRFRS-PRDAQAAGIAIIHQELN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 IFSG-TFRQNL----DPNGKW--RDEEIWKVADQVgLKSVieqfpgQLNF---TLVDGgyvLSHGHKQLMCLARSVLSKA 1360
Cdd:COG1129 90 LVPNlSVAENIflgrEPRRGGliDWRAMRRRAREL-LARL------GLDIdpdTPVGD---LSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1361 KIILLDEPSANLDP----ITYQVIRRvLRQafAGCTVVLCEHRIEAMLD-CQRFLVI 1412
Cdd:COG1129 160 RVLILDEPTASLTEreveRLFRIIRR-LKA--QGVAIIYISHRLDEVFEiADRVTVL 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
440-622 |
8.95e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 55.48 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLL----MLILGELEASEGIIKHSGRVSFSSQISWIMP---------------- 499
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIehlnALLLPDTGTIEWIFKDEKNKKKTKEKEKVLEklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 -------------------GTIKENIIFG-VSYdeyrykSVVK--ACQLQEDITKFAEQDNTVLGEGGVTLSGGQRARIS 557
Cdd:PRK13651 102 eirrrvgvvfqfaeyqlfeQTIEKDIIFGpVSM------GVSKeeAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 558 LARAVYKDADLYLLDSPFGYLD-VLTEE--QIFEscvcKLMAS-KTRILVTSKMEQ-LKKADKILILHEG 622
Cdd:PRK13651 176 LAGILAMEPDFLVFDEPTAGLDpQGVKEilEIFD----NLNKQgKTIILVTHDLDNvLEWTKRTIFFKDG 241
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
440-622 |
9.44e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.92 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLI--LGEL--EAS-EG-------------IIKHSGRVSFSSQISWIMPG- 500
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELypEARvSGevyldgqdifkmdVIELRRRVQMVFQIPNPIPNl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENIIFGVSYD---------EYRYKSVVKACQLQEDItkfaeqdNTVLGEGGVTLSGGQRARISLARAVYKDADLYLL 571
Cdd:PRK14247 98 SIFENVALGLKLNrlvkskkelQERVRWALEKAQLWDEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 572 DSPFGYLDVLTEEQIfESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:PRK14247 171 DEPTANLDPENTAKI-ESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKG 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
438-622 |
9.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 438 NPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII---------------KHSGRVSFSSQISWIMPGTI 502
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenvwdiRHKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIF-----GVSYDEYRyKSVVKACQLQeDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDS---- 573
Cdd:PRK13650 100 EDDVAFglenkGIPHEEMK-ERVNEALELV-GMQDFKEREPA-------RLSGGQKQRVAIAGAVAMRPKIIILDEatsm 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 574 --PFGYLDVL-TEEQIFEScvcklmASKTRILVTSKMEQLKKADKILILHEG 622
Cdd:PRK13650 171 ldPEGRLELIkTIKGIRDD------YQMTVISITHDLDEVALSDRVLVMKNG 216
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
440-632 |
1.22e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 56.43 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEAS--EGIIKHSG---------RVSFSSQISWIMPG-TIKENII 507
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNrkptkqilkRTGFVTQDDILYPHlTVRETLV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 508 FGVSYDEYRYKSVVKACQLQEDITK---FAEQDNTVLGEGGVT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:PLN03211 163 FCSLLRLPKSLTKQEKILVAESVISelgLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 584 EQIFESCVCklMASKTRILVTSkMEQ-----LKKADKILILHEGSSYFYGTFSE 632
Cdd:PLN03211 243 YRLVLTLGS--LAQKGKTIVTS-MHQpssrvYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
439-621 |
1.52e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.25 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG-------------RVSFSSQISWIMPG-TIKE 504
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlarRLALLPQHHLTPEGiTVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFGVS-----------YDEYRyksVVKACQlQEDITKFAEQDNTvlgeggvTLSGGQRARISLARAVYKDADLYLLDS 573
Cdd:PRK11231 96 LVAYGRSpwlslwgrlsaEDNAR---VNQAME-QTRINHLADRRLT-------DLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 91982740 574 PFGYLDVltEEQIfescvcKLMasktrilvtSKMEQLKKADK--ILILHE 621
Cdd:PRK11231 165 PTTYLDI--NHQV------ELM---------RLMRELNTQGKtvVTVLHD 197
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1223-1417 |
1.62e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.74 E-value: 1.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQE----WRKAFGVITQ--KVFIFSGT 1295
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQfpESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1296 FRQNL---DPNGKWRDEEIWKVA----DQVGL-KSVIEQFPgqlnftlvdggYVLSHGHKQLMCLARSVLSKAKIILLDE 1367
Cdd:PRK13643 102 VLKDVafgPQNFGIPKEKAEKIAaeklEMVGLaDEFWEKSP-----------FELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1368 PSANLDPITYQVIRRVLRQAF-AGCTVVLCEHRIEAMLDCQRFL-VIEQGNV 1417
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHqSGQTVVLVTHLMDDVADYADYVyLLEKGHI 222
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
437-485 |
1.76e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 1.76e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHS 485
Cdd:PRK15064 331 NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS 379
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1223-1373 |
2.13e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDG-------VSWNS----MTLQEWRKAFGVITQKVF 1290
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELLIDDhplhfgdYSYRSqrirMIFQDPSTSLNPRQRISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 IFSGTFRQNLDPNGKWRDEEIWKVADQVGLksvieqFPGQLNFTlvdgGYVLSHGHKQLMCLARSVLSKAKIILLDEPSA 1370
Cdd:PRK15112 109 ILDFPLRLNTDLEPEQREKQIIETLRQVGL------LPDHASYY----PHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
...
gi 91982740 1371 NLD 1373
Cdd:PRK15112 179 SLD 181
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1206-1426 |
2.26e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 54.73 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVDdgNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDG--VSWNS-------MTL 1275
Cdd:PRK11432 7 VVLKNITKRFGS--NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKpTEGQIFIDGedVTHRSiqqrdicMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1276 QEW----------RKAFGVITQKVfifsgtfrqnldPNG--KWRDEEIWKVADQVGLKsviEQFPGQLnftlvdggyvlS 1343
Cdd:PRK11432 85 QSYalfphmslgeNVGYGLKMLGV------------PKEerKQRVKEALELVDLAGFE---DRYVDQI-----------S 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1344 HGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIR---RVLRQAFaGCTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMRekiRELQQQF-NITSLYVTHdQSEAFAVSDTVIVMNKGKIMQ 217
|
....*..
gi 91982740 1420 YESLQAL 1426
Cdd:PRK11432 218 IGSPQEL 224
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1219-1398 |
2.48e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1219 GNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQIDGVSWNSMTLQE---WRKAFGVITQKV-FIFS 1293
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSaGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHhLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1294 GTFRQN----LDPNGKWRDEEIWKVA---DQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:PRK10908 94 RTVYDNvaipLIIAGASGDDIRRRVSaalDKVGLLDKAKNFPIQL-----------SGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190
....*....|....*....|....*....|...
gi 91982740 1367 EPSANLDPITYQVIRRVLRQ-AFAGCTVVLCEH 1398
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEfNRVGVTVLMATH 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
437-584 |
2.63e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 55.34 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASegiikhSGRVSFssqiswimpGTIKEniifgVSY-DEY 515
Cdd:PRK11147 331 GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQAD------SGRIHC---------GTKLE-----VAYfDQH 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 516 RY-----KSVVkacqlqeditkfaeqDNtvLGEG-------GVT-----------------------LSGGQRARISLAR 560
Cdd:PRK11147 391 RAeldpeKTVM---------------DN--LAEGkqevmvnGRPrhvlgylqdflfhpkramtpvkaLSGGERNRLLLAR 453
|
170 180
....*....|....*....|....
gi 91982740 561 AVYKDADLYLLDSPFGYLDVLTEE 584
Cdd:PRK11147 454 LFLKPSNLLILDEPTNDLDVETLE 477
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1211-1267 |
2.63e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 53.68 E-value: 2.63e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1211 LTVKYVD---DGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL---------RMLNIKGEIQIDG 1267
Cdd:PRK13547 2 LTADHLHvarRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggapRGARVTGDVTLNG 70
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1206-1419 |
2.90e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 53.60 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQIDGVSWNSMTLQEWRKAFGV 1284
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1285 ITQK--------VFIFSGTF--RQNLDPNGKWRdEEIWKVADQVGLKSVIEQFPgqlnftlvdggYVLSHGHKQLMCLAR 1354
Cdd:PRK13648 88 VFQNpdnqfvgsIVKYDVAFglENHAVPYDEMH-RRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIAG 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1355 SVLSKAKIILLDEPSANLDPITYQ----VIRRVlrQAFAGCTVVLCEHRIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQnlldLVRKV--KSEHNITIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1222-1379 |
5.19e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQNL 1300
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1301 DPNGKWRDEEI---WKVADQVGLKSVIeQFPG--QLNFTLVDggyVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDpI 1375
Cdd:PRK10253 102 VARGRYPHQPLftrWRKEDEEAVTKAM-QATGitHLADQSVD---TLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD-I 176
|
....
gi 91982740 1376 TYQV 1379
Cdd:PRK10253 177 SHQI 180
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1208-1277 |
5.64e-07 |
|
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: 51.76 E-value: 5.64e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 1208 VKDLTVKyvDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFL---RMLNIKGEIQIDGVSWNSMTLQE 1277
Cdd:cd03217 3 IKDLHVS--VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghpKYEVTEGEILFKGEDITDLPPEE 73
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1214-1398 |
5.99e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 54.17 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1214 KYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLL------------SAFLrMLNIK-----GEIQID---GVSWNSM 1273
Cdd:TIGR03719 12 KVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLrimagvdkdfngEARP-QPGIKvgylpQEPQLDptkTVRENVE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1274 T-LQEWRKA---FGVITQKVFIFSGTFRQNLDPNGKWrdEEIWKVADQVGLKSVIEQF-------PGQLNFTlvdggyVL 1342
Cdd:TIGR03719 91 EgVAEIKDAldrFNEISAKYAEPDADFDKLAAEQAEL--QEIIDAADAWDLDSQLEIAmdalrcpPWDADVT------KL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1343 SHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQaFAGcTVVLCEH 1398
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTH 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1208-1280 |
6.96e-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: 53.92 E-value: 6.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNA--ILENISFSISPGQRVGLLGRTGSGKS-TLLSAfLRML-----NIKGEIQIDGVSWNSMTLQEWR 1279
Cdd:COG4172 9 VEDLSVAFGQGGGTveAVKGVSFDIAAGETLALVGESGSGKSvTALSI-LRLLpdpaaHPSGSILFDGQDLLGLSERELR 87
|
.
gi 91982740 1280 K 1280
Cdd:COG4172 88 R 88
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1222-1447 |
7.09e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAflrmlnIKGEIQIDGvswNSMTL-QEWRKAFgVITQKVFIFSGTFRQNL 1300
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLAL------LKNEISADG---GSYTFpGNWQLAW-VNQETPALPQPALEYVI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1301 DPNGKWRD-EEIWKVADQVGLKSVIEQFPGQLN----FTLVDGGYVLSHG----HKQL--------------MCLARSVL 1357
Cdd:PRK10636 86 DGDREYRQlEAQLHDANERNDGHAIATIHGKLDaidaWTIRSRAASLLHGlgfsNEQLerpvsdfsggwrmrLNLAQALI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1358 SKAKIILLDEPSANLDPITYQVIRRVLRqAFAGcTVVLCEHRIEaMLD--CQRFLVIEQGNVWQ----YESLQALLSEKS 1431
Cdd:PRK10636 166 CRSDLLLLDEPTNHLDLDAVIWLEKWLK-SYQG-TLILISHDRD-FLDpiVDKIIHIEQQSLFEytgnYSSFEVQRATRL 242
|
250
....*....|....*.
gi 91982740 1432 VFQRALSSSEKMKLFH 1447
Cdd:PRK10636 243 AQQQAMYESQQERVAH 258
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1208-1384 |
7.55e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAI--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWNSMTLQ-----EWRK 1280
Cdd:PRK11022 6 VDKLSVHFGDESAPFraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAEKLEFNGQDLQrisekERRN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1281 AFGVITQKVFIFSGTfrqNLDP------------------NGKWRDEEIWKVADQVGL---KSVIEQFPGQlnftlvdgg 1339
Cdd:PRK11022 86 LVGAEVAMIFQDPMT---SLNPcytvgfqimeaikvhqggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQ--------- 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 91982740 1340 yvLSHGHKQLMCLARSVLSKAKIILLDEPSANLD-PITYQVIRRVL 1384
Cdd:PRK11022 154 --LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLL 197
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
405-700 |
7.55e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 7.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 405 FQELLEKVQLNNDD--------RKTSNGENHLSfshlclvgnpvLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELE 476
Cdd:PRK13545 7 FEHVTKKYKMYNKPfdklkdlfFRSKDGEYHYA-----------LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 477 ASEGIIKHSGR---VSFSSQISWIMPGTikENI-----IFGVSYDEyrYKSVVKACQLQEDITKFAEQDNTvlgeggvTL 548
Cdd:PRK13545 76 PNKGTVDIKGSaalIAISSGLNGQLTGI--ENIelkglMMGLTKEK--IKEIIPEIIEFADIGKFIYQPVK-------TY 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDvlteeQIF-ESCVCKL----MASKTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:PRK13545 145 SSGMKSRLGFAISVHINPDILVIDEALSVGD-----QTFtKKCLDKMnefkEQGKTIFFISHSLSQVKSfCTKALWLHYG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 623 SSYFYGTFSELQSLRPDFsskLMGYdtfDQFTEERRSSILTETLRRFS----VDDASTTWNKAKQSFRQTGEFgeKRKNS 698
Cdd:PRK13545 220 QVKEYGDIKEVVDHYDEF---LKKY---NQMSVEERKDFREEQISQFQhgllQEDQTGRERKRKKGKKTSRKF--KKKRV 291
|
..
gi 91982740 699 IL 700
Cdd:PRK13545 292 LI 293
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
428-575 |
8.08e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.46 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHlclvGN-PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSQISWIMPGTIKENI 506
Cdd:PRK11831 13 VSFTR----GNrCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IF--GVSY-DEYRYKSVvkACQLQEDiTKFAEQ--DNTVL------GEGGVT------LSGGQRARISLARAVYKDADLY 569
Cdd:PRK11831 89 LFqsGALFtDMNVFDNV--AYPLREH-TQLPAPllHSTVMmkleavGLRGAAklmpseLSGGMARRAALARAIALEPDLI 165
|
....*.
gi 91982740 570 LLDSPF 575
Cdd:PRK11831 166 MFDEPF 171
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1222-1373 |
8.80e-07 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 51.74 E-value: 8.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSaFLRMLN--IKGEIQIDGVSWNSMTLQ---EWR-KAFGVITQkvFifsgt 1295
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDtpTSGDVIFNGQPMSKLSSAakaELRnQKLGFIYQ--F----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1296 frQNLDPN-------------GKWRDEEIWKVADQ----VGLKSVIEQFPGQlnftlvdggyvLSHGHKQLMCLARSVLS 1358
Cdd:PRK11629 96 --HHLLPDftalenvamplliGKKKPAEINSRALEmlaaVGLEHRANHRPSE-----------LSGGERQRVAIARALVN 162
|
170
....*....|....*
gi 91982740 1359 KAKIILLDEPSANLD 1373
Cdd:PRK11629 163 NPRLVLADEPTGNLD 177
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
410-622 |
9.07e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 53.49 E-value: 9.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 410 EKVQLNNDDRKTSNGENHLSFSHLCLV---GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG 486
Cdd:COG3845 240 REVLLRVEKAPAEPGEVVLEVENLSVRddrGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 487 R--------------VSFssqIS-------WIMPGTIKENIIFGvsydEYRYKSVVKACQLQED-ITKFAEQdntVLGEG 544
Cdd:COG3845 320 EditglsprerrrlgVAY---IPedrlgrgLVPDMSVAENLILG----RYRRPPFSRGGFLDRKaIRAFAEE---LIEEF 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 545 GV----------TLSGG--QRArIsLARAVYKDADLYLLDSP-FGyLDVLTEEQIFEscvcKLMASKTR----ILVTSKM 607
Cdd:COG3845 390 DVrtpgpdtparSLSGGnqQKV-I-LARELSRDPKLLIAAQPtRG-LDVGAIEFIHQ----RLLELRDAgaavLLISEDL 462
|
250
....*....|....*.
gi 91982740 608 -EQLKKADKILILHEG 622
Cdd:COG3845 463 dEILALSDRIAVMYEG 478
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1218-1415 |
9.67e-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: 53.29 E-value: 9.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1218 DGNAILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLNIKGEIQIDGVSWNSMTLQEW-RKAFGVITQKVF--- 1290
Cdd:TIGR02633 12 GGVKALDGIDLEVRPGECVGLCGENGAGKSTLmkiLSGVYPHGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTlvp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 -------IFSGtfRQNLDPNGKWRDEEIWKVADQVgLKSVieQFPGqLNFTLVDGGYVLshGHKQLMCLARSVLSKAKII 1363
Cdd:TIGR02633 92 elsvaenIFLG--NEITLPGGRMAYNAMYLRAKNL-LREL--QLDA-DNVTRPVGDYGG--GQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1364 LLDEPSANLDPITYQVIRRVLRQAFA-GCTVVLCEHRI-EAMLDCQRFLVIEQG 1415
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLnEVKAVCDTICVIRDG 217
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1222-1270 |
1.12e-06 |
|
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: 51.38 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLlsafLRML-NI----KGEIQIDG-VSW 1270
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTL----LRLLaGIyppdSGTVTVRGrVSS 87
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
439-572 |
1.15e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.11 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGiikhSGRVSFsSQISWIMPGTIKENIifGVSYDEYRYK 518
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPV----AGCVDV-PDNQFGREASLIDAI--GRKGDFKDAV 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 519 SVVKACQLQEDIT---KFAEqdntvlgeggvtLSGGQRARISLARAVYKDADLYLLD 572
Cdd:COG2401 117 ELLNAVGLSDAVLwlrRFKE------------LSTGQKFRFRLALLLAERPKLLVID 161
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1208-1418 |
1.32e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 53.48 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1208 VKDLTVKYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEIQIDGVSWNSmTLQEWRKAFGVIT 1286
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPpTSGTVLVGGKDIET-NLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSG-TFRQNL----DPNGKWRDEEiwkvadQVGLKSVIEQfpGQLNFTLVDGGYVLSHGHKQLMCLARSVLSKAK 1361
Cdd:TIGR01257 1010 QHNILFHHlTVAEHIlfyaQLKGRSWEEA------QLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1362 IILLDEPSANLDPITYQVIRRVLRQAFAGCTVVLCEHRI-EAMLDCQRFLVIEQGNVW 1418
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMdEADLLGDRIAIISQGRLY 1139
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1223-1372 |
1.32e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.62 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLNIKGEIQIDGVSWNSMTLQEW-RKAFGVITQKVF-------- 1290
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLmkvLSGVYPHGTYEGEIIFEGEELQASNIRDTeRAGIAIIHQELAlvkelsvl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1291 --IFSGtfrQNLDPNGKWRDEEIWKVAD----QVGLKSVIEQFPGQLnftlvdGGyvlshGHKQLMCLARSVLSKAKIIL 1364
Cdd:PRK13549 101 enIFLG---NEITPGGIMDYDAMYLRAQkllaQLKLDINPATPVGNL------GL-----GQQQLVEIAKALNKQARLLI 166
|
....*...
gi 91982740 1365 LDEPSANL 1372
Cdd:PRK13549 167 LDEPTASL 174
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1223-1384 |
1.45e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIK-GEIQIDGVSWNSMT---LQEWRKAFGvitqkvFIFSGTFrQ 1298
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIIFNGQRIDTLSpgkLQALRRDIQ------FIFQDPY-A 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1299 NLDP------------------NGKWRDEEIWKVADQVGLKSVIE-QFPgqlnftlvdggYVLSHGHKQLMCLARSVLSK 1359
Cdd:PRK10261 413 SLDPrqtvgdsimeplrvhgllPGKAAAARVAWLLERVGLLPEHAwRYP-----------HEFSGGQRQRICIARALALN 481
|
170 180
....*....|....*....|....*.
gi 91982740 1360 AKIILLDEPSANLD-PITYQVIRRVL 1384
Cdd:PRK10261 482 PKVIIADEAVSALDvSIRGQIINLLL 507
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
437-574 |
1.75e-06 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 52.33 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKtSLLMLIL-GELEASEGIIKHSGR-VSFSS-------QISWI------MPG- 500
Cdd:COG1129 16 GVKALDGVSLELRPGEVHALLGENGAGK-STLMKILsGVYQPDSGEILLDGEpVRFRSprdaqaaGIAIIhqelnlVPNl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 TIKENIIFGvsyDEYRYKSVVKACQLQEDITKFAEQ-----D-NTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSP 574
Cdd:COG1129 95 SVAENIFLG---REPRRGGLIDWRAMRRRARELLARlgldiDpDTPVGD----LSVAQQQLVEIARALSRDARVLILDEP 167
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1207-1421 |
1.75e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYVDdgNAILENISFSISPGQRVGLLGRTGSGKSTLLSA---------------FLR-------MLNIKGEIq 1264
Cdd:PRK10938 262 VLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndltlFGRrrgsgetIWDIKKHI- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1265 idGVSWNSMTLqEWRKAFGVITqkvFIFSGTFrqnlDPNGKWR--DEEIWKVADQ----VGLKSVIEQFPGQlnftlvdg 1338
Cdd:PRK10938 339 --GYVSSSLHL-DYRVSTSVRN---VILSGFF----DSIGIYQavSDRQQKLAQQwldiLGIDKRTADAPFH-------- 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1339 gyVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFA-GCTVVL-CEHRIEAMLDC--QRFLVIEQ 1414
Cdd:PRK10938 401 --SLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQLLfVSHHAEDAPACitHRLEFVPD 478
|
....*..
gi 91982740 1415 GNVWQYE 1421
Cdd:PRK10938 479 GDIYRYV 485
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
450-600 |
1.91e-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: 48.91 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 450 KGEMLAITGSTGAGKTSLLMLILGELEASEGIIKhsgrvsfssqisWIMPGTIKENIIFgvsydeyryksvvkacqlqed 529
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI------------YIDGEDILEEVLD--------------------- 47
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 530 itkfaEQDNTVLGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTR 600
Cdd:smart00382 48 -----QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS 113
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
440-628 |
1.99e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 52.80 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEAS---------------EGIIKH-SGRVSFSSQISWIMPG-TI 502
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFhigvegvitydgitpEEIKKHyRGDVVYNAETDVHFPHlTV 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIF------------GVSYDEYRYKSV-VKACQLQEDITKfaeqdNTVLGEGGVT-LSGGQRARISLARAVYKDADL 568
Cdd:TIGR00956 156 GETLDFaarcktpqnrpdGVSREEYAKHIAdVYMATYGLSHTR-----NTKVGNDFVRgVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 569 YLLDSPFGYLDVLTEEQiFESCVcKLMAS--KTRILVT---SKMEQLKKADKILILHEGSSYFYG 628
Cdd:TIGR00956 231 QCWDNATRGLDSATALE-FIRAL-KTSANilDTTPLVAiyqCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
437-579 |
2.02e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 51.77 E-value: 2.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 437 GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGeLEA-SEGIIKHSGRVsfssqISWIMPG--------------- 500
Cdd:PRK11650 16 KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAG-LERiTSGEIWIGGRV-----VNELEPAdrdiamvfqnyalyp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 501 --TIKENI-----IFGVSYDEYRyKSVVKACQLQEdITKFAE----QdntvlgeggvtLSGGQRARISLARAVYKDADLY 569
Cdd:PRK11650 90 hmSVRENMayglkIRGMPKAEIE-ERVAEAARILE-LEPLLDrkprE-----------LSGGQRQRVAMGRAIVREPAVF 156
|
170
....*....|
gi 91982740 570 LLDSPFGYLD 579
Cdd:PRK11650 157 LFDEPLSNLD 166
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
441-633 |
2.08e-06 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 51.63 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSG------RVSFSSQIS----------WIMP----- 499
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkrRKEFARRIGvvfgqrsqlwWDLPaidsf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 500 GTIKEniIFGVSYDEY--RYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSP-FG 576
Cdd:COG4586 118 RLLKA--IYRIPDAEYkkRLDELVELLDLGELLDTPVRQ-----------LSLGQRMRCELAAALLHRPKILFLDEPtIG 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 91982740 577 yLDVLTEEQI--FESCVCKlmASKTRILVTSK-M---EQLkkADKILILHEGSSYFYGTFSEL 633
Cdd:COG4586 185 -LDVVSKEAIreFLKEYNR--ERGTTILLTSHdMddiEAL--CDRVIVIDHGRIIYDGSLEEL 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1223-1415 |
2.48e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.95 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsaflrMlNI--------KGEIQIDG--VSWNS----------MTLQEwrkaF 1282
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTL------M-KIlyglyqpdSGEILIDGkpVRIRSprdaialgigMVHQH----F 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1283 GVItqKVFifsgTFRQNL-----DPNGKWRD-----EEIWKVADQVGLK----SVIEQfpgqlnftlvdggyvLSHGHKQ 1348
Cdd:COG3845 90 MLV--PNL----TVAENIvlglePTKGGRLDrkaarARIRELSERYGLDvdpdAKVED---------------LSVGEQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1349 ----LMCLARsvlsKAKIILLDEPSANLDP----ITYQVIRRvLRQafAGCTVVLCEHRI-EAMLDCQRFLVIEQG 1415
Cdd:COG3845 149 rveiLKALYR----GARILILDEPTAVLTPqeadELFEILRR-LAA--EGKSIIFITHKLrEVMAIADRVTVLRRG 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1222-1403 |
3.84e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 50.67 E-value: 3.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNIKGEIQIDGVSWN-----SMTLQEWRKafgVITQKV-FIFsgt 1295
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADRFRWNgidllKLSPRERRK---IIGREIaMIF--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1296 frQN----LDPNGK-----------------------WRDEEIWKVADQVGLKS---VIEQFPgqlnftlvdggYVLSHG 1345
Cdd:COG4170 96 --QEpsscLDPSAKigdqlieaipswtfkgkwwqrfkWRKKRAIELLHRVGIKDhkdIMNSYP-----------HELTEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1346 HKQLMCLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQ--AFAGCTVVLCEHRIEAM 1403
Cdd:COG4170 163 ECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlnQLQGTSILLISHDLESI 222
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1218-1419 |
3.94e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.80 E-value: 3.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1218 DGNAILENISFSISPGQRVGLLGRTGSGKSTLLsaflRML----NI-KGEIQIDGVSWNS---------MTLQEW----- 1278
Cdd:PRK11000 14 GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLL----RMIagleDItSGDLFIGEKRMNDvppaergvgMVFQSYalyph 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1279 -----RKAFGVITQKVfifsgtfrqnldpNGKWRDEEIWKVADQVGLKSVIEQFPGQLnftlvdggyvlSHGHKQLMCLA 1353
Cdd:PRK11000 90 lsvaeNMSFGLKLAGA-------------KKEEINQRVNQVAEVLQLAHLLDRKPKAL-----------SGGQRQRVAIG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 1354 RSVLSKAKIILLDEPSANLDP-ITYQV---IRRVLRQafAGCTVVLCEH-RIEAMLDCQRFLVIEQGNVWQ 1419
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAaLRVQMrieISRLHKR--LGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQ 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
441-639 |
4.75e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.07 E-value: 4.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-VSFSSQISWIMPG--------------TIKEN 505
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQeMRFASTTAALAAGvaiiyqelhlvpemTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 IIFG--------VSYDEYRYKSVVKACQLQEDITKfaeqdNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK11288 100 LYLGqlphkggiVNRRLLNYEAREQLEHLGVDIDP-----DTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 578 LDVLTEEQIFeSCVCKLMASKTRIL-VTSKMEQL-KKADKILILHEGSsyFYGTFSELQSLRPD 639
Cdd:PRK11288 171 LSAREIEQLF-RVIRELRAEGRVILyVSHRMEEIfALCDAITVFKDGR--YVATFDDMAQVDRD 231
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1222-1401 |
5.01e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 5.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-MLNIKGEIQIDgVSWNsmtlQEWRKAFGVitqkvfifsgtfrQNL 1300
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGaLKGTPVAGCVD-VPDN----QFGREASLI-------------DAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1301 DPNGKWRDEEiwKVADQVGLKSVieqfpgQLNFTLVDggyVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITYQVI 1380
Cdd:COG2401 107 GRKGDFKDAV--ELLNAVGLSDA------VLWLRRFK---ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRV 175
|
170 180
....*....|....*....|...
gi 91982740 1381 RRVLRQAF--AGCTVVLCEHRIE 1401
Cdd:COG2401 176 ARNLQKLArrAGITLVVATHHYD 198
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1159-1415 |
5.49e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1159 FKFIDIqteesiCTKIMKELHSEDSPNALVIKNEHVKKCDTWPSGGEmvvkdltvkyvddgNAILENISFSISPGQRVGL 1238
Cdd:PLN03211 40 LKFMDV------CYRVKFENMKNKGSNIKRILGHKPKISDETRQIQE--------------RTILNGVTGMASPGEILAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1239 LGRTGSGKSTLLSAF---LRMLNIKGEIQIDGVSWNSMTLqewrKAFGVITQKVFIFSG-TFRQNLD-------PNGKWR 1307
Cdd:PLN03211 100 LGPSGSGKSTLLNALagrIQGNNFTGTILANNRKPTKQIL----KRTGFVTQDDILYPHlTVRETLVfcsllrlPKSLTK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1308 DEEIwKVADqvglkSVIEQFP-GQLNFTLVDGGYV--LSHGHKQLMCLARSVLSKAKIILLDEPSANLDPIT-YQVIRRV 1383
Cdd:PLN03211 176 QEKI-LVAE-----SVISELGlTKCENTIIGNSFIrgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAaYRLVLTL 249
|
250 260 270
....*....|....*....|....*....|....*.
gi 91982740 1384 LRQAFAGCTVVLCEH----RIEAMLDcqRFLVIEQG 1415
Cdd:PLN03211 250 GSLAQKGKTIVTSMHqpssRVYQMFD--SVLVLSEG 283
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
428-647 |
7.11e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.44 E-value: 7.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 428 LSFSHLCLV--GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEAS--EGIIKHSGRVSFSSQ---------- 493
Cdd:PRK13547 2 LTADHLHVArrHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaPRGARVTGDVTLNGEplaaidaprl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 494 --ISWIMPGTIKENiiFGVSYDEY----RYKSVVKACQLQEDITKFAEQ------DNTVLGEGGVTLSGGQRARISLARA 561
Cdd:PRK13547 82 arLRAVLPQAAQPA--FAFSAREIvllgRYPHARRAGALTHRDGEIAWQalalagATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 562 VYK---------DADLYLLDSPFGYLDVLTEEQIFEScvCKLMASKTRILVTSKMEQL----KKADKILILHEGSSYFYG 628
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDT--VRRLARDWNLGVLAIVHDPnlaaRHADRIAMLADGAIVAHG 237
|
250
....*....|....*....
gi 91982740 629 TFSELqsLRPDFSSKLMGY 647
Cdd:PRK13547 238 APADV--LTPAHIARCYGF 254
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1169-1437 |
9.23e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.17 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1169 SICTKIMKELHSEDSPNALV---IKNEHV-KKCDTWPSGGEMV--VKDLTVKyvDDGNAilENISFSISPGQRVGLLGRT 1242
Cdd:PRK09700 223 SVCSGMVSDVSNDDIVRLMVgreLQNRFNaMKENVSNLAHETVfeVRNVTSR--DRKKV--RDISFSVCRGEILGFAGLV 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1243 GSGKSTLLSAFLRMLNIK-GEIQIDGVSWN-SMTLQEWRKAFGVITQKV----FIFSGTFRQNLD-----PNGKW----- 1306
Cdd:PRK09700 299 GSGRTELMNCLFGVDKRAgGEIRLNGKDISpRSPLDAVKKGMAYITESRrdngFFPNFSIAQNMAisrslKDGGYkgamg 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1307 ----RDEEiwKVADQ----VGLK-SVIEQfpgqlNFTlvdggyVLSHGHKQLMCLARSVLSKAKIILLDEPSANLDPITY 1377
Cdd:PRK09700 379 lfheVDEQ--RTAENqrelLALKcHSVNQ-----NIT------ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAK 445
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1378 QVIRRVLRQ-AFAGCTVVLCEHRI-EAMLDCQRFLVIEQGNVWQYESLQALLSEKSVFQRAL 1437
Cdd:PRK09700 446 AEIYKVMRQlADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWAL 507
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1207-1373 |
9.65e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKYvdDGNAILENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLniKGEIQIDG--VSW-------------- 1270
Cdd:PRK15064 321 EVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTL----LRTL--VGELEPDSgtVKWsenanigyyaqdha 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1271 ----NSMTLQEWrkafgvITQkvfifsgtfrqnldpngkWRDEeiwKVADQVgLKSVIeqfpGQLNFTLVDGG---YVLS 1343
Cdd:PRK15064 393 ydfeNDLTLFDW------MSQ------------------WRQE---GDDEQA-VRGTL----GRLLFSQDDIKksvKVLS 440
|
170 180 190
....*....|....*....|....*....|
gi 91982740 1344 HGHKQLMCLARSVLSKAKIILLDEPSANLD 1373
Cdd:PRK15064 441 GGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1223-1401 |
1.05e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.91 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLlsafLRMLN-----IKGEIQIDGVswnSMTLQEWRKAFG----VITQKVfifs 1293
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTL----LKILSgnyqpDAGSILIDGQ---EMRFASTTAALAagvaIIYQEL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1294 gtfrqNLDPNgkwrdeeiWKVADQVGLKsvieQFPGQlnFTLVDGGYV-----------------------LSHGHKQLM 1350
Cdd:PRK11288 89 -----HLVPE--------MTVAENLYLG----QLPHK--GGIVNRRLLnyeareqlehlgvdidpdtplkyLSIGQRQMV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1351 CLARSVLSKAKIILLDEPSANLDPITYQVIRRVLRQAFAGCTVVL-CEHRIE 1401
Cdd:PRK11288 150 EIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILyVSHRME 201
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
921-1285 |
1.14e-05 |
|
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: 49.80 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 921 LLALSL-FRGLPLVHTLITASKILHRKMLH---SILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLtIFDFIQLLFIV 996
Cdd:COG4615 57 LLVLLLlSRLASQLLLTRLGQHAVARLRLRlsrRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 997 VGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLR--AFRRQTYFETLFH 1074
Cdd:COG4615 136 LGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKlnRRRRRAFFDEDLQ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1075 ------KALNLHTANWFmyLATLRWFQMridMIFVLFFIVVTFISILTTGEGEGTTGIILTLaMNIMSTLQWAVNSsidT 1148
Cdd:COG4615 216 ptaeryRDLRIRADTIF--ALANNWGNL---LFFALIGLILFLLPALGWADPAVLSGFVLVL-LFLRGPLSQLVGA---L 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1149 DSLMRS-VSrvFKFIDiqteesictKIMKELHSEDSPNALVIKNEHVKKCDTwpsggeMVVKDLTVKY--VDDGNA-ILE 1224
Cdd:COG4615 287 PTLSRAnVA--LRKIE---------ELELALAAAEPAAADAAAPPAPADFQT------LELRGVTYRYpgEDGDEGfTLG 349
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 1225 NISFSISPGQRVGLLGRTGSGKSTllsaFLRMLN-----IKGEIQIDGVSWNSMTLQEWRKAFGVI 1285
Cdd:COG4615 350 PIDLTIRRGELVFIVGGNGSGKST----LAKLLTglyrpESGEILLDGQPVTADNREAYRQLFSAV 411
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
440-622 |
1.30e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGEleaSEG------IIKHSGRVSFSS-----------------QISW 496
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGR---SYGrnisgtVFKDGKEVDVSTvsdaidaglayvtedrkGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 497 IMPGTIKENI----IFGVSY-------------DEYRYKSVVKAcqlqeditkfaeqdNTVLgEGGVTLSGGQRARISLA 559
Cdd:NF040905 352 NLIDDIKRNItlanLGKVSRrgvideneeikvaEEYRKKMNIKT--------------PSVF-QKVGNLSGGNQQKVVLS 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 560 RAVYKDADLYLLDSPFGYLDVLTEEQIFeSCVCKLMAS-KTRILVTSKM-EQLKKADKILILHEG 622
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGIDVGAKYEIY-TIINELAAEgKGVIVISSELpELLGMCDRIYVMNEG 480
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1220-1382 |
1.31e-05 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 48.54 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1220 NAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVswNSMTLQEWRKAFGVItqKVF--IFSGTF 1296
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPdSGSILIDGK--DVTKLPEYKRAKYIG--RVFqdPMMGTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1297 -----RQNL---DPNGKWRdeeiwkvadqvGL-----KSVIEQFPGQLNfTLVDG---------GYvLSHGHKQLMCLAR 1354
Cdd:COG1101 95 psmtiEENLalaYRRGKRR-----------GLrrgltKKRRELFRELLA-TLGLGlenrldtkvGL-LSGGQRQALSLLM 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 91982740 1355 SVLSKAKIILLDEPSANLDP--------ITYQVIRR 1382
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPktaalvleLTEKIVEE 197
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
945-1024 |
1.32e-05 |
|
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: 48.58 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 945 RKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILL 1024
Cdd:cd18551 73 RRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLI 152
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
439-633 |
2.02e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 48.08 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR---------VSFSSQISWIMPGtiKENIIFG 509
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrglLALRQQVATVFQD--PEQQIFY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 510 VSYDEYRYKSVVKACQLQEDITKFAEQDNTVLGEGGV------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTE 583
Cdd:PRK13638 93 TDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFrhqpiqCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 584 EQIFeSCVCKLMASKTRILVTSKMEQL--KKADKILILHEGSSYFYGTFSEL 633
Cdd:PRK13638 173 TQMI-AIIRRIVAQGNHVIISSHDIDLiyEISDAVYVLRQGQILTHGAPGEV 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
432-473 |
2.09e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.71 E-value: 2.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 91982740 432 HLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILG 473
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
406-623 |
2.14e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.01 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 406 QELLEKVQLNNDDRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILG-ELEASEGIIKH 484
Cdd:PRK09700 244 RELQNRFNAMKENVSNLAHETVFEVRNVTSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGvDKRAGGEIRLN 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 485 SGRVSFSSQISWIMPG-----------------TIKENIIFGVSYDEYRYKSVVKACQLQEDiTKFAEQDNTVLG----- 542
Cdd:PRK09700 324 GKDISPRSPLDAVKKGmayitesrrdngffpnfSIAQNMAISRSLKDGGYKGAMGLFHEVDE-QRTAENQRELLAlkchs 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 543 -EGGVT-LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFescvcKLMAS-----KTRILVTSKM-EQLKKAD 614
Cdd:PRK09700 403 vNQNITeLSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIY-----KVMRQladdgKVILMVSSELpEIITVCD 477
|
....*....
gi 91982740 615 KILILHEGS 623
Cdd:PRK09700 478 RIAVFCEGR 486
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1222-1394 |
2.26e-05 |
|
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: 46.85 E-value: 2.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTL---LSAFLRMLNIKGEIQIDGvswnsmtlQEWRKAFGVIT---QKVFIFSG- 1294
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLldvLAGRKTAGVITGEILING--------RPLDKNFQRSTgyvEQQDVHSPn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 -TFRQNLDPNGKWRDeeiwkvadqvglksvieqfpgqlnftlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPSANLD 1373
Cdd:cd03232 94 lTVREALRFSALLRG---------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|..
gi 91982740 1374 PIT-YQVIRRVLRQAFAGCTVV 1394
Cdd:cd03232 141 SQAaYNIVRFLKKLADSGQAIL 162
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1215-1384 |
2.33e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 47.15 E-value: 2.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1215 YVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGvswNSMTLQEWRKAFGVITQkvfifS 1293
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVeSGQIQIDG---KTATRGDRSRFMAYLGH-----L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1294 GTFRQNLDPNgkwrdEEIWKVADQVGLKSviEQFPGQLnFTLVD-GGYV------LSHGHKQLMCLARSVLSKAKIILLD 1366
Cdd:PRK13543 91 PGLKADLSTL-----ENLHFLCGLHGRRA--KQMPGSA-LAIVGlAGYEdtlvrqLSAGQKKRLALARLWLSPAPLWLLD 162
|
170
....*....|....*...
gi 91982740 1367 EPSANLDPITYQVIRRVL 1384
Cdd:PRK13543 163 EPYANLDLEGITLVNRMI 180
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1222-1399 |
2.54e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 2.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLN-IKGEI--------------QIDGVSWNSMTLQEW-RKAFGVI 1285
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELApVSGEIglakgiklgyfaqhQLEFLRADESPLQHLaRLAPQEL 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1286 TQKVFIFSGTFRQNLDpngkwrdeeiwKVADQVglksviEQFPGqlnftlvdggyvlshGHKQLMCLARSVLSKAKIILL 1365
Cdd:PRK10636 407 EQKLRDYLGGFGFQGD-----------KVTEET------RRFSG---------------GEKARLVLALIVWQRPNLLLL 454
|
170 180 190
....*....|....*....|....*....|....*..
gi 91982740 1366 DEPSANLDpityQVIRRVLRQA---FAGCTVVLCEHR 1399
Cdd:PRK10636 455 DEPTNHLD----LDMRQALTEAlidFEGALVVVSHDR 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
441-666 |
2.89e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR--------------VSFSSQ-ISWIMPGTIKEN 505
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInynkldhklaaqlgIGIIYQeLSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 I---------IFGVSYDEYRYKSVVKACQLqeDITKFAEQDNTVLGEggvtLSGGQRARISLARAVYKDADLYLLDSPFG 576
Cdd:PRK09700 101 LyigrhltkkVCGVNIIDWREMRVRAAMML--LRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 577 YLDVLTEEQIFeSCVCKLMASKTRILVTS-KMEQLKK-ADKILILHEGSSYFYGTFSELQSlrPDFSSKLMGYDTFDQFT 654
Cdd:PRK09700 175 SLTNKEVDYLF-LIMNQLRKEGTAIVYIShKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSN--DDIVRLMVGRELQNRFN 251
|
250
....*....|....
gi 91982740 655 --EERRSSILTETL 666
Cdd:PRK09700 252 amKENVSNLAHETV 265
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
858-1078 |
2.97e-05 |
|
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: 47.80 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 858 LIWCVLVFLVEVAASLFVLWLLKnnpvnggnngtkiantsYVV--VITSSSFYYIFYIYVGVadtlLALSLFRGLPL-VH 934
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLK-----------------PLLddIFVEKDLEALLLVPLAI----IGLFLLRGLASyLQ 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 935 TLITAS---KILH---RKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQP 1008
Cdd:cd18552 60 TYLMAYvgqRVVRdlrNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDW 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1009 Y---IFLATVPGLAVFI-LLRAYFLHTSQqlKQLESEGRspIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALN 1078
Cdd:cd18552 140 KltlIALVVLPLAALPIrRIGKRLRKISR--RSQESMGD--LTSVLQETLSGIRVVKAFGAEDYEIKRFRKANE 209
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1206-1417 |
3.46e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.23 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1206 MVVKDLTvKYVDDGNAiLENISFSISPGQRVGLLGRTGSGKSTLLSAF-LRMLNIKGEIQI---DGVSWNSMTLQE---- 1277
Cdd:PRK11701 7 LSVRGLT-KLYGPRKG-CRDVSFDLYPGEVLGIVGESGSGKTTLLNALsARLAPDAGEVHYrmrDGQLRDLYALSEaerr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1278 --WRKAFGVITQKVfifsgtfRQNLDPN-------------------GKWRDEEI-WkvADQVGL-KSVIEQFPGQlnft 1334
Cdd:PRK11701 85 rlLRTEWGFVHQHP-------RDGLRMQvsaggnigerlmavgarhyGDIRATAGdW--LERVEIdAARIDDLPTT---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1335 lvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPSANLDpITYQ-----VIRRVLRQafAGCTVVLCEHRIE-AMLDCQR 1408
Cdd:PRK11701 152 -------FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQarlldLLRGLVRE--LGLAVVIVTHDLAvARLLAHR 221
|
....*....
gi 91982740 1409 FLVIEQGNV 1417
Cdd:PRK11701 222 LLVMKQGRV 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
425-590 |
3.65e-05 |
|
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: 48.21 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 425 ENHLSFSHLCLV---GNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMlILGELEASEG---IIKHSGRVSFSSQISWIM 498
Cdd:TIGR00954 449 DNGIKFENIPLVtpnGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGgrlTKPAKGKLFYVPQRPYMT 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 499 PGTIKENIIFGVSYDEYRYKSVVKacQLQEDITKFAEQDNTVLGEGGVT--------LSGGQRARISLARAVYKDADLYL 570
Cdd:TIGR00954 528 LGTLRDQIIYPDSSEDMKRRGLSD--KDLEQILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAI 605
|
170 180
....*....|....*....|
gi 91982740 571 LDSPFGYLDVLTEEQIFESC 590
Cdd:TIGR00954 606 LDECTSAVSVDVEGYMYRLC 625
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
441-622 |
3.96e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.19 E-value: 3.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR-VSFSS--------------QISWIMPGTIKEN 505
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeIDFKSskealengismvhqELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 506 IIFGvsydeyRYKS----VVKACQLQEDITKFAEQDNTV-LGEGGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK10982 94 MWLG------RYPTkgmfVDQDKMYRDTKAIFDELDIDIdPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 91982740 581 LTEEQIFeSCVCKLMASKTRILVTS-KMEQLKK-ADKILILHEG 622
Cdd:PRK10982 168 KEVNHLF-TIIRKLKERGCGIVYIShKMEEIFQlCDEITILRDG 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
433-622 |
4.32e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 47.01 E-value: 4.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 433 LCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMlILGELEASEGIIKHSGRV--------------SFSSQISWIM 498
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLR-TLNRMNDKVSGYRYSGDVllggrsifnyrdvlEFRRRVGMLF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 499 ------PGTIKENIIFGVSYDEY----RYKSVVKAcQLQEDITKFAEQDNtvLGEGGVTLSGGQRARISLARAVYKDADL 568
Cdd:PRK14271 108 qrpnpfPMSIMDNVLAGVRAHKLvprkEFRGVAQA-RLTEVGLWDAVKDR--LSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 569 YLLDSPFGYLDVLTEEQIfESCVCKLMASKTRILVTSKMEQLKK-ADKILILHEG 622
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKI-EEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDG 238
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
440-629 |
4.94e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 47.15 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGII-----KHSGRVSFSSQISWIMPGTIKE--------NI 506
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiYIGDKKNNHELITNPYSKKIKNfkelrrrvSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IFgvSYDEYR-YKSVVKA---------CQLQEDITKFAEQ-------DNTVLGEGGVTLSGGQRARISLARAVYKDADLY 569
Cdd:PRK13631 121 VF--QFPEYQlFKDTIEKdimfgpvalGVKKSEAKKLAKFylnkmglDDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 91982740 570 LLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKMEQ-LKKADKILILHEGSSYFYGT 629
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHvLEVADEVIVMDKGKILKTGT 259
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
547-657 |
6.23e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 6.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 547 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDvLTEEQIFESCVCKLmaSKTRILVTSKMEQLKK-ADKILILHEgssy 625
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLD-LHAVLWLETYLLKW--PKTFIVVSHAREFLNTvVTDILHLHG---- 416
|
90 100 110
....*....|....*....|....*....|..
gi 91982740 626 fygtfSELQSLRPDfssklmgYDTFDQFTEER 657
Cdd:PLN03073 417 -----QKLVTYKGD-------YDTFERTREEQ 436
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1214-1250 |
9.47e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 9.47e-05
10 20 30
....*....|....*....|....*....|....*..
gi 91982740 1214 KYVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLL 1250
Cdd:PRK11819 14 KVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLL 50
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1202-1401 |
1.01e-04 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.73 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1202 SGGEMVVKDLTVKYVDdgNAILENISFSISPGQRVGLLGRTGSGKSTllsaFLRMLNI-----KGEIQIDGVS------- 1269
Cdd:PRK10619 2 SENKLNVIDLHKRYGE--HEVLKGVSLQANAGDVISIIGSSGSGKST----FLRCINFlekpsEGSIVVNGQTinlvrdk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1270 ------WNSMTLQEWRKAFGVITQKVFIFSG-TFRQN--------LDPNGKWRDEEIWKVADQVGL-KSVIEQFPGQLnf 1333
Cdd:PRK10619 76 dgqlkvADKNQLRLLRTRLTMVFQHFNLWSHmTVLENvmeapiqvLGLSKQEARERAVKYLAKVGIdERAQGKYPVHL-- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1334 tlvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPSANLDP-ITYQVIRRVLRQAFAGCTVVLCEHRIE 1401
Cdd:PRK10619 154 ---------SGGQQQRVSIARALAMEPEVLLFDEPTSALDPeLVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
429-574 |
1.40e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 46.20 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 429 SFShlclvGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFS--------------SQI 494
Cdd:PRK15439 20 QYS-----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltpakahqlgiylvPQE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 495 SWIMPG-TIKENIIFGVSYDEYRYKSVVK-----ACQLQEDITkfaeqdntvlgegGVTLSGGQRARISLARAVYKDADL 568
Cdd:PRK15439 95 PLLFPNlSVKENILFGLPKRQASMQKMKQllaalGCQLDLDSS-------------AGSLEVADRQIVEILRGLMRDSRI 161
|
....*.
gi 91982740 569 YLLDSP 574
Cdd:PRK15439 162 LILDEP 167
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1221-1375 |
1.76e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 45.08 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1221 AILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML-----NIKGEIQIDGVSWN---------SMTLQEWRKAFgvit 1286
Cdd:PRK10418 17 PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpagvrQTAGRVLLDGKPVApcalrgrkiATIMQNPRSAF---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1287 QKVFIFSGTFRQNLDPNGKWRDEE-IWKVADQVGL---KSVIEQFPGQLnftlvdggyvlSHGHKQLMCLARSVLSKAKI 1362
Cdd:PRK10418 93 NPLHTMHTHARETCLALGKPADDAtLTAALEAVGLenaARVLKLYPFEM-----------SGGMLQRMMIALALLCEAPF 161
|
170
....*....|...
gi 91982740 1363 ILLDEPSANLDPI 1375
Cdd:PRK10418 162 IIADEPTTDLDVV 174
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
904-1078 |
1.80e-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: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 904 SSSFYYIFYIYVGVAdtllALSLFRGLPLVhtlITASKI---LHRKMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDD 980
Cdd:cd18557 36 NELALILLAIYLLQS----VFTFVRYYLFN---IAGERIvarLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 981 FLPLTIFDFIQLLFIVVGAIIVVSALQP---YIFLATVPGLAVFILLRAYFLhtsQQLKQLESEGRSPIFTHLVTSLKGL 1057
Cdd:cd18557 109 AVTDNLSQLLRNILQVIGGLIILFILSWkltLVLLLVIPLLLIASKIYGRYI---RKLSKEVQDALAKAGQVAEESLSNI 185
|
170 180
....*....|....*....|.
gi 91982740 1058 WTLRAFRRQTYFETLFHKALN 1078
Cdd:cd18557 186 RTVRSFSAEEKEIRRYSEALD 206
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
418-622 |
2.18e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.49 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 418 DRKTSNGENHLSFSHLCLVGNPVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIK-HSGRVSFSSQISW 496
Cdd:PRK10982 241 DKENKPGEVILEVRNLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITlHGKKINNHNANEA 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 497 IMPGtikeniiFGVSYDEYR-----------YKSVVKacQLQEDITKFAEQDNT--------VLGEGGV----------T 547
Cdd:PRK10982 321 INHG-------FALVTEERRstgiyayldigFNSLIS--NIRNYKNKVGLLDNSrmksdtqwVIDSMRVktpghrtqigS 391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 91982740 548 LSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQIFESCVCKLMASKTRILVTSKM-EQLKKADKILILHEG 622
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNG 467
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1223-1374 |
2.60e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 2.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRML------NIKGEIQIDGVSWNSMTLQEWRKAFGVITQ--KVFIFSG 1294
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIisetgqTIVGDYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 TFRQNLDPN----GKWRDEEIWKVADQVGLKSVIEQFPGQLNFTLvdggyvlSHGHKQLMCLARSVLSKAKIILLDEPSA 1370
Cdd:PRK13645 107 TIEKDIAFGpvnlGENKQEAYKKVPELLKLVQLPEDYVKRSPFEL-------SGGQKRRVALAGIIAMDGNTLVLDEPTG 179
|
....
gi 91982740 1371 NLDP 1374
Cdd:PRK13645 180 GLDP 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
424-580 |
2.69e-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: 45.55 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 424 GENhlSFShlcLVGNPVLKninlnikKGEMLAITGSTGAGKTSLLMLILGEL---------EAS-EGIIKH-SG------ 486
Cdd:COG1245 84 GEN--GFR---LYGLPVPK-------KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSwDEVLKRfRGtelqdy 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 487 ---------RVSFSSQ----ISWIMPGTIKENIifgVSYDEY-RYKSVVKacQLqeDITKFAEQDNTvlgeggvTLSGGQ 552
Cdd:COG1245 152 fkklangeiKVAHKPQyvdlIPKVFKGTVRELL---EKVDERgKLDELAE--KL--GLENILDRDIS-------ELSGGE 217
|
170 180
....*....|....*....|....*...
gi 91982740 553 RARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:COG1245 218 LQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
441-622 |
2.81e-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: 45.20 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKtSLLMLIL----------GELEASEGIIKHS--------GRVSFSSQISWIMPGTI 502
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGK-STLMKILsgvyphgtwdGEIYWSGSPLKASnirdteraGIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 503 KENIIFG--VSYDEYR--YKSVVKACQ-LQEDITKFAEQDNTVLGEGGvtlsGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:TIGR02633 96 AENIFLGneITLPGGRmaYNAMYLRAKnLLRELQLDADNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 91982740 578 LdVLTEEQIFESCVCKLMASKTR-ILVTSKMEQLKK-ADKILILHEG 622
Cdd:TIGR02633 172 L-TEKETEILLDIIRDLKAHGVAcVYISHKLNEVKAvCDTICVIRDG 217
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
440-471 |
2.87e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 44.68 E-value: 2.87e-04
10 20 30
....*....|....*....|....*....|..
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLI 471
Cdd:COG1135 20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCI 51
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1222-1417 |
3.19e-04 |
|
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: 43.41 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFlrMLNIKGEIQIDG-VSWNSMTLQEwrkaFGVITQKVFIFSG------ 1294
Cdd:cd03233 22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKAL--ANRTEGNVSVEGdIHYNGIPYKE----FAEKYPGEIIYVSeedvhf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1295 ---TFRQNLDPNGKWRDEEIwkvadqvglksvieqfpgqlnftlVDGgyvLSHGHKQLMCLARSVLSKAKIILLDEPSAN 1371
Cdd:cd03233 96 ptlTVRETLDFALRCKGNEF------------------------VRG---ISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 1372 LDPIT----YQVIRRVLRQAFAGCTVVL--CEHRIEAMLDcqRFLVIEQGNV 1417
Cdd:cd03233 149 LDSSTaleiLKCIRTMADVLKTTTFVSLyqASDEIYDLFD--KVLVLYEGRQ 198
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
86-302 |
3.35e-04 |
|
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: 44.46 E-value: 3.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 86 VLLYLGEVTKAVQPVLLGRIIASYDPDntEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTL 165
Cdd:cd07346 6 LLLLLATALGLALPLLTKLLIDDVIPA--GDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 166 KLSSRVLDKISIGQLISLLSNNLNKFDEGL-ALAHFIWIAPLQVVLLMGLLWDLLQFSAFCGLGLLIVLVIFQAILGKMM 244
Cdd:cd07346 84 RLSLSFFDRNRTGDLMSRLTSDVDAVQNLVsSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 245 VK-YRD--KRAAKINERLVitsEVIDNIYSVKAYCWE----SAMEKIIESLREEELKMTRRSAYM 302
Cdd:cd07346 164 RKaSREvrESLAELSAFLQ---ESLSGIRVVKAFAAEereiERFREANRDLRDANLRAARLSALF 225
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
945-1112 |
3.88e-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: 44.01 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 945 RKMLHSILHA-PMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQP---YIFLATVPglaV 1020
Cdd:cd18576 72 RKDLYRHLQRlPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWkltLLMLATVP---V 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1021 FILLRAYF------LHTSQQLKQLESegrspiFTHLVTSLKGLWTLRAFRRQTYFETLFHKALN--LHTAnwfMYLATLR 1092
Cdd:cd18576 149 VVLVAVLFgrrirkLSKKVQDELAEA------NTIVEETLQGIRVVKAFTREDYEIERYRKALErvVKLA---LKRARIR 219
|
170 180
....*....|....*....|
gi 91982740 1093 WFQMRIdMIFVLFFIVVTFI 1112
Cdd:cd18576 220 ALFSSF-IIFLLFGAIVAVL 238
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
858-1115 |
3.99e-04 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 44.30 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 858 LIWCVLVFLVEVAASLFVLWLLKnnpvnggnngtkIANTSYVVVITS--SSFYYIFYIYVGVadtLLALSLFRGLPLVHT 935
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIK------------RAIDDYIVPGQGdlQGLLLLALLYLGL---LLLSFLLQYLQTYLL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 936 LITASKILH--RKMLHS-ILHAPMSTFNKLKAGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAIIVVSALQPY--- 1009
Cdd:cd18544 66 QKLGQRIIYdlRRDLFShIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRlal 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1010 IFLATVPglaVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFRRQTYFETLFHKALNLHtanwfmYLA 1089
Cdd:cd18544 146 ISLLVLP---LLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEY------RKA 216
|
250 260
....*....|....*....|....*.
gi 91982740 1090 tlrwfQMRIDMIFVLFFIVVTFISIL 1115
Cdd:cd18544 217 -----NLKSIKLFALFRPLVELLSSL 237
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1222-1373 |
4.87e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1222 ILENISFSISPGQRVGLLGRTGSGKSTLLSAFLR-MLNIKGEIQI----------------------DGVSWNSMTLQEW 1278
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGeVLLDDGRIIYeqdlivarlqqdpprnvegtvyDFVAEGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1279 RKAFGVITQKVFIFS--------GTFRQNLDPNGKWR-DEEIWKVADQVGLKSvieqfpgqlNFTLVDggyvLSHGHKQL 1349
Cdd:PRK11147 98 LKRYHDISHLVETDPseknlnelAKLQEQLDHHNLWQlENRINEVLAQLGLDP---------DAALSS----LSGGWLRK 164
|
170 180
....*....|....*....|....
gi 91982740 1350 MCLARSVLSKAKIILLDEPSANLD 1373
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLD 188
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1207-1415 |
5.41e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 44.25 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1207 VVKDLTVKyVDDGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRMLNI-KGEIQIDGVSWNSMTLQEWRKA---- 1281
Cdd:COG3845 259 EVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPaSGSIRLDGEDITGLSPRERRRLgvay 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1282 -------FGVITQkvfiFS-------GTFRQNLDPNGKWRDeeiWKVADQVGlKSVIEQF---PGQLNfTLVDGgyvLSH 1344
Cdd:COG3845 338 ipedrlgRGLVPD----MSvaenlilGRYRRPPFSRGGFLD---RKAIRAFA-EELIEEFdvrTPGPD-TPARS---LSG 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 91982740 1345 GHKQLMCLARSVLSKAKIILLDEPSANLDpI--TYQVIRRVLRQAFAGCTVVLcehrIEAMLD-----CQRFLVIEQG 1415
Cdd:COG3845 406 GNQQKVILARELSRDPKLLIAAQPTRGLD-VgaIEFIHQRLLELRDAGAAVLL----ISEDLDeilalSDRIAVMYEG 478
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
441-586 |
5.88e-04 |
|
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: 44.29 E-value: 5.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGeLEASEGIIKHSGR-------------------V------SFS---- 491
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQdldglsrralrplrrrmqvVfqdpfgSLSprmt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 492 -SQIswimpgtIKENIIF---GVSYDEyRYKSVVKAcqLQE------DITKFAEQdntvlgeggvtLSGGQRARISLARA 561
Cdd:COG4172 381 vGQI-------IAEGLRVhgpGLSAAE-RRARVAEA--LEEvgldpaARHRYPHE-----------FSGGQRQRIAIARA 439
|
170 180
....*....|....*....|....*
gi 91982740 562 VYKDADLYLLDSPFGYLDVLTEEQI 586
Cdd:COG4172 440 LILEPKLLVLDEPTSALDVSVQAQI 464
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
440-595 |
5.91e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 5.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEA---SEGIIKHSGR---VSFSSQISW-------IMPGTIKENI 506
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRpldSSFQRSIGYvqqqdlhLPTSTVRESL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 507 IFG--------VS-YDEYRYksVVKACQLQEdITKFAEqdnTVLGEGGVTLSGGQRARISLA-RAVYKDADLYLLDSPFG 576
Cdd:TIGR00956 858 RFSaylrqpksVSkSEKMEY--VEEVIKLLE-MESYAD---AVVGVPGEGLNVEQRKRLTIGvELVAKPKLLLFLDEPTS 931
|
170
....*....|....*....
gi 91982740 577 YLDVLTEEQIfescvCKLM 595
Cdd:TIGR00956 932 GLDSQTAWSI-----CKLM 945
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1201-1395 |
6.52e-04 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 44.24 E-value: 6.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1201 PSGGEMV--VKDLTVKYVddgnaiLENISFSISPGQRVGLLGRTGSGKSTLLSA-FLRMLNIKGEIQIDGVSWNSMTLQ- 1276
Cdd:COG1129 250 AAPGEVVleVEGLSVGGV------VRDVSFSVRAGEILGIAGLVGAGRTELARAlFGADPADSGEIRLDGKPVRIRSPRd 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 1277 ----------EWRKAFGVITQKvfifsgTFRQN-----LDPNGKWR-------DEEIWKVADQVGLK-SVIEQFPGQlnf 1333
Cdd:COG1129 324 airagiayvpEDRKGEGLVLDL------SIRENitlasLDRLSRGGlldrrreRALAEEYIKRLRIKtPSPEQPVGN--- 394
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 1334 tlvdggyvLSHGHKQLMCLARSVLSKAKIILLDEPSANLDP-----ItYQVIRRVLRQafaGCTVVL 1395
Cdd:COG1129 395 --------LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVgakaeI-YRLIRELAAE---GKAVIV 449
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
910-1044 |
6.85e-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: 43.62 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 910 IFYIYVGVA---DTLLALSLFRglplvhtlITASKILHR---KMLHSILHAPMSTFNKLKAGGILNRFSKDIAILDDFLP 983
Cdd:cd18577 51 LYFVYLGIGsfvLSYIQTACWT--------ITGERQARRirkRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIG 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 91982740 984 LTIFDFIQLLFIVVGAIIV---VS---ALqpyIFLATVPGLAVFILLRAYFLHTSQQlKQLESEGRS 1044
Cdd:cd18577 123 EKLGLLIQSLSTFIAGFIIafiYSwklTL---VLLATLPLIAIVGGIMGKLLSKYTK-KEQEAYAKA 185
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
448-625 |
8.92e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 42.26 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 448 IKKGEMLAITGSTGAGKTSLLMLI----LGELEA-----SEGIIKHSG----RVSFSSQISWIMPGTIKEniiFGVSYDE 514
Cdd:cd03279 25 LDNNGLFLICGPTGAGKSTILDAItyalYGKTPRygrqeNLRSVFAPGedtaEVSFTFQLGGKKYRVERS---RGLDYDQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 515 YRyKSVVKAcqlQEDITKFAEQDNTvlgeggvTLSGGQRARISLARAVY----------KDADLYLLDSPFGYLDVLTEE 584
Cdd:cd03279 102 FT-RIVLLP---QGEFDRFLARPVS-------TLSGGETFLASLSLALAlsevlqnrggARLEALFIDEGFGTLDPEALE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 91982740 585 QIFEscVCKLMASKTR-ILVTSKMEQLKKA-DKILILHEGSSY 625
Cdd:cd03279 171 AVAT--ALELIRTENRmVGVISHVEELKERiPQRLEVIKTPGG 211
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
443-487 |
9.89e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.61 E-value: 9.89e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 91982740 443 NINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGR 487
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMR 68
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
440-643 |
1.03e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 42.87 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 440 VLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEG--------IIKHSGR-------VSFSSQISWIMPGTIKE 504
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsvlirgepITKENIRevrkfvgLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 505 NIIFG---VSYDE----YRYKSVVKACQLQEDITKFAEQdntvlgeggvtLSGGQRARISLARAVYKDADLYLLDSPFGY 577
Cdd:PRK13652 99 DIAFGpinLGLDEetvaHRVSSALHMLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 578 LDVLTEEQIFEsCVCKLMAS--KTRILVTSKMEQLKK-ADKILILHEGSSYFYGTFSELqSLRPDFSSK 643
Cdd:PRK13652 168 LDPQGVKELID-FLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI-FLQPDLLAR 234
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
441-640 |
1.08e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.50 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELEASEGIIKHSGRVSFSSqISWIMPGTIK--ENIIFGVSYDEYRYK 518
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIA-ISAGLSGQLTgiENIEFKMLCMGFKRK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 519 SVVKacqLQEDITKFAEqdntvLGE----GGVTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvlteeQIF-ESCVCK 593
Cdd:PRK13546 119 EIKA---MTPKIIEFSE-----LGEfiyqPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGD-----QTFaQKCLDK 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 91982740 594 LM----ASKTRILVTSKMEQLKK-ADKILILHEGssyFYGTFSELQSLRPDF 640
Cdd:PRK13546 186 IYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGG---KLKDYGELDDVLPKY 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
441-471 |
1.16e-03 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.87 E-value: 1.16e-03
10 20 30
....*....|....*....|....*....|.
gi 91982740 441 LKNINLNIKKGEMLAITGSTGAGKTSLLMLI 471
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCI 51
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
547-580 |
1.35e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.26 E-value: 1.35e-03
10 20 30
....*....|....*....|....*....|....
gi 91982740 547 TLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
450-619 |
1.99e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 450 KGEMLAITGSTGAGKTSLL-MLILGELEASEGIIKHSGrvsfssqiswimpgtIKENIIfgVSYDEYRYKSVVkacqlqe 528
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILdAIGLALGGAQSATRRRSG---------------VKAGCI--VAAVSAELIFTR------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 529 ditkfaeqdntvlgeggVTLSGGQRARISLARAV----YKDADLYLLDSPFGYLDvLTEEQIFeSCVCKLMASKTR--IL 602
Cdd:cd03227 76 -----------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLD-PRDGQAL-AEAILEHLVKGAqvIV 136
|
170
....*....|....*..
gi 91982740 603 VTSKMEQLKKADKILIL 619
Cdd:cd03227 137 ITHLPELAELADKLIHI 153
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
901-1078 |
2.61e-03 |
|
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: 41.66 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 901 VITSSSFYYIFYIYVGVADTLLA---LSLFRGLPLVHTLITASKILHRKMLHSILHAPMSTFNKLKAGGILNRFSkDIAI 977
Cdd:cd18570 32 IIPSGDINLLNIISIGLILLYLFqslLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 978 LDDFLPLTIFDFIQLLFIVVGAIIVVSALQPYIFLATVPGLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKGL 1057
Cdd:cd18570 111 IREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGI 190
|
170 180
....*....|....*....|....*
gi 91982740 1058 WTLRAFRRQTYF----ETLFHKALN 1078
Cdd:cd18570 191 ETIKSLNAEEQFlkkiEKKFSKLLK 215
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
455-617 |
3.35e-03 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 40.67 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 455 AITGSTGAGKTSLLMLIL----GELEASEGIIKHS----GRVSFSSQISWIMPGTIKENIIFGVSYDEYRYKSVVKacql 526
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSKGGAHDpkliREGEVRAQVKLAFENANGKKYTITRSLAILENVIFCH---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 527 QEDITKFAEqdntvlgEGGVTLSGGQRA------RISLARAVYKDADLYLLDSPFGYLDvltEEQIFEScVCKLMASKTR 600
Cdd:cd03240 102 QGESNWPLL-------DMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EENIEES-LAEIIEERKS 170
|
170 180
....*....|....*....|...
gi 91982740 601 ------ILVTSKMEQLKKADKIL 617
Cdd:cd03240 171 qknfqlIVITHDEELVDAADHIY 193
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1223-1251 |
3.44e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.03 E-value: 3.44e-03
10 20
....*....|....*....|....*....
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTLLS 1251
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLS 45
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1223-1267 |
3.46e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.80 E-value: 3.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 91982740 1223 LENISFSISPGQRVGLLGRTGSGKSTL--LSAFLRMLNiKGEIQIDG 1267
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLsnLIAGVTMPN-KGTVDIKG 85
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
945-1080 |
3.50e-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: 41.28 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 91982740 945 RKMLHSILHAPMSTFNKLK--AGGILNRFSKDIAILDDFLPLTIFDFIQLLFIVVGAII---VVS---ALqpyIFLATVP 1016
Cdd:cd18578 89 KLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIiafVYGwklAL---VGLATVP 165
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 91982740 1017 GLAVFILLRAYFLHTSQQLKQLESEGRSPIFTHLVTSLKglwTLRAFRRQTYFETLFHKALNLH 1080
Cdd:cd18578 166 LLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIR---TVASLTLEDYFLEKYEEALEEP 226
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1232-1298 |
5.16e-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: 39.28 E-value: 5.16e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 91982740 1232 PGQRVGLLGRTGSGKSTLLSAFLRMLNIKGE--IQIDGVSWNSMTLQEWRKAFGVITQKVFIFSGTFRQ 1298
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGgvIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRL 69
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
549-586 |
6.80e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 40.33 E-value: 6.80e-03
10 20 30
....*....|....*....|....*....|....*...
gi 91982740 549 SGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEEQI 586
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQV 193
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
548-580 |
6.98e-03 |
|
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: 40.04 E-value: 6.98e-03
10 20 30
....*....|....*....|....*....|...
gi 91982740 548 LSGGQRARISLARAVYKDADLYLLDSPFGYLDV 580
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
439-493 |
9.37e-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: 40.44 E-value: 9.37e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 91982740 439 PVLKNINLNIKKGEMLAITGSTGAGKTSLLMLILGELeaSEGIIKHSGRVSFSSQ 493
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLL--PDPAAHPSGSILFDGQ 76
|
|
| |
