|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-533 |
0e+00 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 601.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQIPDYHDSTSTKE 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 86 VLKSAFSPLLQMEEKMEKLEAEMGVETDpnklqkLMGEYGELQDQYANNGGYEIESNIEKIAHGLNIQMFIHS-PFSQLS 164
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDE------DLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDrPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 165 GGEKTKVGLG----------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLED 234
Cdd:COG0488 155 GGWRRRVALArallsepdllLL----------DEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 235 GEVTTYHTNFTGFVKEKEEKLLKEFQAYEEQQKKIKKMKEAIKRLRDWANRATppnadlhrRARNMERALERMEKLNRPI 314
Cdd:COG0488 225 GKLTLYPGNYSAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAK--------QAQSRIKALEKLEREEPPR 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 315 LNRTkMNLEMESTERSGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG 394
Cdd:COG0488 297 RDKT-VEIRFPPPERLGKKVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 395 SNVKIGYLSQNIFSSIKDETVIETFRDVV-NVTEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLI 473
Cdd:COG0488 376 ETVKIGYFDQHQEELDPDKTVLDELRDGApGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 474 LDEPTNHLDIESREVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKIHCFEGNYT 533
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYD 515
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-542 |
2.19e-108 |
|
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: 337.29 E-value: 2.19e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 2 IICSVNKVAKMYGGN-AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQIPDYHDS 80
Cdd:TIGR03719 3 YIYTMNRVSKVVPPKkEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 81 TSTKEVLKSAFSPLLQMEEKMEKLEAEMGVETDpnKLQKLMGEYGELQDQYANNGGYEIESNIEKIAHGLNIQMFiHSPF 160
Cdd:TIGR03719 83 KTVRENVEEGVAEIKDALDRFNEISAKYAEPDA--DFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW-DADV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 161 SQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGEVTTY 240
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 241 HTNFTGFVKEKEekllkefQAYEEQQKKIKKMKEAIKRLRDWAnRATPPNadlhRRARNMERaLERMEKLNRPILNRTKM 320
Cdd:TIGR03719 240 EGNYSSWLEQKQ-------KRLEQEEKEESARQKTLKRELEWV-RQSPKG----RQAKSKAR-LARYEELLSQEFQKRNE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 321 NLEM--ESTERSGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVK 398
Cdd:TIGR03719 307 TAEIyiPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 IGYLSQNIFSSIKDETVIETFRD-----VVNVTEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLI 473
Cdd:TIGR03719 387 LAYVDQSRDALDPNKTVWEEISGgldiiKLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 474 LDEPTNHLDIESREVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAK-KIHCFEGNYTWAKEKMTKR 542
Cdd:TIGR03719 467 LDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGDsHVEWFEGNFSEYEEDKKRR 536
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-543 |
1.55e-101 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 319.76 E-value: 1.55e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 2 IICSVNKVAKMYGGN-AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQIPDYHDS 80
Cdd:PRK11819 5 YIYTMNRVSKVVPPKkQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 81 TSTKEVLKSAFSPLLQMEEKMEKLEAEMGveTDPNKLQKLMGEYGELQDQYANNGGYEIESNIEKIAHGLNIQMFiHSPF 160
Cdd:PRK11819 85 KTVRENVEEGVAEVKAALDRFNEIYAAYA--EPDADFDALAAEQGELQEIIDAADAWDLDSQLEIAMDALRCPPW-DAKV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 161 SQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGEVTTY 240
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPW 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 241 HTNFTGFVKEKEekllkefQAYEEQQKKIKKMKEAIKRLRDWANRAtpPNAdlhRRARNMERaLERMEKLNRPilNRTKM 320
Cdd:PRK11819 242 EGNYSSWLEQKA-------KRLAQEEKQEAARQKALKRELEWVRQS--PKA---RQAKSKAR-LARYEELLSE--EYQKR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 321 NLEME----STERSGNDVIMLKDISKCFGDKLLFEGVNMHITyqnRAAI---IGENGTGKSTLLKLILQQLFPDKGEVRI 393
Cdd:PRK11819 307 NETNEifipPGPRLGDKVIEAENLSKSFGDRLLIDDLSFSLP---PGGIvgiIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 394 GSNVKIGYLSQNiFSSIKDE-TVIETF---RDVVNV--TEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQ 467
Cdd:PRK11819 384 GETVKLAYVDQS-RDALDPNkTVWEEIsggLDIIKVgnREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQ 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 468 DINLLILDEPTNHLDIESREVLEEALEDFQGSLLAVSHDRYFLNKL------FD---KIYWieakkihcFEGNYTwAKEK 538
Cdd:PRK11819 463 GGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIathilaFEgdsQVEW--------FEGNFQ-EYEE 533
|
....*
gi 503253044 539 MTKRR 543
Cdd:PRK11819 534 DKKRR 538
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-589 |
7.54e-92 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 296.48 E-value: 7.54e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 24 FEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQIPdyhdstsTKEVLKSAFSPLLQ-MEEKME 102
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDP-------PRNVEGTVYDFVAEgIEEQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 103 KLEA----EMGVETDPNklQKLMGEYGELQDQYANNGGYEIESNIEKIAHGLNIQMfiHSPFSQLSGGEKTKVGLGLMLL 178
Cdd:PRK11147 97 YLKRyhdiSHLVETDPS--EKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 179 KQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGEVTTYHTNFTGFVKEKEEKLLKE 258
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNYDQYLLEKEEALRVE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 259 FQAYEEQQKKIKK----MKEAIKRlrdwanratppnadlhRRARNmE---RAL-----ERMEKLNRPilnrTKMNLEMES 326
Cdd:PRK11147 253 ELQNAEFDRKLAQeevwIRQGIKA----------------RRTRN-EgrvRALkalrrERSERREVM----GTAKMQVEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 327 TERSGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQNI 406
Cdd:PRK11147 312 ASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 407 FSSIKDETVIETFRD-----VVNvteGEARHILA---RFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPT 478
Cdd:PRK11147 392 AELDPEKTVMDNLAEgkqevMVN---GRPRHVLGylqDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSNLLILDEPT 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 479 NHLDIESREVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAK-KIHCFEGNYTWAKEKMTKRRESTlQLSLEKKKEV 557
Cdd:PRK11147 469 NDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEGNgKIGRYVGGYHDARQQQAQYLALK-QPAVKKKEEA 547
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 503253044 558 SLPKKEPIKNKRK--------DAENLEEDLVKLEDSIVAL 589
Cdd:PRK11147 548 AAPKAETVKRSSKklsyklqrELEQLPQLLEDLEAEIEAL 587
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
26-592 |
6.30e-82 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 270.50 E-value: 6.30e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 26 IKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQipdyhdstSTKEVLKSAFSPLLQMEEKMEKLE 105
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQ--------ETPALPQPALEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 106 AEMGVETDPNKLQKLMGEYGELQDQYAnnggYEIESNIEKIAHGLNI-QMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLL 184
Cdd:PRK10636 96 AQLHDANERNDGHAIATIHGKLDAIDA----WTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQALICRSDLL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 185 LLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGEVTTYHTNFTGFVKEKEEKLLKEFQAYEE 264
Cdd:PRK10636 172 LLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLAQQQAMYES 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 265 QQKKIKKMKEAIKRLRDWANRAtppnadlhRRARNMERALERMEkLNRPILNRTKMNLEMESTERSGNDVIMLKDISKCF 344
Cdd:PRK10636 252 QQERVAHLQSYIDRFRAKATKA--------KQAQSRIKMLERME-LIAPAHVDNPFHFSFRAPESLPNPLLKMEKVSAGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQNIFSSIK-DETVIETF-RDV 422
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRaDESPLQHLaRLA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 423 VNVTEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSLLA 502
Cdd:PRK10636 403 PQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 503 VSHDRYFLNKLFDKIYWIEAKKIHCFEGNYTWAKEKMTKRRESTLQLSLEKKKEVSLPKKEPIKNKRKDAE--------- 573
Cdd:PRK10636 483 VSHDRHLLRSTTDDLYLVHDGKVEPFDGDLEDYQQWLSDVQKQENQTDEAPKENNANSAQARKDQKRREAElrtqtqplr 562
|
570 580
....*....|....*....|...
gi 503253044 574 ----NLEEDLVKLEDSIVALDKK 592
Cdd:PRK10636 563 keiaRLEKEMEKLNAQLAQAEEK 585
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-532 |
2.90e-78 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 257.90 E-value: 2.90e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIicSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQipD---Y 77
Cdd:PRK15064 1 ML--STANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQ--DqfaF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 78 HDSTstkeVLKSAFSPLLQMEEKMEKLEA-----EMgVETDPNKLQKLMGEYGELqdqyannGGYEIESNIEKIAHGLNI 152
Cdd:PRK15064 77 EEFT----VLDTVIMGHTELWEVKQERDRiyalpEM-SEEDGMKVADLEVKFAEM-------DGYTAEARAGELLLGVGI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 153 QMFIHS-PFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVID 231
Cdd:PRK15064 145 PEEQHYgLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMAD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 232 LEDGEVTTYHTNFTGFVKEKEekllkefQAYEEQQKKIKKMKEAIKRLRDWANRATpPNADlhrRARnmeRALERMEKLN 311
Cdd:PRK15064 225 LDYGELRVYPGNYDEYMTAAT-------QARERLLADNAKKKAQIAELQSFVSRFS-ANAS---KAK---QATSRAKQID 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 312 RPILNRTK----MN--LEMESTERSGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLF 385
Cdd:PRK15064 291 KIKLEEVKpssrQNpfIRFEQDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 386 PDKGEVRIGSNVKIGYLSQNIFSSI-KDETVIETFRDVVNVTEGE--ARHILARFMFYGYTVFQKVSQLSGGERMRLRLA 462
Cdd:PRK15064 371 PDSGTVKWSENANIGYYAQDHAYDFeNDLTLFDWMSQWRQEGDDEqaVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFG 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 463 QLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKIHCFEGNY 532
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTY 520
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
335-524 |
1.15e-59 |
|
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: 195.75 E-value: 1.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQnifssikdet 414
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 415 vietfrdvvnvtegearhilarfmfygytvfqkvsqLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALE 494
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 503253044 495 DFQGSLLAVSHDRYFLNKLFDKIYWIEAKK 524
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-532 |
4.83e-54 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 196.62 E-value: 4.83e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAgeetpdtgdIH----LKKDAAVGYLTQIPDYHDSTSTKEVLKS 89
Cdd:PLN03073 188 GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMA---------MHaidgIPKNCQILHVEQEVVGDDTTALQCVLNT 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 90 AFSPLLQMEEKMEKLEAEMGVETDPNKLQKLMGEYGELQDQYANN------------GGYEIESNIEKIAHGLNIQMFI- 156
Cdd:PLN03073 259 DIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKDAVSQrleeiykrleliDAYTAEARAASILAGLSFTPEMq 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 157 HSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGE 236
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 237 VTTYHTNFTGFVKEKEEKLLKEFQAYEEQQKKIKKMKEAIKRLRDWANRATPPNADLhrrarnmeRALERMEKLNRpILN 316
Cdd:PLN03073 419 LVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRI--------KALDRLGHVDA-VVN 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 317 RTKMNLEMESTE-RSGNDVIMLKDISKCF-GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG 394
Cdd:PLN03073 490 DPDYKFEFPTPDdRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRS 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 395 SNVKIGYLSQNIFS--SIKDETVIETFRDVVNVTEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLL 472
Cdd:PLN03073 570 AKVRMAVFSQHHVDglDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHIL 649
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 473 ILDEPTNHLDIESREVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKIHCFEGNY 532
Cdd:PLN03073 650 LLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTF 709
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-245 |
6.57e-44 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 164.47 E-value: 6.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 2 IICSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQIPDYHDST 81
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 82 STkevlksafsPLLQMEEkmeklEAEMGVETDPNKLQKLMGEYGELQDQYAnnggyeiesniekiahglniqmfihspfS 161
Cdd:COG0488 394 KT---------VLDELRD-----GAPGGTEQEVRGYLGRFLFSGDDAFKPV----------------------------G 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 162 QLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGEVTTYH 241
Cdd:COG0488 432 VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYP 511
|
....
gi 503253044 242 TNFT 245
Cdd:COG0488 512 GGYD 515
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
5-236 |
3.43e-42 |
|
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: 148.75 E-value: 3.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYltqipdyhdststk 84
Cdd:cd03221 2 ELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGY-------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 evlksafspllqmeekmekleaemgvetdpnklqklmgeygelqdqyannggyeiesniekiahglniqmfihspFSQLS 164
Cdd:cd03221 68 ---------------------------------------------------------------------------FEQLS 72
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 165 GGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGE 236
Cdd:cd03221 73 GGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
334-528 |
1.08e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.58 E-value: 1.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV-----KIGYLSQNif 407
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfGKPPrrarrRIGYVPQR-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 408 ssikdETVIETF----RDVV------------NVTEGE---ARHILARFMFYGYtVFQKVSQLSGGERMRLRLAQLMYQD 468
Cdd:COG1121 84 -----AEVDWDFpitvRDVVlmgrygrrglfrRPSRADreaVDEALERVGLEDL-ADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 469 INLLILDEPTNHLDIESREVLEEALEDFQG---SLLAVSHDRYFLNKLFDKIYWIeAKKIHCF 528
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLL-NRGLVAH 219
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-237 |
1.44e-29 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 117.27 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIicSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIH----------LKKDAAVGY 70
Cdd:COG4555 1 MI--EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILidgedvrkepREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 71 LTQIPDYHDSTSTKEVLKSafspllqmeekmekleaemgvetdpnklqklmgeYGELQDqyanNGGYEIESNIEKIAHGL 150
Cdd:COG4555 79 LPDERGLYDRLTVRENIRY----------------------------------FAELYG----LFDEELKKRIEELIELL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 151 NIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVN 227
Cdd:COG4555 121 GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKegkTVLFSSHIMQEVEALCD 200
|
250
....*....|
gi 503253044 228 KVIDLEDGEV 237
Cdd:COG4555 201 RVVILHKGKV 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
337-525 |
3.27e-29 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 114.91 E-value: 3.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIGYLSQN 405
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 406 ifSSIKDETVIETFRDVVN-----VTEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNH 480
Cdd:COG4619 83 --PALWGGTVRDNLPFPFQlrerkFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503253044 481 LDIESREVLEEALEDF----QGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:COG4619 161 LDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
337-524 |
4.71e-29 |
|
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: 113.11 E-value: 4.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGsNVKIGYLSqnifssikdetvi 416
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID-GKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 417 etfrdvvnvtegeaRHILARFMFYgytvfqkVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDF 496
Cdd:cd00267 68 --------------LEELRRRIGY-------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
|
170 180 190
....*....|....*....|....*....|.
gi 503253044 497 QG---SLLAVSHDRYFLNKLFDKIYWIEAKK 524
Cdd:cd00267 127 AEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
337-525 |
5.42e-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: 113.26 E-value: 5.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV---------KIGYLSQNi 406
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIkkepeevkrRIGYLPEE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 407 FSSIKDETVIETFRdvvnvtegearhilarfmfygytvfqkvsqLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR 486
Cdd:cd03230 82 PSLYENLTVRENLK------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESR 131
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503253044 487 EVLEEALEDF---QGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:cd03230 132 REFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
337-524 |
2.41e-28 |
|
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: 112.57 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK---------IGYLSQNi 406
Cdd:COG4133 5 AENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRdaredyrrrLAYLGHA- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 407 fSSIKDE-TVIETFR-----DVVNVTEGEARHILARFMFYGYTvFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNH 480
Cdd:COG4133 84 -DGLKPElTVRENLRfwaalYGLRADREAIDEALEAVGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503253044 481 LDIESREVLEEALEDF---QGSLLAVSHDRYFLnkLFDKIYWIEAKK 524
Cdd:COG4133 162 LDAAGVALLAELIAAHlarGGAVLLTTHQPLEL--AAARVLDLGDFK 206
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
337-528 |
6.42e-28 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 111.47 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI------GSNVKIGYLSQniFSSI 410
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQ--RRSI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 411 kDETVIETFRDVVnvTEGEARHILArFMFYGYTVFQKV-----------------SQLSGGERMRLRLAQLMYQDINLLI 473
Cdd:cd03235 80 -DRDFPISVRDVV--LMGLYGHKGL-FRRLSKADKAKVdealervglseladrqiGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 474 LDEPTNHLDIESREVLEEALEDFQG---SLLAVSHDRYFLNKLFDKIYWIeAKKIHCF 528
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLL-NRTVVAS 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
337-528 |
1.19e-27 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 109.83 E-value: 1.19e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIGYLSQN 405
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLaslspkelarKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 406 IfssikdetvietfrDVVNVTegearHILARFmfygytvfqkVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIES 485
Cdd:cd03214 82 L--------------ELLGLA-----HLADRP----------FNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503253044 486 R-EVLE--EAL-EDFQGSLLAVSHDryfLN---KLFDKIYWIEAKKIHCF 528
Cdd:cd03214 133 QiELLEllRRLaRERGKTVVMVLHD---LNlaaRYADRVILLKDGRIVAQ 179
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
335-518 |
5.40e-27 |
|
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: 107.47 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGD--KLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGY 401
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdGVDLRdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 402 LSQN--IFS-SIKDetvietfrdvvNVtegearhilarfmfygytvfqkvsqLSGGERMRLRLAQLMYQDINLLILDEPT 478
Cdd:cd03228 81 VPQDpfLFSgTIRE-----------NI-------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503253044 479 NHLDIESREVLEEALEDFQG--SLLAVSHdRYFLNKLFDKIY 518
Cdd:cd03228 125 SALDPETEALILEALRALAKgkTVIVIAH-RLSTIRDADRII 165
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
14-506 |
3.26e-26 |
|
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: 112.69 E-value: 3.26e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPD---TGDIHLK-KDAA----------VGYLTQIPDyhd 79
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDgRDLLelsealrgrrIGMVFQDPM--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 80 ststkevlkSAFSPLLQMEEKMEKLEaemgvetdpnkLQKLMGEygelqdqyannggyEIESNIEKIAHGLNIQMFIHSP 159
Cdd:COG1123 94 ---------TQLNPVTVGDQIAEALE-----------NLGLSRA--------------EARARVLELLEAVGLERRLDRY 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 160 FSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMA----VEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDG 235
Cdd:COG1123 140 PHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDG 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 236 EVTTYHTNFTGFVKEkeekllkefqayeeqqkkikKMKEAIKRLRDWANRATPPNADlhrrarnmeralermeklNRPIL 315
Cdd:COG1123 220 RIVEDGPPEEILAAP--------------------QALAAVPRLGAARGRAAPAAAA------------------AEPLL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 316 nRTKmNLEMESTERSGNDVIMLKDISkcF----GDKLlfegvnmhityqnraAIIGENGTGKSTLLKLILQQLFPDKGEV 391
Cdd:COG1123 262 -EVR-NLSKRYPVRGKGGVRAVDDVS--LtlrrGETL---------------GLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 392 RI-GSNV-------------KIGYLSQNIFSS------IKDEtVIETFRDVVNVTEGEARHILARFMfygytvfQKV--- 448
Cdd:COG1123 323 LFdGKDLtklsrrslrelrrRVQMVFQDPYSSlnprmtVGDI-IAEPLRLHGLLSRAERRERVAELL-------ERVglp 394
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 449 --------SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR----EVLEEALEDFQGSLLAVSHD 506
Cdd:COG1123 395 pdladrypHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRDLQRELGLTYLFISHD 464
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-525 |
1.71e-25 |
|
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: 110.66 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEET--PDTGDI--HLKKDAAVGYLtqipdyhdst 81
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyHVALCEKCGYV---------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 82 stkEVLKSAFSPLLQMEEKMEKLEAEMGVETDPNK----------LQKLMGEYGE---LQD--QYANNGGYEIESNIEKI 146
Cdd:TIGR03269 73 ---ERPSKVGEPCPVCGGTLEPEEVDFWNLSDKLRrrirkriaimLQRTFALYGDdtvLDNvlEALEEIGYEGKEAVGRA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 147 AHGLNIQMFIHSPF---SQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLR----DYSGTVLVISHDR 219
Cdd:TIGR03269 150 VDLIEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeavkASGISMVLTSHWP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 220 YFLDEVVNKVIDLEDGEVttyhtnftgfvkekeekllkefqayeeqqKKIKKMKEAIkrlrdwanratppnadlhrrARN 299
Cdd:TIGR03269 230 EVIEDLSDKAIWLENGEI-----------------------------KEEGTPDEVV--------------------AVF 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 300 MERALErmeklnrpilnrtkmnLEMESTERSGNDVIMLKDISKCF-----GDKLLFEGVNMHITYQNRAAIIGENGTGKS 374
Cdd:TIGR03269 261 MEGVSE----------------VEKECEVEVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 375 TLLKLILQQLFPDKGE--VRIGSN--------------VK--IGYLSQNiFSSIKDETVIETFRD--------------- 421
Cdd:TIGR03269 325 TLSKIIAGVLEPTSGEvnVRVGDEwvdmtkpgpdgrgrAKryIGILHQE-YDLYPHRTVLDNLTEaiglelpdelarmka 403
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 422 -----VVNVTEGEARHILARFmfygytvfqkVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD-IESREVLE---EA 492
Cdd:TIGR03269 404 vitlkMVGFDEEKAEEILDKY----------PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHsilKA 473
|
570 580 590
....*....|....*....|....*....|...
gi 503253044 493 LEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:TIGR03269 474 REEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-234 |
2.21e-25 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 104.10 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKD----------AAVGYLtqi 74
Cdd:COG4133 4 EAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEpirdaredyrRRLAYL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 75 pdYHDSTstkevLKSAFSPLlqmeekmEKLEAemgvetdpnkLQKLmgeYGELQDqyannggyeiESNIEKIAHGLNIQM 154
Cdd:COG4133 81 --GHADG-----LKPELTVR-------ENLRF----------WAAL---YGLRAD----------REAIDEALEAVGLAG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 155 FIHSPFSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHDRYF 221
Cdd:COG4133 124 LADLPVRQLSAGQKRRVALArlllspaplwLL----------DEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLE 193
|
250
....*....|...
gi 503253044 222 LDEVvnKVIDLED 234
Cdd:COG4133 194 LAAA--RVLDLGD 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
334-525 |
2.90e-25 |
|
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: 104.94 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV---------KIGYLS 403
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIdGEDVrkeprearrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 404 QNIFS----SIKD--ETVIETFRDVVNVTEGEARHILARFMFYGYTVfQKVSQLSGGERMRLRLAQLMYQDINLLILDEP 477
Cdd:COG4555 81 DERGLydrlTVREniRYFAELYGLFDEELKKRIEELIELLGLEEFLD-RRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503253044 478 TNHLDIESREVLEEALEDFQGSLLAV---SHDRYFLNKLFDKIYWIEAKKI 525
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVlfsSHIMQEVEALCDRVVILHKGKV 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
334-506 |
4.38e-25 |
|
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: 104.74 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------K 398
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSL----PPgevtALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 IGYLSQNiFSSIKDETVietfRDVV------------NVTEGE---ARHILARFmfyGYTVF--QKVSQLSGGERMRLRL 461
Cdd:COG1120 77 IAYVPQE-PPAPFGLTV----RELValgryphlglfgRPSAEDreaVEEALERT---GLEHLadRPVDELSGGERQRVLI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503253044 462 AQLMYQDINLLILDEPTNHLDIESR-EVLE--EALEDFQG-SLLAVSHD 506
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDLAHQlEVLEllRRLARERGrTVVMVLHD 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
14-237 |
1.98e-24 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 102.03 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL------KKDAA-----VGYLTQIPDY--HDS 80
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdgkditKKNLRelrrkVGLVFQNPDDqlFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 81 TSTKEVlksAFSPLlqmeekmekleaEMGVETDpnklqklmgeygelqdqyannggyEIESNIEKIAHGLNIQMFIHSPF 160
Cdd:COG1122 92 TVEEDV---AFGPE------------NLGLPRE------------------------EIRERVEEALELVGLEHLADRPP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 161 SQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVN 227
Cdd:COG1122 133 HELSGGQKQRVAIAgvlamepevlVL----------DEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELAD 202
|
250
....*....|
gi 503253044 228 KVIDLEDGEV 237
Cdd:COG1122 203 RVIVLDDGRI 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-236 |
2.09e-24 |
|
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: 101.39 E-value: 2.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNA--IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK---------KDAA--VGYL 71
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslKELRrkVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 72 TQIPDYHDSTST--KEVlksAFSPL-LQMEEKmekleaemgvetdpnklqklmgeygelqdqyannggyEIESNIEKIAH 148
Cdd:cd03225 81 FQNPDDQFFGPTveEEV---AFGLEnLGLPEE-------------------------------------EIEERVEEALE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 149 GLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEV 225
Cdd:cd03225 121 LVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLEL 200
|
250
....*....|.
gi 503253044 226 VNKVIDLEDGE 236
Cdd:cd03225 201 ADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
335-506 |
1.05e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 100.14 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV---------KIG 400
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTV----EPgeifGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlGEDVardpaevrrRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 401 YLSQNiFSSIKDETVIET---FRDVVNVTEGEAR----HILARFmfyGYTVF--QKVSQLSGGERMRLRLAQLMYQDINL 471
Cdd:COG1131 77 YVPQE-PALYPDLTVRENlrfFARLYGLPRKEAReridELLELF---GLTDAadRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190
....*....|....*....|....*....|....*...
gi 503253044 472 LILDEPTNHLDIESREVLEEALEDF--QG-SLLAVSHD 506
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLRELaaEGkTVLLSTHY 190
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
344-558 |
4.84e-23 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 103.05 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQNIFsSIKDETVIETF---- 419
Cdd:PRK15064 11 FGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQF-AFEEFTVLDTVimgh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 420 ---------RDVV----NVTEGE---ARHILARFMFY-GYTV------------------FQKVSQLSGGERMRLRLAQL 464
Cdd:PRK15064 90 telwevkqeRDRIyalpEMSEEDgmkVADLEVKFAEMdGYTAearagelllgvgipeeqhYGLMSEVAPGWKLRVLLAQA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 465 MYQDINLLILDEPTNHLDIESREVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKIHCFEGNYTWAKEKMTKRRE 544
Cdd:PRK15064 170 LFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVYPGNYDEYMTAATQARE 249
|
250
....*....|....
gi 503253044 545 STLQLSLEKKKEVS 558
Cdd:PRK15064 250 RLLADNAKKKAQIA 263
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
325-525 |
8.65e-23 |
|
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: 102.54 E-value: 8.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 325 ESTERSGNDVIMLKDISKCF--GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK--- 398
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLRdld 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 -------IGYLSQN--IFSSikdetvieTFRDVV-----NVTEGEARHILAR-----F---MFYGY--TVFQKVSQLSGG 454
Cdd:COG4987 404 eddlrrrIAVVPQRphLFDT--------TLRENLrlarpDATDEELWAALERvglgdWlaaLPDGLdtWLGEGGRRLSGG 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 455 ERMRLRLAQLMYQDINLLILDEPTNHLDIES-REVLEEALEDFQG-SLLAVSHDRYFLNKlFDKIYWIEAKKI 525
Cdd:COG4987 476 ERRRLALARALLRDAPILLLDEPTEGLDAATeQALLADLLEALAGrTVLLITHRLAGLER-MDRILVLEDGRI 547
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
335-527 |
8.79e-23 |
|
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: 97.40 E-value: 8.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCF-GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIGYL 402
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVdGKDItkknlrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 403 SQN----IFSsikdETVIEtfrDV----VN--VTEGEAR----HILARFMFYGYtVFQKVSQLSGGERMRLRLAQLMYQD 468
Cdd:COG1122 81 FQNpddqLFA----PTVEE---DVafgpENlgLPREEIRerveEALELVGLEHL-ADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 469 INLLILDEPTNHLDIESREVLEEALEDFQG---SLLAVSHDRYFLNKLFDKIYWIEAKKIHC 527
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDGRIVA 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
8-237 |
1.25e-22 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 102.56 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 8 KVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQipdyhdstSTKEVL 87
Cdd:PRK10636 317 KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ--------HQLEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 88 KSAFSPLLQMEEKMEKlEAEmgvetdpNKLQKLMGEYGELQDQyannggyeiesniekiahglniqmfIHSPFSQLSGGE 167
Cdd:PRK10636 389 RADESPLQHLARLAPQ-ELE-------QKLRDYLGGFGFQGDK-------------------------VTEETRRFSGGE 435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 168 KTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:PRK10636 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
325-525 |
1.61e-22 |
|
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: 101.76 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 325 ESTERSGNDVIMLKDISKCFGD-KLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNV-- 397
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSYPGgRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINgvdlSDLdp 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 -----KIGYLSQN--IFS-SIKD--------------ETVIET--FRDVVN---------VTEGEARhilarfmfygytv 444
Cdd:COG4988 407 aswrrQIAWVPQNpyLFAgTIREnlrlgrpdasdeelEAALEAagLDEFVAalpdgldtpLGEGGRG------------- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 445 fqkvsqLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALED-FQGS-LLAVSHDRYFLnKLFDKIYWIEA 522
Cdd:COG4988 474 ------LSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlAKGRtVILITHRLALL-AQADRILVLDD 546
|
...
gi 503253044 523 KKI 525
Cdd:COG4988 547 GRI 549
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
350-479 |
1.63e-22 |
|
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: 94.25 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 350 FEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG-----------SNVKIGYLSQNiFSSIKDETVIET 418
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD-PQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 419 FRDVVNVT-------EGEARHILARFMFYGY---TVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTN 479
Cdd:pfam00005 80 LRLGLLLKglskrekDARAEEALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
5-237 |
1.71e-22 |
|
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: 97.04 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK---------KDAA--VGYLTQ 73
Cdd:COG1120 3 EAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslsrRELArrIAYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 74 IPDYHDSTSTKEVLksafspllqmeekmekleaEMGvetdpnKL--QKLMGEYGElQDqyannggYEIesnIEKIAHGLN 151
Cdd:COG1120 83 EPPAPFGLTVRELV-------------------ALG------RYphLGLFGRPSA-ED-------REA---VEEALERTG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 152 IQMFIHSPFSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDL---MAV-EWLGSFLRDYSGTVLVISH 217
Cdd:COG1120 127 LEHLADRPVDELSGGERQRVLIAralaqeppllLL----------DEPTSHLDLahqLEVlELLRRLARERGRTVVMVLH 196
|
250 260
....*....|....*....|....*
gi 503253044 218 D-----RYFldevvNKVIDLEDGEV 237
Cdd:COG1120 197 DlnlaaRYA-----DRLVLLKDGRI 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
296-525 |
2.43e-22 |
|
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: 101.83 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 296 RARNMERALERMEKLnrpilnrtkMNLEMESTERSGNDV-------IMLKDISkcFG----DKLLFEGVNMHITYQNRAA 364
Cdd:COG2274 437 RFQDAKIALERLDDI---------LDLPPEREEGRSKLSlprlkgdIELENVS--FRypgdSPPVLDNISLTIKPGERVA 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGYLSQN--IFS-SIKD-----------ETVIETF 419
Cdd:COG2274 506 IVGRSGSGKSTLLKLLLGLYEPTSGRILIdGIDLRqidpaslrrqIGVVLQDvfLFSgTIREnitlgdpdatdEEIIEAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 420 RDVvNVTEgearHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG- 498
Cdd:COG2274 586 RLA-GLHD----FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKg 660
|
250 260
....*....|....*....|....*...
gi 503253044 499 -SLLAVSHDRYFLnKLFDKIYWIEAKKI 525
Cdd:COG2274 661 rTVIIIAHRLSTI-RLADRIIVLDKGRI 687
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
337-518 |
2.75e-22 |
|
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: 95.23 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGD--KLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIGYLS 403
Cdd:cd03225 2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVdGKDLtklslkelrrKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 404 QNIFSSIKDETVIEtfrDVV------NVTEGEARHILARFM-FYGYTVFQK--VSQLSGGERMRLRLAQLMYQDINLLIL 474
Cdd:cd03225 82 QNPDDQFFGPTVEE---EVAfglenlGLPEEEIEERVEEALeLVGLEGLRDrsPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503253044 475 DEPTNHLDIESREVLEEALEDFQG---SLLAVSHDRYFLNKLFDKIY 518
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVI 205
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
344-506 |
6.07e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 93.84 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQNifSSIkDETVIETFRDVV 423
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQR--SEV-PDSLPLTVRDLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 424 NV-----------TEGEAR----HILARFmfyGYTVFQK--VSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR 486
Cdd:NF040873 79 AMgrwarrglwrrLTRDDRaavdDALERV---GLADLAGrqLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESR 155
|
170 180
....*....|....*....|...
gi 503253044 487 EVLEEALEDFQG---SLLAVSHD 506
Cdd:NF040873 156 ERIIALLAEEHArgaTVVVVTHD 178
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
332-505 |
1.60e-21 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 94.00 E-value: 1.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 332 NDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDK-------GEVRIGSNV-----KI 399
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYgndvrlfGERRGGEDVwelrkRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 400 GYLSQNIFSSI-KDETVIET----FRDVV----NVTEGE---ARHILARFMFYGYTvFQKVSQLSGGERMRLRLAQLMYQ 467
Cdd:COG1119 81 GLVSPALQLRFpRDETVLDVvlsgFFDSIglyrEPTDEQrerARELLELLGLAHLA-DRPFGTLSQGEQRRVLIARALVK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503253044 468 DINLLILDEPTNHLDIESREVLEEALEDF--QG--SLLAVSH 505
Cdd:COG1119 160 DPELLILDEPTAGLDLGARELLLALLDKLaaEGapTLVLVTH 201
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
330-531 |
2.81e-21 |
|
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: 93.12 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 330 SGNDVIMLKDISKCFGDKLLFEGVNMHItYQNRA-AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV---------- 397
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDV-PRGEIlAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdGQDItglsekelye 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 ---KIGYLSQN--IFSSIkdeTVIEtfrdvvNV----------TEGEARHIlarfmfygytVFQKV-------------S 449
Cdd:COG1127 80 lrrRIGMLFQGgaLFDSL---TVFE------NVafplrehtdlSEAEIREL----------VLEKLelvglpgaadkmpS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 450 QLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHDryfLNKLF---DKIYWIEA 522
Cdd:COG1127 141 ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVVTHD---LDSAFaiaDRVAVLAD 217
|
....*....
gi 503253044 523 KKIHcFEGN 531
Cdd:COG1127 218 GKII-AEGT 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
5-237 |
4.70e-21 |
|
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: 90.53 E-value: 4.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI-----HLKKDAA-----VGYLTQI 74
Cdd:cd03230 2 EVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIkvlgkDIKKEPEevkrrIGYLPEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 75 PDYHDSTSTKEVLKsafspllqmeekmekleaemgvetdpnklqklmgeygelqdqyannggyeiesniekiahglniqm 154
Cdd:cd03230 82 PSLYENLTVRENLK------------------------------------------------------------------ 95
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 155 fihspfsqLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHDRYFLDEVVNKVID 231
Cdd:cd03230 96 --------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAI 167
|
....*.
gi 503253044 232 LEDGEV 237
Cdd:cd03230 168 LNNGRI 173
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
5-225 |
7.07e-21 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 92.05 E-value: 7.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL-----KKDAA-----VGYLTQI 74
Cdd:COG1131 2 EVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvARDPAevrrrIGYVPQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 75 PDYHDSTSTKEVLksafspllqmeekmekleaemgvetdpnklqKLMGE-YGelqdqyanNGGYEIESNIEKIAHGLNIQ 153
Cdd:COG1131 82 PALYPDLTVRENL-------------------------------RFFARlYG--------LPRKEARERIDELLELFGLT 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 154 MFIHSPFSQLSGGEKTKVGLG-----------LmllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDr 219
Cdd:COG1131 123 DAADRKVGTLSGGMKQRLGLAlallhdpelliL-----------DEPTSGLDPEARRELWELLRELAAegkTVLLSTHY- 190
|
....*.
gi 503253044 220 yfLDEV 225
Cdd:COG1131 191 --LEEA 194
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-236 |
1.27e-20 |
|
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: 88.84 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKkdaavgyltqipdyhdststk 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 evlksafspllqmeekmekleaemGVETDPNKLQKLMgeygelqdqyannggyeiesniEKIAhglniqmFIHspfsQLS 164
Cdd:cd00267 60 ------------------------GKDIAKLPLEELR----------------------RRIG-------YVP----QLS 82
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 165 GGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVNKVIDLEDGE 236
Cdd:cd00267 83 GGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEegrTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
344-532 |
4.08e-20 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 94.63 E-value: 4.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQ--------NIFSSI----- 410
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQdpprnvegTVYDFVaegie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 411 KDETVIETFRDVVNVTEGE--ARHI--LARFM--------------------FYGYTVFQKVSQLSGGERMRLRLAQLMY 466
Cdd:PRK11147 93 EQAEYLKRYHDISHLVETDpsEKNLneLAKLQeqldhhnlwqlenrinevlaQLGLDPDAALSSLSGGWLRKAALGRALV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 467 QDINLLILDEPTNHLDIESREVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKIHCFEGNY 532
Cdd:PRK11147 173 SNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYPGNY 238
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
335-530 |
5.15e-20 |
|
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: 89.48 E-value: 5.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV-------------KIG 400
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 401 YLSQN--IFSSIkdeTVI--------ETFRDVVNVTEGEARHILARFMFYGyTVFQKVSQLSGGERMRLRLAQLMYQDIN 470
Cdd:cd03261 81 MLFQSgaLFDSL---TVFenvafplrEHTRLSEEEIREIVLEKLEAVGLRG-AEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 471 LLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHDryfLNKLF---DKIYWIEAKKIhCFEG 530
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELgltsIMVTHD---LDTAFaiaDRIAVLYDGKI-VAEG 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
352-507 |
8.80e-20 |
|
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: 93.12 E-value: 8.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 352 GVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV-----------KIGYLSQN--IFS-SIK------ 411
Cdd:TIGR02857 340 PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPladadadswrdQIAWVPQHpfLFAgTIAenirla 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 412 -----DETVIETFRDVvnvteGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR 486
Cdd:TIGR02857 420 rpdasDAEIREALERA-----GLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
|
170 180
....*....|....*....|...
gi 503253044 487 EVLEEALEDF-QG-SLLAVSHDR 507
Cdd:TIGR02857 495 AEVLEALRALaQGrTVLLVTHRL 517
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-240 |
1.20e-19 |
|
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: 86.72 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL-KKDAAvgyltqipdyhdSTST 83
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLdGKDLA------------SLSP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 84 KEVLKS-AFspLLQMeekmekLEAemgvetdpnklqklmgeygelqdqyannggyeiesniekiahgLNIQMFIHSPFSQ 162
Cdd:cd03214 69 KELARKiAY--VPQA------LEL-------------------------------------------LGLAHLADRPFNE 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 163 LSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDL---MAV-EWLGSFLRDYSGTVLVISHD-----RYFld 223
Cdd:cd03214 98 LSGGERQRVLLAralaqeppilLL----------DEPTSHLDIahqIELlELLRRLARERGKTVVMVLHDlnlaaRYA-- 165
|
250
....*....|....*..
gi 503253044 224 evvNKVIDLEDGEVTTY 240
Cdd:cd03214 166 ---DRVILLKDGRIVAQ 179
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-517 |
1.23e-19 |
|
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: 92.93 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 27 KEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK--KDAAVGYL--TQIPDYHDSTSTKEvLKSAFSPllQMEEKME 102
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEpsWDEVLKRFrgTELQDYFKKLANGE-IKVAHKP--QYVDLIP 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 103 KLeaemgvetdpnklqkLMGEYGELQDQYANNGgyeiesNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPD 182
Cdd:COG1245 174 KV---------------FKGTVRELLEKVDERG------KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDAD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 183 LLLLDEPTNHLDL---MAVewlGSFLRDYSG---TVLVISHDRYFLDeVVNKVIDLEDGEVTTYhtnftGFVKekeekll 256
Cdd:COG1245 233 FYFFDEPSSYLDIyqrLNV---ARLIRELAEegkYVLVVEHDLAILD-YLADYVHILYGEPGVY-----GVVS------- 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 257 kefqayeeqqkKIKKMKEAIkrlrdwanratppNADL--HRRARNMeraleRMEKlnRPILNRTKMnlemESTERSGNDV 334
Cdd:COG1245 297 -----------KPKSVRVGI-------------NQYLdgYLPEENV-----RIRD--EPIEFEVHA----PRREKEEETL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGD-KLLFEGVNMH----ITyqnraaIIGENGTGKSTLLKLILQQLFPDKGEVRigSNVKIGYLSQNIfSS 409
Cdd:COG1245 342 VEYPDLTKSYGGfSLEVEGGEIRegevLG------IVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQYI-SP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 410 IKDETVIETFRDVVNVTEGE--ARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESRE 487
Cdd:COG1245 413 DYDGTVEEFLRSANTDDFGSsyYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 492
|
490 500 510
....*....|....*....|....*....|....
gi 503253044 488 VLEEAL----EDFQGSLLAVSHDRYFLNKLFDKI 517
Cdd:COG1245 493 AVAKAIrrfaENRGKTAMVVDHDIYLIDYISDRL 526
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
345-505 |
1.32e-19 |
|
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: 86.50 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGYLSQNI--FS-SI 410
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdGADISqwdpnelgdhVGYLPQDDelFSgSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 411 KDetvietfrdvvNVtegearhilarfmfygytvfqkvsqLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLE 490
Cdd:cd03246 93 AE-----------NI-------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170
....*....|....*...
gi 503253044 491 EALEDFQ---GSLLAVSH 505
Cdd:cd03246 137 QAIAALKaagATRIVIAH 154
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
5-237 |
2.06e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 86.79 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDA-----------AVGYLTQ 73
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPlsampppewrrQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 74 IPD-YHDStstkevLKSAFSPLLQMEEKmekleaemgvETDPNKLQKLMGEYGeLQDQYANnggyeiesniekiahglni 152
Cdd:COG4619 82 EPAlWGGT------VRDNLPFPFQLRER----------KFDRERALELLERLG-LPPDILD------------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 153 qmfihSPFSQLSGGEKTKVGL--GLMLLKQPDLllLDEPTNHLD----LMAVEWLGSFLRDYSGTVLVISHDRYFLDEVV 226
Cdd:COG4619 126 -----KPVERLSGGERQRLALirALLLQPDVLL--LDEPTSALDpentRRVEELLREYLAEEGRAVLWVSHDPEQIERVA 198
|
250
....*....|.
gi 503253044 227 NKVIDLEDGEV 237
Cdd:COG4619 199 DRVLTLEAGRL 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
362-525 |
2.11e-19 |
|
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: 87.26 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 362 RAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGYLSQNI---FSSIKDetvietfrdvvNVTE 427
Cdd:cd03245 32 KVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRqldpadlrrnIGYVPQDVtlfYGTLRD-----------NITL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 428 G----EARHILARFMFYGYTVF-------------QKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLE 490
Cdd:cd03245 101 GaplaDDERILRAAELAGVTDFvnkhpngldlqigERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLK 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 503253044 491 EALEDFQG--SLLAVSHdRYFLNKLFDKIYWIEAKKI 525
Cdd:cd03245 181 ERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-226 |
3.26e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 87.45 E-value: 3.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL------KKDAAVGYLTQIPDYHDS--TSTK 84
Cdd:COG1121 16 YGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQRAEVDWDfpITVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 EVLksafspllqmeekmekleaemgvetdpnklqkLMGEYGEL-------QDQYAnnggyEIESNIEKiahgLNIQMFIH 157
Cdd:COG1121 96 DVV--------------------------------LMGRYGRRglfrrpsRADRE-----AVDEALER----VGLEDLAD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 158 SPFSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHD-----R 219
Cdd:COG1121 135 RPIGELSGGQQQRVLLAralaqdpdllLL----------DEPFAGVDAATEEALYELLRELRRegkTILVVTHDlgavrE 204
|
....*..
gi 503253044 220 YFlDEVV 226
Cdd:COG1121 205 YF-DRVL 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
335-495 |
4.86e-19 |
|
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: 86.09 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHIT---YqnraAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK---------IGY 401
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGpgmY----GLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 402 LSQNiFSSIKDETVIEtFRDVVNVTEG--------EARHILARFMFYGYtVFQKVSQLSGGERMRLRLAQLMYQDINLLI 473
Cdd:cd03264 77 LPQE-FGVYPNFTVRE-FLDYIAWLKGipskevkaRVDEVLELVNLGDR-AKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180
....*....|....*....|..
gi 503253044 474 LDEPTNHLDIESREVLEEALED 495
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSE 175
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-517 |
6.10e-19 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 90.64 E-value: 6.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 32 VGLVGRNGSGKTTLIRLLAGEETPDTGDIH--LKKDAAVGYL--TQIPDYHDSTSTKEVlKSAFSPllQMEEKMEKLeae 107
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGDYEeePSWDEVLKRFrgTELQNYFKKLYNGEI-KVVHKP--QYVDLIPKV--- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 108 mgvetdpnklqkLMGEYGELQDQYANNGgyeiesNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLD 187
Cdd:PRK13409 176 ------------FKGKVRELLKKVDERG------KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 188 EPTNHLDL---MAVEWLgsfLRDYSG--TVLVISHDRYFLDEVVNkVIDLEDGEVTTYhtnftGFVKekeekllkefqay 262
Cdd:PRK13409 238 EPTSYLDIrqrLNVARL---IRELAEgkYVLVVEHDLAVLDYLAD-NVHIAYGEPGAY-----GVVS------------- 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 263 eeqqkKIKKMKEAIkrlrdwanratppNADLH--RRARNMeraleRMEKlnRPILNRTKMnlemESTERSGNDVIMLKDI 340
Cdd:PRK13409 296 -----KPKGVRVGI-------------NEYLKgyLPEENM-----RIRP--EPIEFEERP----PRDESERETLVEYPDL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 341 SKCFGD-KLLFEGVNMH----ITyqnraaIIGENGTGKSTLLKLILQQLFPDKGEVriGSNVKIGYLSQNIFSSiKDETV 415
Cdd:PRK13409 347 TKKLGDfSLEVEGGEIYegevIG------IVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPD-YDGTV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 416 IETFRDVVNV-------TEgearhILARFMFYgyTVFQK-VSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR- 486
Cdd:PRK13409 418 EDLLRSITDDlgssyykSE-----IIKPLQLE--RLLDKnVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRl 490
|
490 500 510
....*....|....*....|....*....|....
gi 503253044 487 ---EVLEEALEDFQGSLLAVSHDRYFLNKLFDKI 517
Cdd:PRK13409 491 avaKAIRRIAEEREATALVVDHDIYMIDYISDRL 524
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
335-522 |
6.88e-19 |
|
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: 84.55 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV------------KIGY 401
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdGEDLtdledelpplrrRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 402 LSQ--NIFSSIkdeTVIEtfrdvvNVTEGearhilarfmfygytvfqkvsqLSGGERMRLRLAQLMYQDINLLILDEPTN 479
Cdd:cd03229 81 VFQdfALFPHL---TVLE------NIALG----------------------LSGGQQQRVALARALAMDPDVLLLDEPTS 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503253044 480 HLDIESREVLEEALEDFQGSL----LAVSHDRYFLNKLFDKIYWIEA 522
Cdd:cd03229 130 ALDPITRREVRALLKSLQAQLgitvVLVTHDLDEAARLADRVVVLRD 176
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
352-506 |
2.35e-18 |
|
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: 84.69 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 352 GVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV----KIGYLSQ--NIFSS----IKDETVIETF-- 419
Cdd:cd03267 39 GISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRRigVVFGQktqlWWDLPVIDSFyl 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 420 -RDVVNVTEGEARHILARF---MFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIES----REVLEE 491
Cdd:cd03267 119 lAAIYDLPPARFKKRLDELselLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAqeniRNFLKE 198
|
170
....*....|....*
gi 503253044 492 ALEDFQGSLLAVSHD 506
Cdd:cd03267 199 YNRERGTTVLLTSHY 213
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
286-506 |
3.38e-18 |
|
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: 88.19 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 286 ATPPNADLHRRARnmeRALERMEKLNRPILNRTKMNLEMESTERSGNDVIMLKDISKCF-GDKLLFEGVNMHITYQNRAA 364
Cdd:TIGR02868 289 ALPAAAQQLTRVR---AAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVA 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLFPDKGEVRIGS-----------NVKIGYLSQN--IFSSikdeTVIETFR-DVVNVTEGEA 430
Cdd:TIGR02868 366 ILGPSGSGKSTLLATLAGLLDPLQGEVTLDGvpvssldqdevRRRVSVCAQDahLFDT----TVRENLRlARPDATDEEL 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 431 RHILARF--------MFYGY-TVFQKVSQ-LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE-SREVLEEALEDFQG- 498
Cdd:TIGR02868 442 WAALERVgladwlraLPDGLdTVLGEGGArLSGGERQRLALARALLADAPILLLDEPTEHLDAEtADELLEDLLAALSGr 521
|
....*...
gi 503253044 499 SLLAVSHD 506
Cdd:TIGR02868 522 TVVLITHH 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
335-525 |
7.27e-18 |
|
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: 81.59 E-value: 7.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFG--DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVrigsnvkigYLSQNIFSSIKD 412
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 413 etvieTFRDVVNVTEGEArhilarFMFYGyTVFQKV-SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD-IESREVLE 490
Cdd:cd03247 72 -----ALSSLISVLNQRP------YLFDT-TLRNNLgRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLS 139
|
170 180 190
....*....|....*....|....*....|....*...
gi 503253044 491 ---EALEDfqGSLLAVSHDRYFLNKlFDKIYWIEAKKI 525
Cdd:cd03247 140 lifEVLKD--KTLIWITHHLTGIEH-MDKILFLENGKI 174
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
5-235 |
8.84e-18 |
|
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: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKkdaavgyltqIPDYHDSTSTK 84
Cdd:cd03268 2 KTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD----------GKSYQKNIEAL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 EVLKS-----AFSPLLQMEEKMEKLEAEMGVEtdpnklqklmgeygelqdqyannggyeiESNIEKIAHGLNIQMFIHSP 159
Cdd:cd03268 72 RRIGAlieapGFYPNLTARENLRLLARLLGIR----------------------------KKRIDEVLDVVGLKDSAKKK 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 160 FSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSF---LRDYSGTVLVISHDRYFLDEVVNKVIDLEDG 235
Cdd:cd03268 124 VKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGIINKG 202
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
335-525 |
1.34e-17 |
|
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: 81.77 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGD----KLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV------------ 397
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 --KIGYLSQNiFSSIKDETVIEtfrdvvNV-------------TEGEARHILARFMFyGYTVFQKVSQLSGGERMRLRLA 462
Cdd:cd03255 81 rrHIGFVFQS-FNLLPDLTALE------NVelplllagvpkkeRRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 463 QLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG----SLLAVSHDRyFLNKLFDKIYWIEAKKI 525
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
337-507 |
1.48e-17 |
|
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: 81.80 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV--------KIGYLSQNiF 407
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVtgvpperrNIGMVFQD-Y 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 408 SSIKDETVIEtfrdvvNV-----------TEGEARHILARFMF----YGYtvfQKVSQLSGGERMRLRLAQLMYQDINLL 472
Cdd:cd03259 82 ALFPHLTVAE------NIafglklrgvpkAEIRARVRELLELVglegLLN---RYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 503253044 473 ILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHDR 507
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELgittIYVTHDQ 191
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
337-526 |
1.70e-17 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 81.15 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDK-LLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV--------KIGYLSQNI- 406
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDVd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 407 ----FSSIKDEtVIETFRDVVNVTEgEARHILARFMFYGYTVFQKVSqLSGGERMRLRLAQLMYQDINLLILDEPTNHLD 482
Cdd:cd03226 82 yqlfTDSVREE-LLLGLKELDAGNE-QAETVLKDLDLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503253044 483 IESREVLEEALEDFQG---SLLAVSHDRYFLNKLFDKIYWIEAKKIH 526
Cdd:cd03226 159 YKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-226 |
1.85e-17 |
|
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: 81.43 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL------KKDAAVGYLTQIPDYh 78
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQRRSI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 79 DST---STKEVLKSAfspllqmeekmekLEAEMGVETDPNKLQKlmgeygelqdqyannggyeiesniEKIAHGL---NI 152
Cdd:cd03235 80 DRDfpiSVRDVVLMG-------------LYGHKGLFRRLSKADK------------------------AKVDEALervGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 153 QMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHD----RYFLDEV 225
Cdd:cd03235 123 SELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDlglvLEYFDRV 202
|
.
gi 503253044 226 V 226
Cdd:cd03235 203 L 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
337-505 |
2.56e-17 |
|
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: 79.39 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVKIGylsqnifssik 411
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSV----RRgevhALLGENGAGKSTLMKILSGLYKPDSGEILVdGKEVSFA----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 412 detvietfrdvvNVTEGEARHIlarfmfygYTVFqkvsQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEE 491
Cdd:cd03216 68 ------------SPRDARRAGI--------AMVY----QLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170
....*....|....*..
gi 503253044 492 ALEDF--QG-SLLAVSH 505
Cdd:cd03216 124 VIRRLraQGvAVIFISH 140
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
335-506 |
4.25e-17 |
|
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: 80.59 E-value: 4.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDK----LLFEGVNMHItYQNR-AAIIGENGTGKSTLLKLILQQLFPDKGEVRI------GSNVKIGYLS 403
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSV-EEGEfVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 404 QNiFSSIKDETVIE--TF-RDVVNVTEGEARHILARFM-FYGYTVFQKV--SQLSGGERMRLRLAQLMYQDINLLILDEP 477
Cdd:cd03293 80 QQ-DALLPWLTVLDnvALgLELQGVPKAEARERAEELLeLVGLSGFENAypHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 503253044 478 TNHLDIESREVLEEAL----EDFQGSLLAVSHD 506
Cdd:cd03293 159 FSALDALTREQLQEELldiwRETGKTVLLVTHD 191
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
335-530 |
5.17e-17 |
|
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: 80.69 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGD-KLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV-------------KI 399
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdGTDInklkgkalrqlrrQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 400 GYLSQNiFSSIKDETVIE-----------TFRDVVN-VTEGE---ARHILARFMFYGYtVFQKVSQLSGGERMRLRLAQL 464
Cdd:cd03256 81 GMIFQQ-FNLIERLSVLEnvlsgrlgrrsTWRSLFGlFPKEEkqrALAALERVGLLDK-AYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 465 MYQDINLLILDEPTNHLD-IESREVLE---EALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKIhCFEG 530
Cdd:cd03256 159 LMQQPKLILADEPVASLDpASSRQVMDllkRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI-VFDG 227
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
230-322 |
8.04e-17 |
|
ABC transporter; This domain is an extension of some members of pfam00005 and other ABC-transporter families.
Pssm-ID: 463731 [Multi-domain] Cd Length: 85 Bit Score: 75.69 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 230 IDLEDGEVTTYHTNFTGFVKEKEEKLLKEFQAYEEQQKKIKKMKEAIKRLRDWANRAtppnadlhRRARNMERALERMEK 309
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKA--------KQAQSRIKALEKMER 72
|
90
....*....|...
gi 503253044 310 LNRPILNRTKMNL 322
Cdd:pfam12848 73 IEKPERDKPKLRF 85
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
334-526 |
1.99e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 78.56 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCF-GDKLLFEGVNMHI-----TYqnraaIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV------KIG 400
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIekgefVF-----LTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrrEIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 401 YLSQNI------FSSIKDETVIEtfrdvvNV------TEGEARHILARFMFygytVFQKV----------SQLSGGERMR 458
Cdd:COG2884 76 YLRRRIgvvfqdFRLLPDRTVYE------NValplrvTGKSRKEIRRRVRE----VLDLVglsdkakalpHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 459 LRLAQLMyqdIN---LLILDEPTNHLDIE-SREVLeEALEDF--QG-SLLAVSHDRYFLNKLFDKIYWIEAKKIH 526
Cdd:COG2884 146 VAIARAL---VNrpeLLLADEPTGNLDPEtSWEIM-ELLEEInrRGtTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
345-506 |
2.31e-16 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 79.09 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIGYLSQNIfssikDE 413
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLaGVDLhglsrrararRVALVEQDS-----DT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 414 TVIETFRDVVNV---------------TEGEARHILARFmfyGYTVF--QKVSQLSGGERMRLRLAQLMYQDINLLILDE 476
Cdd:TIGR03873 87 AVPLTVRDVVALgriphrslwagdsphDAAVVDRALART---ELSHLadRDMSTLSGGERQRVHVARALAQEPKLLLLDE 163
|
170 180 190
....*....|....*....|....*....|...
gi 503253044 477 PTNHLDIESR-EVLE--EALEDFQGSLLAVSHD 506
Cdd:TIGR03873 164 PTNHLDVRAQlETLAlvRELAATGVTVVAALHD 196
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
13-310 |
2.46e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 82.69 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQipdyhdstsTKEVLksafs 92
Cdd:PRK11147 329 IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQ---------HRAEL----- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 93 pllqmeekmekleaemgvetDPNKlqKLMGEYGElqdqyannGGYEIESNIEKiAHGLN-IQMFIHS------PFSQLSG 165
Cdd:PRK11147 395 --------------------DPEK--TVMDNLAE--------GKQEVMVNGRP-RHVLGyLQDFLFHpkramtPVKALSG 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 166 GEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLE-DGEVTTYhtnf 244
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEgNGKIGRY---- 519
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 245 tgfVKEKEEKLLKEFQAYEEQQKKIKKMKEAIkrlrdwANRATPPNADLHRRARNMERALE----RMEKL 310
Cdd:PRK11147 520 ---VGGYHDARQQQAQYLALKQPAVKKKEEAA------APKAETVKRSSKKLSYKLQRELEqlpqLLEDL 580
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
334-518 |
4.21e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 77.86 E-value: 4.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCF-----GDKLL--FEGVNMHItyqnRA----AIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVK---- 398
Cdd:COG4778 4 LLEVENLSKTFtlhlqGGKRLpvLDGVSFSV----AAgecvALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGwvdl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 ---------------IGYLSQniF-------SSIkdETVIETFRDV---VNVTEGEARHILARFmfygyTVFQKVSQL-- 451
Cdd:COG4778 80 aqaspreilalrrrtIGYVSQ--FlrviprvSAL--DVVAEPLLERgvdREEARARARELLARL-----NLPERLWDLpp 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 452 ---SGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDF--QG-SLLAVSHDRYFLNKLFDKIY 518
Cdd:COG4778 151 atfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGtAIIGIFHDEEVREAVADRVV 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
336-522 |
5.47e-16 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 77.34 E-value: 5.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 336 MLKDISKCFGD---KLLFEgvnmhiTYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV--------------- 397
Cdd:cd03297 2 LCVDIEKRLPDftlKIDFD------LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 KIGYLSQN--IFS--SIKDETVIETFRDVVNVTEGEARHILARFMFyGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLI 473
Cdd:cd03297 76 KIGLVFQQyaLFPhlNVRENLAFGLKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503253044 474 LDEPTNHLDIESREV----LEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEA 522
Cdd:cd03297 155 LDEPFSALDRALRLQllpeLKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMED 207
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
335-502 |
7.30e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.10 E-value: 7.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI----------GSNVKIGYLSQ 404
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpararLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 niFSSIKDE-TVIETFRDVVNVTEGEARHI------LARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEP 477
Cdd:PRK13536 122 --FDNLDLEfTVRENLLVFGRYFGMSTREIeavipsLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180
....*....|....*....|....*
gi 503253044 478 TNHLDIESREVLEEALEdfqgSLLA 502
Cdd:PRK13536 200 TTGLDPHARHLIWERLR----SLLA 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
364-506 |
1.07e-15 |
|
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: 76.78 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV-------------KIGYLSQNIFSS------IKdETVIETFRDVV 423
Cdd:cd03257 35 GLVGESGSGKSTLARAILGLLKPTSGSIIFdGKDLlklsrrlrkirrkEIQMVFQDPMSSlnprmtIG-EQIAEPLRIHG 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 424 NVTEGEARHILARFMFYGY----TVFQK-VSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR----EVLEEALE 494
Cdd:cd03257 114 KLSKKEARKEAVLLLLVGVglpeEVLNRyPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQaqilDLLKKLQE 193
|
170
....*....|..
gi 503253044 495 DFQGSLLAVSHD 506
Cdd:cd03257 194 ELGLTLLFITHD 205
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
335-506 |
1.49e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.12 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNVKIGYLSQNIFSSI 410
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALSARAASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 411 KDETVIETFrDVVNVTE-GEARHiLARFMFYGYT-----------------VFQKVSQLSGGERMRLRLAQLMYQDINLL 472
Cdd:PRK09536 84 QDTSLSFEF-DVRQVVEmGRTPH-RSRFDTWTETdraaveramertgvaqfADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 503253044 473 ILDEPTNHLDI----ESREVLEEALEDFQGSLLAVsHD 506
Cdd:PRK09536 162 LLDEPTASLDInhqvRTLELVRRLVDDGKTAVAAI-HD 198
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
332-526 |
1.75e-15 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 75.85 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 332 NDVIMLKDISKCFGDKLL----FEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRI-GSNV------- 397
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggLDR--PTSGEVLIdGQDIsslsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 -------KIGYlsqnIFSS---IKDETVIEtfrdvvNVT-------------EGEARHILARFMFYGYtVFQKVSQLSGG 454
Cdd:COG1136 80 larlrrrHIGF----VFQFfnlLPELTALE------NVAlplllagvsrkerRERARELLERVGLGDR-LDHRPSQLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 455 ERMRLRLAQLMYQDINLLILDEPTNHLDIE-SREVLE---EALEDFQGSLLAVSHDRyFLNKLFDKIYWIEAKKIH 526
Cdd:COG1136 149 QQQRVAIARALVNRPKLILADEPTGNLDSKtGEEVLEllrELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
364-521 |
1.86e-15 |
|
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: 75.34 E-value: 1.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPD-----KGEVR----IGSNVKIGYLSQNiFSSIKDETV-----IETFRDVVNVTEGE 429
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGElppnsKGGAHdpklIREGEVRAQVKLA-FENANGKKYtitrsLAILENVIFCHQGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 430 ARHILARfmfygytvfqKVSQLSGGERM------RLRLAQLMYQDINLLILDEPTNHLDIESR-----EVLEEALEDFQG 498
Cdd:cd03240 105 SNWPLLD----------MRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeeslaEIIEERKSQKNF 174
|
170 180
....*....|....*....|...
gi 503253044 499 SLLAVSHDRYFLNKLfDKIYWIE 521
Cdd:cd03240 175 QLIVITHDEELVDAA-DHIYRVE 196
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-237 |
2.39e-15 |
|
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: 76.28 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 12 MYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTG-DIH-------------LKKdaAVGY----LTQ 73
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgerrggedvweLRK--RIGLvspaLQL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 74 ipDYHDSTSTKEVLKSAFSpllqmeekmekleAEMGvetdpnklqkLMGEYGELQDQYAnnggyeiesniEKIAHGLNIQ 153
Cdd:COG1119 90 --RFPRDETVLDVVLSGFF-------------DSIG----------LYREPTDEQRERA-----------RELLELLGLA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 154 MFIHSPFSQLSGGEKTKVGLG-----------LmllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSG----TVLVISHd 218
Cdd:COG1119 134 HLADRPFGTLSQGEQRRVLIAralvkdpelliL-----------DEPTAGLDLGARELLLALLDKLAAegapTLVLVTH- 201
|
250 260
....*....|....*....|..
gi 503253044 219 ryFLDEV---VNKVIDLEDGEV 237
Cdd:COG1119 202 --HVEEIppgITHVLLLKDGRV 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
335-511 |
2.40e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.35 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IML--KDISKCFGDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK--------- 398
Cdd:PRK13548 1 AMLeaRNLSVRLGGRTLLDDVSLTL----RPgevvAILGPNGAGKSTLLRALSGELSPDSGEVRLnGRPLAdwspaelar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 -IGYLSQNifSSIkdetvieTF----RDVV-------NVTEGEARHILARFM-----------FYgytvfqkvSQLSGGE 455
Cdd:PRK13548 77 rRAVLPQH--SSL-------SFpftvEEVVamgraphGLSRAEDDALVAAALaqvdlahlagrDY--------PQLSGGE 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 456 RMRLRLA----QLMYQDIN--LLILDEPTNHLDIESREVLEEALEDF----QGSLLAVSHDryfLN 511
Cdd:PRK13548 140 QQRVQLArvlaQLWEPDGPprWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHD---LN 202
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
365-517 |
2.53e-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: 75.91 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLFPDKGEVRIgSNVKIGYLSQNIfSSIKDETVIETFRDVVN--VTEGEARHILARFMFYGY 442
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYI-KADYEGTVRDLLSSITKdfYTHPYFKTEIAKPLQIEQ 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 443 TVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDF----QGSLLAVSHDRYFLNKLFDKI 517
Cdd:cd03237 108 ILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFaennEKTAFVVEHDIIMIDYLADRL 186
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
333-506 |
2.63e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 75.92 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 333 DVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQNIFSSIKD 412
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 413 ETVIETF-RDVVNVTEGEARHILARFMfYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEE 491
Cdd:PRK09544 83 PLTVNRFlRLRPGTKKEDILPALKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170
....*....|....*....
gi 503253044 492 ALEDFQGSL----LAVSHD 506
Cdd:PRK09544 162 LIDQLRRELdcavLMVSHD 180
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
334-502 |
4.61e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 76.38 E-value: 4.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV---------KIGYLS 403
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcGEPVpsrarharqRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 404 QniFSSIK-DETVIET---FRDVVNVTEGEARHI---LARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDE 476
Cdd:PRK13537 87 Q--FDNLDpDFTVRENllvFGRYFGLSAAAARALvppLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180
....*....|....*....|....*.
gi 503253044 477 PTNHLDIESREVLEEALEdfqgSLLA 502
Cdd:PRK13537 165 PTTGLDPQARHLMWERLR----SLLA 186
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-238 |
4.88e-15 |
|
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: 78.27 E-value: 4.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL---------KKD--AAVGYLTQipDYHD-ST 81
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLggvdlrdldEDDlrRRIAVVPQ--RPHLfDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 82 STKEVLKSAfSPLLQMEEKMEKLE-AEMG--VETDPNKLQKLMGEYGElqdqyannggyeiesniekiahglniqmfihs 158
Cdd:COG4987 424 TLRENLRLA-RPDATDEELWAALErVGLGdwLAALPDGLDTWLGEGGR-------------------------------- 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 159 pfsQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLD-LMAVEWLGSFLRDYSG-TVLVISHDRYFLDEvV 226
Cdd:COG4987 471 ---RLSGGERRRLALArallrdapilLL----------DEPTEGLDaATEQALLADLLEALAGrTVLLITHRLAGLER-M 536
|
250
....*....|..
gi 503253044 227 NKVIDLEDGEVT 238
Cdd:COG4987 537 DRILVLEDGRIV 548
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
13-237 |
4.89e-15 |
|
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: 78.72 E-value: 4.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNA--IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI--------HLKKDA---AVGYLTQ------ 73
Cdd:COG2274 483 YPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIlidgidlrQIDPASlrrQIGVVLQdvflfs 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 74 ------IPDYHDSTSTKEVLKSAfspllqmeekmEKLEAEMGVETDPNKLQKLMGEYGelqdqyannggyeiesniekia 147
Cdd:COG2274 563 gtirenITLGDPDATDEEIIEAA-----------RLAGLHDFIEALPMGYDTVVGEGG---------------------- 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 148 hglniqmfihspfSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSG--TVLVI 215
Cdd:COG2274 610 -------------SNLSGGQRQRLAIArallrnprilIL----------DEATSALDAETEAIILENLRRLLKgrTVIII 666
|
250 260
....*....|....*....|..
gi 503253044 216 SHDRYFLDEvVNKVIDLEDGEV 237
Cdd:COG2274 667 AHRLSTIRL-ADRIIVLDKGRI 687
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
353-494 |
5.50e-15 |
|
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: 74.57 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 353 VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIGYLSQNIFssIKDETVIETFR- 420
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGLVSQDVF--LFNDTVAENIAy 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 421 DVVNVTEGEAR--------HILARFMFYGY-TVF-QKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLE 490
Cdd:cd03251 99 GRPGATREEVEeaaraanaHEFIMELPEGYdTVIgERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQ 178
|
....
gi 503253044 491 EALE 494
Cdd:cd03251 179 AALE 182
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-238 |
5.75e-15 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 73.83 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKD--------AAVGYLTQIPDYHDSTSTK 84
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKpikakerrKSIGYVMQDVDYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 EvlksafspllqmEEKMEKLEAEMGVETDPNKLQKLMGEYgELQDQYannggyeiesniekiahglniqmfihsPFSqLS 164
Cdd:cd03226 90 R------------EELLLGLKELDAGNEQAETVLKDLDLY-ALKERH---------------------------PLS-LS 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 165 GGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVNKVIDLEDGEVT 238
Cdd:cd03226 129 GGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-191 |
5.94e-15 |
|
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: 72.30 E-value: 5.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAA-----------VGYLTQipdyhdststkevlKSA 90
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtdderkslrkeIGYVFQ--------------DPQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 91 FSPLLQMEEkmekleaemgvetdpnklqkLMGEYGELQDQYANnggyEIESNIEKIAHGLNIQMF----IHSPFSQLSGG 166
Cdd:pfam00005 70 LFPRLTVRE--------------------NLRLGLLLKGLSKR----EKDARAEEALEKLGLGDLadrpVGERPGTLSGG 125
|
170 180
....*....|....*....|....*
gi 503253044 167 EKTKVGLGLMLLKQPDLLLLDEPTN 191
Cdd:pfam00005 126 QRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
337-505 |
6.18e-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: 73.85 E-value: 6.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV------KIGYLSQNiFSS 409
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLdiaarnRIGYLPEE-RGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 410 IKDETVIET---FRDVVNVTEGEARH----ILARFMFYGYTvFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD 482
Cdd:cd03269 82 YPKMKVIDQlvyLAQLKGLKKEEARRrideWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180
....*....|....*....|....*.
gi 503253044 483 IESREVLEEALEDFQG---SLLAVSH 505
Cdd:cd03269 161 PVNVELLKDVIRELARagkTVILSTH 186
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
345-505 |
7.56e-15 |
|
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: 73.55 E-value: 7.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGS---NVKIGYLSQNIF-----SSIKDE-TV 415
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILylghlPGLKPElSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 416 IETFRDVVNVTEGEARHILARFMFYGYTVFQK--VSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEAL 493
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAAVGLTGFEDlpAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
170
....*....|....*
gi 503253044 494 EDF---QGSLLAVSH 505
Cdd:TIGR01189 171 RAHlarGGIVLLTTH 185
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
335-506 |
1.11e-14 |
|
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: 73.75 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI-----LQQLFPDKGEVRI-GSNV----------- 397
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLdGKDIydldvdvlelr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 -KIGYLSQ--NIFS-SIKDetvietfrdvvNVTEG---------EARHILARFMFYGYTVFQKVS------QLSGGERMR 458
Cdd:cd03260 81 rRVGMVFQkpNPFPgSIYD-----------NVAYGlrlhgiklkEELDERVEEALRKAALWDEVKdrlhalGLSGGQQQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503253044 459 LRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG--SLLAVSHD 506
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
325-525 |
1.16e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 77.17 E-value: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 325 ESTERSGNDVIMLKDISkcFG----DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK- 398
Cdd:PRK11160 329 TSTAAADQVSLTLNNVS--FTypdqPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLnGQPIAd 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 ---------IGYLSQ--NIFS------------SIKDETVIETFRDV--VNVTEGEARhiLARFMFYGYtvfqkvSQLSG 453
Cdd:PRK11160 407 yseaalrqaISVVSQrvHLFSatlrdnlllaapNASDEALIEVLQQVglEKLLEDDKG--LNAWLGEGG------RQLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 454 GERMRLRLAQLMYQDINLLILDEPTNHLDIES-REVLEEALEDFQG-SLLAVSHDRYFLNKlFDKIYWIEAKKI 525
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNkTVLMITHRLTGLEQ-FDRICVMDNGQI 551
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
345-505 |
1.88e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 76.36 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGYLSQN--IF 407
Cdd:COG1132 351 GDRPVLKDISLTI----PPgetvALVGPSGSGKSTLVNLLLRFYDPTSGRILIdGVDIRdltleslrrqIGVVPQDtfLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 408 S-SIK-----------DETVIETFRDVvnvtegEARHILARFMfYGY-TVfqkVSQ----LSGGERMRLRLAQLMYQDIN 470
Cdd:COG1132 427 SgTIRenirygrpdatDEEVEEAAKAA------QAHEFIEALP-DGYdTV---VGErgvnLSGGQRQRIAIARALLKDPP 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 503253044 471 LLILDEPTNHLDIESREVLEEALEDF-QG-SLLAVSH 505
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLmKGrTTIVIAH 533
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-230 |
2.25e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 73.21 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 25 EIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAaVGYLTQ--IPDYhdSTSTKEVLksafspllqmeekME 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-VSYKPQyiKADY--EGTVRDLL-------------SS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 103 KLEaemGVETDPnklqklmgeygelqdQYANnggyeiesnieKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPD 182
Cdd:cd03237 85 ITK---DFYTHP---------------YFKT-----------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDAD 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503253044 183 LLLLDEPTNHLD----LMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVI 230
Cdd:cd03237 136 IYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
14-217 |
2.29e-14 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 72.01 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVgylTQIPDYHDST---STKEVLKSA 90
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA---EQRDEPHENIlylGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 91 FSPLlqmeekmEKLeaemgvetdpnklqklmgeygelqDQYANNGGYEiESNIEKIAHGLNIQMFIHSPFSQLSGGEKTK 170
Cdd:TIGR01189 88 LSAL-------ENL------------------------HFWAAIHGGA-QRTIEDALAAVGLTGFEDLPAAQLSAGQQRR 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503253044 171 VGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDY---SGTVLVISH 217
Cdd:TIGR01189 136 LALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
334-506 |
3.04e-14 |
|
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: 75.71 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCF--GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQqLFPDK----GEVRI-GSNV--------- 397
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGgrisGEVLLdGRDLlelsealrg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 -KIGYLSQNIFSSIKDETVIETFRDVV---NVTEGEAR-HILARFMFYGYTVF--QKVSQLSGGERMRLRLAQLMYQDIN 470
Cdd:COG1123 83 rRIGMVFQDPMTQLNPVTVGDQIAEALenlGLSRAEARaRVLELLEAVGLERRldRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503253044 471 LLILDEPTNHLDIESREVLEEALEDFQG----SLLAVSHD 506
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRergtTVLLITHD 202
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
22-63 |
3.47e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 3.47e-14
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:COG1134 45 VSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
22-237 |
4.03e-14 |
|
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: 71.85 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL------KKDAA-----VGYLTQipdyhDST----STKEV 86
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdgtdirQLDPAdlrrnIGYVPQ-----DVTlfygTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 87 LKSAfSPLLQMEEKMEKleAEMG-----VETDPNKLQKLMGEYGElqdqyannggyeiesniekiahglniqmfihspfs 161
Cdd:cd03245 98 ITLG-APLADDERILRA--AELAgvtdfVNKHPNGLDLQIGERGR----------------------------------- 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 162 QLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG--TVLVISHdRYFLDEVVNKVIDLEDGEV 237
Cdd:cd03245 140 GLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
364-517 |
5.40e-14 |
|
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: 74.78 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGYLSQ-----------NI--FSSIKDETVIETf 419
Cdd:COG4618 362 GVIGPSGSGKSTLARLLVGVWPPTAGSVRLdGADLSqwdreelgrhIGYLPQdvelfdgtiaeNIarFGDADPEKVVAA- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 420 rdvvnvtegeAR----H--ILaRFMFyGY-TVfqkV----SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREV 488
Cdd:COG4618 441 ----------AKlagvHemIL-RLPD-GYdTR---IgeggARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAA 505
|
170 180 190
....*....|....*....|....*....|..
gi 503253044 489 LEEALEDF---QGSLLAVSHDRYFLNKLfDKI 517
Cdd:COG4618 506 LAAAIRALkarGATVVVITHRPSLLAAV-DKL 536
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
349-526 |
5.53e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 71.53 E-value: 5.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 349 LFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQL--FPDKGEVRIgsnvkigylSQNIFSSikDETVIETFRDVVNVT 426
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDV---------PDNQFGR--EASLIDAIGRKGDFK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 427 EgeARHILARfMFYG--YTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE-SREV---LEEALEDFQGSL 500
Cdd:COG2401 114 D--AVELLNA-VGLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQtAKRVarnLQKLARRAGITL 190
|
170 180
....*....|....*....|....*.
gi 503253044 501 LAVSHDRYFLNKLFDKIYWIEAKKIH 526
Cdd:COG2401 191 VVATHHYDVIDDLQPDLLIFVGYGGV 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
334-478 |
6.21e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 74.68 E-value: 6.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLI--LQQlfPDKGEVRI-GSNVK-------- 398
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTV----RPgeihALLGENGAGKSTLMKILygLYQ--PDSGEILIdGKPVRirsprdai 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 ---IGYLSQNiFSSIKDETVIE--------TFRDVVNVteGEARHILARFM-FYGYTV--FQKVSQLSGGERMRLRLAQL 464
Cdd:COG3845 79 algIGMVHQH-FMLVPNLTVAEnivlglepTKGGRLDR--KAARARIRELSeRYGLDVdpDAKVEDLSVGEQQRVEILKA 155
|
170
....*....|....
gi 503253044 465 MYQDINLLILDEPT 478
Cdd:COG3845 156 LYRGARILILDEPT 169
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
335-505 |
7.37e-14 |
|
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: 70.71 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV--------KIG----- 400
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYqkniealrRIGaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 401 -------------YLSQNIFsSIKDETVIETFrDVVNvtEGEARHilarfmfygytvfQKVSQLSGGERMRLRLAQLMYQ 467
Cdd:cd03268 81 pgfypnltarenlRLLARLL-GIRKKRIDEVL-DVVG--LKDSAK-------------KKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503253044 468 DINLLILDEPTNHLD----IESREVLeEALEDFQGSLLAVSH 505
Cdd:cd03268 144 NPDLLILDEPTNGLDpdgiKELRELI-LSLRDQGITVLISSH 184
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
335-506 |
9.36e-14 |
|
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: 70.75 E-value: 9.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV---------KIGYLSQN 405
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlppkdrDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 406 --------IFSSI---------KDETVIETFRDVVNVTEGEarHILARfmfygytvfqKVSQLSGGERMRLRLAQLMYQD 468
Cdd:cd03301 81 yalyphmtVYDNIafglklrkvPKDEIDERVREVAELLQIE--HLLDR----------KPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503253044 469 INLLILDEPTNHLD----IESREVLEEALEDFQGSLLAVSHD 506
Cdd:cd03301 149 PKVFLMDEPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
337-527 |
1.19e-13 |
|
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: 69.86 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQqlFPD----KGEVRIGSNvkigylsqnifsSIKD 412
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKyevtEGEILFKGE------------DITD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 413 ETVIETFR-----------DVVNVTEGEarhiLARFMFYGytvfqkvsqLSGGERMRLRLAQLMYQDINLLILDEPTNHL 481
Cdd:cd03217 69 LPPEERARlgiflafqyppEIPGVKNAD----FLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503253044 482 DIESREVLEEALEDFQG---SLLAVSHDRYFLNKLF-DKIYWIEAKKIHC 527
Cdd:cd03217 136 DIDALRLVAEVINKLREegkSVLIITHYQRLLDYIKpDRVHVLYDGRIVK 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
344-506 |
1.23e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.56 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIGYLSQNIfSSIKD 412
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIqhyaskevarRIGLLAQNA-TTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 413 ETVIETfrdvvnVTEGEARH-------------ILARFM-FYGYT--VFQKVSQLSGGERMRLRLAQLMYQDINLLILDE 476
Cdd:PRK10253 96 ITVQEL------VARGRYPHqplftrwrkedeeAVTKAMqATGIThlADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190
....*....|....*....|....*....|....
gi 503253044 477 PTNHLDIESREVLEEALEDF---QG-SLLAVSHD 506
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELnreKGyTLAAVLHD 203
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
365-511 |
1.26e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLIlQQLFPDKGEVRIGSN-----------VKIGYLSQNI---FS---------SIKDETVIETFRD 421
Cdd:PRK03695 27 LVGPNGAGKSTLLARM-AGLLPGSGSIQFAGQpleawsaaelaRHRAYLSQQQtppFAmpvfqyltlHQPDKTRTEAVAS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 422 VVNvtegearhILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQ---DIN----LLILDEPTNHLDIESREVLEEALE 494
Cdd:PRK03695 106 ALN--------EVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpDINpagqLLLLDEPMNSLDVAQQAALDRLLS 177
|
170 180
....*....|....*....|
gi 503253044 495 DFQGSLLAV---SHDryfLN 511
Cdd:PRK03695 178 ELCQQGIAVvmsSHD---LN 194
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
345-505 |
1.31e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 69.90 E-value: 1.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVKIG-------YLS-QNifsSIKDE-T 414
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdGGDIDDPdvaeachYLGhRN---AMKPAlT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 415 VIE--TF-RDVVNVTEGEARHILARFMF-------YGYtvfqkvsqLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE 484
Cdd:PRK13539 90 VAEnlEFwAAFLGGEELDIAAALEAVGLaplahlpFGY--------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
170 180
....*....|....*....|....
gi 503253044 485 SREVLEEALEDFQ---GSLLAVSH 505
Cdd:PRK13539 162 AVALFAELIRAHLaqgGIVIAATH 185
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-237 |
1.35e-13 |
|
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: 70.24 E-value: 1.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL-KKDAA--------VGYLTQipD 76
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVTgvpperrnIGMVFQ--D 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 77 Y----HDStstkeVLKSAFSPLlqmeekmekleaemgvetdpnKLQKLMGEygelqdqyannggyEIESNIEKIAHGLNI 152
Cdd:cd03259 81 YalfpHLT-----VAENIAFGL---------------------KLRGVPKA--------------EIRARVRELLELVGL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 153 QMFIHSPFSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSG----TVLVISHD 218
Cdd:cd03259 121 EGLLNRYPHELSGGQQQRVALAralarepsllLL----------DEPLSALDAKLREELREELKELQRelgiTTIYVTHD 190
|
250 260
....*....|....*....|..
gi 503253044 219 ryfLDEVV---NKVIDLEDGEV 237
Cdd:cd03259 191 ---QEEALalaDRIAVMNEGRI 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
332-529 |
1.42e-13 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.88 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 332 NDVIMLKDISKCF----------------------GDKLLFEGVNMHItYQNRA-AIIGENGTGKSTLLKLILQQLFPDK 388
Cdd:COG1134 2 SSMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEV-ERGESvGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 389 GEVRIgsNVKIGYL-------------SQNIFSS-----IKDETVIETFRDVVNVTE-GEARHilarfmfygytvfQKVS 449
Cdd:COG1134 81 GRVEV--NGRVSALlelgagfhpeltgRENIYLNgrllgLSRKEIDEKFDEIVEFAElGDFID-------------QPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 450 QLSGGERMRLRLAqLMYQ---DInlLILDEPTNHLDIESREVLEEALEDFQ---GSLLAVSHDRYFLNKLFDKIYWIEAK 523
Cdd:COG1134 146 TYSSGMRARLAFA-VATAvdpDI--LLVDEVLAVGDAAFQKKCLARIRELResgRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
....*.
gi 503253044 524 KIHCFE 529
Cdd:COG1134 223 RLVMDG 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
335-490 |
1.85e-13 |
|
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: 69.74 E-value: 1.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCF-GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV------KIGYLSQNI 406
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 407 ------FSSIKDETVIETFRDVVNVTEGEARHILARFMfygyTVFQKV----------SQLSGGERMRLRLAQLMYQDIN 470
Cdd:cd03292 81 gvvfqdFRLLPDRNVYENVAFALEVTGVPPREIRKRVP----AALELVglshkhralpAELSGGEQQRVAIARAIVNSPT 156
|
170 180
....*....|....*....|.
gi 503253044 471 LLILDEPTNHLDIE-SREVLE 490
Cdd:cd03292 157 ILIADEPTGNLDPDtTWEIMN 177
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
6-236 |
2.21e-13 |
|
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: 68.75 E-value: 2.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI-------------HLKKDAAVGYLT 72
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSIlidgedltdledeLPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 73 QipdyhdststkevlksafspllqmeekmekleaemgvetDPNKLQKLmgeygelqdqyannggyeieSNIEKIAHGlni 152
Cdd:cd03229 83 Q---------------------------------------DFALFPHL--------------------TVLENIALG--- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 153 qmfihspfsqLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDY---SG-TVLVISHD 218
Cdd:cd03229 101 ----------LSGGQQQRVALAralamdpdvlLL----------DEPTSALDPITRREVRALLKSLqaqLGiTVVLVTHD 160
|
250
....*....|....*...
gi 503253044 219 RYFLDEVVNKVIDLEDGE 236
Cdd:cd03229 161 LDEAARLADRVVVLRDGK 178
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
335-506 |
2.41e-13 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 70.11 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNVKIGYLSQNIfsSI 410
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDgldvATTPSRELAKRL--AI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 411 -KDETVIE---TFRDVV----------NVTEGEARHI---LARFmfyGYTVFQK--VSQLSGGERMRLRLAQLMYQDINL 471
Cdd:COG4604 80 lRQENHINsrlTVRELVafgrfpyskgRLTAEDREIIdeaIAYL---DLEDLADryLDELSGGQRQRAFIAMVLAQDTDY 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 503253044 472 LILDEPTNHLDIE-SRE---VLEEALEDFQGSLLAVSHD 506
Cdd:COG4604 157 VLLDEPLNNLDMKhSVQmmkLLRRLADELGKTVVIVLHD 195
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-237 |
3.22e-13 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 71.33 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL-KKDAA---------VGYLTQi 74
Cdd:COG1118 4 EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLnGRDLFtnlpprerrVGFVFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 75 pDY----HDStstkeV-------LKSAFSPLLQMEEKMEKLEAEMGVEtdpnklqklmgeygELQDQYannggyeiesni 143
Cdd:COG1118 83 -HYalfpHMT-----VaeniafgLRVRPPSKAEIRARVEELLELVQLE--------------GLADRY------------ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 144 ekiahglniqmfihsPfSQLSGGEKTKVGLG---------LMllkqpdlllLDEPTNHLD------LMavEWLGSFLRDY 208
Cdd:COG1118 131 ---------------P-SQLSGGQRQRVALAralavepevLL---------LDEPFGALDakvrkeLR--RWLRRLHDEL 183
|
250 260 270
....*....|....*....|....*....|..
gi 503253044 209 SGTVLVISHDRyflDEVV---NKVIDLEDGEV 237
Cdd:COG1118 184 GGTTVFVTHDQ---EEALelaDRVVVMNQGRI 212
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-238 |
3.25e-13 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 69.83 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIicSVNKVAKMYG----GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL---------KKD-- 65
Cdd:COG1124 1 ML--EVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFdgrpvtrrrRKAfr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 66 AAVGYLTQipDYHdststkevlkSAFSPLLQMEEKMEKLEAEMGVETDPNKLQKLMGEYGeLQDQYANNggyeiesniek 145
Cdd:COG1124 79 RRVQMVFQ--DPY----------ASLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVG-LPPSFLDR----------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 146 iahglniqmFIHspfsQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLM----AVEWLGSFLRDYSGTVLVISHDRYF 221
Cdd:COG1124 135 ---------YPH----QLSGGQRQRVAIARALILEPELLLLDEPTSALDVSvqaeILNLLKDLREERGLTYLFVSHDLAV 201
|
250
....*....|....*..
gi 503253044 222 LDEVVNKVIDLEDGEVT 238
Cdd:COG1124 202 VAHLCDRVAVMQNGRIV 218
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-230 |
3.95e-13 |
|
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: 3.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 25 EIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHlkKDAAVGYLTQ--IPDYHDstSTKEVLKSAFSPllQMEEKME 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQyiSPDYDG--TVEEFLRSANTD--DFGSSYY 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 103 KLEaemgvetdpnklqklmgeygelqdqyannggyeiesniekIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPD 182
Cdd:COG1245 436 KTE----------------------------------------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDAD 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503253044 183 LLLLDEPTNHLD----LMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVI 230
Cdd:COG1245 476 LYLLDEPSAHLDveqrLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLM 527
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
334-495 |
4.51e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 69.73 E-value: 4.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCF----GDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLILQQLFPDKGEVRI------GSNVKI 399
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTV----AAgefvALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 400 GYLSQNifssikD-----ETVIEtfrdvvNVTEG-------------EARHILARFmfyGYTVFQK--VSQLSGGERMRL 459
Cdd:COG1116 83 GVVFQE------PallpwLTVLD------NVALGlelrgvpkaerreRARELLELV---GLAGFEDayPHQLSGGMRQRV 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 503253044 460 RLAQLMYQDINLLILDEPTNHLDIESREVLEEALED 495
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLR 183
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-62 |
4.75e-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: 70.90 E-value: 4.75e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:COG3842 7 ELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL 64
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
348-525 |
5.10e-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: 68.29 E-value: 5.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 348 LLFEGVNMH----ITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSN-----------VKIGYLSQNIFSSIKD 412
Cdd:cd03298 8 FSYGEQPMHfdltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVdvtaappadrpVSMLFQENNLFAHLTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 413 ETVIETFRDV---VNVTEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVL 489
Cdd:cd03298 88 EQNVGLGLSPglkLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503253044 490 EEALEDF----QGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:cd03298 168 LDLVLDLhaetKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
5-62 |
5.22e-13 |
|
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: 69.00 E-value: 5.22e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 5 SVNKVAKMYGGNA----IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:COG4181 10 ELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRL 71
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
335-506 |
5.75e-13 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 68.63 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLL-FegvNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV--------KIGYLSQ 404
Cdd:COG3840 2 LRLDDLTYRYGDFPLrF---DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDLtalppaerPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 --NIFSSIkdeTVIET----FRDVVNVTEGE---ARHILARFMFYGYTVFqKVSQLSGGERMRLRLAQLMYQDINLLILD 475
Cdd:COG3840 79 enNLFPHL---TVAQNiglgLRPGLKLTAEQraqVEQALERVGLAGLLDR-LPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190
....*....|....*....|....*....|....*
gi 503253044 476 EPTNHLDI----ESREVLEEALEDFQGSLLAVSHD 506
Cdd:COG3840 155 EPFSALDPalrqEMLDLVDELCRERGLTVLMVTHD 189
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-62 |
6.13e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 70.49 E-value: 6.13e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:COG3839 5 ELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI 62
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
352-494 |
6.61e-13 |
|
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: 68.41 E-value: 6.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 352 GVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGYLSQN--IFS-SIKDETVI- 416
Cdd:cd03254 21 DINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdGIDIRdisrkslrsmIGVVLQDtfLFSgTIMENIRLg 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 417 --ETFRDVVNVTEGEAR-HILARFMFYGY--TVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEE 491
Cdd:cd03254 101 rpNATDEEVIEAAKEAGaHDFIMKLPNGYdtVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQE 180
|
...
gi 503253044 492 ALE 494
Cdd:cd03254 181 ALE 183
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-237 |
7.73e-13 |
|
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: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 8 KVAKMYGGN-AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKdaavgylTQIPDYHDStstkev 86
Cdd:cd03292 5 NVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG-------QDVSDLRGR------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 87 lksafspllqmeeKMEKLEAEMGVETDPNKLQKLMGEYGE--LQDQYANNGGYEIESNIEKIAHGLNIQMFIHSPFSQLS 164
Cdd:cd03292 72 -------------AIPYLRRKIGVVFQDFRLLPDRNVYENvaFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELS 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 165 GGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:cd03292 139 GGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-60 |
9.10e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 67.94 E-value: 9.10e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV 79
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
5-240 |
9.41e-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: 67.69 E-value: 9.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKkdaavGYLTQIPDYHdststk 84
Cdd:cd03269 2 EVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-----GKPLDIAARN------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 evlKSAFSPllqmEEKmeKLEAEMGVETDPNKLQKLMGeygeLQDQYANNggyEIESNIEKiahgLNIQMFIHSPFSQLS 164
Cdd:cd03269 71 ---RIGYLP----EER--GLYPKMKVIDQLVYLAQLKG----LKKEEARR---RIDEWLER----LELSEYANKRVEELS 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 165 GGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVNKVIDLEDGEVTTY 240
Cdd:cd03269 131 KGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-238 |
1.11e-12 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 68.13 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIhlkkdaavgyltqipdyhdststkEVLksAFSPLlqmeEKM 101
Cdd:cd03267 40 ISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEV------------------------RVA--GLVPW----KRR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 102 EKLEAEMGVetdpnklqkLMGEYGEL------QDQYA-NNGGYEIE-----SNIEKIAHGLNIQMFIHSPFSQLSGGEKT 169
Cdd:cd03267 90 KKFLRRIGV---------VFGQKTQLwwdlpvIDSFYlLAAIYDLPparfkKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 170 KVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYS----GTVLVISHDRYFLDEVVNKVIDLEDGEVT 238
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNrergTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
5-226 |
1.31e-12 |
|
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: 67.50 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNA----IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL------KKDAAVGYLTQi 74
Cdd:cd03293 2 EVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 75 pdyHDS-----TSTKEVlksAFSPLLQMEEKMEKLEaemgvetdpnKLQKLMGEYGeLQDqYANnggyeiesniekiahg 149
Cdd:cd03293 81 ---QDAllpwlTVLDNV---ALGLELQGVPKAEARE----------RAEELLELVG-LSG-FEN---------------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 150 lniqmfiHSPfSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLD-LMAV---EWLGSFLRDYSGTVLVI 215
Cdd:cd03293 127 -------AYP-HQLSGGMRQRVALAralavdpdvlLL----------DEPFSALDaLTREqlqEELLDIWRETGKTVLLV 188
|
250
....*....|.
gi 503253044 216 SHDryfLDEVV 226
Cdd:cd03293 189 THD---IDEAV 196
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
352-497 |
1.32e-12 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 70.52 E-value: 1.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 352 GVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGYLSQNIFssIKDETVIETFR 420
Cdd:TIGR02203 350 SISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLdGHDLAdytlaslrrqVALVSQDVV--LFNDTIANNIA 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 421 --DVVNVTEGEARHILArfMFYG------------YTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR 486
Cdd:TIGR02203 428 ygRTEQADRAEIERALA--AAYAqdfvdklplgldTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESE 505
|
170
....*....|.
gi 503253044 487 EVLEEALEDFQ 497
Cdd:TIGR02203 506 RLVQAALERLM 516
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
335-525 |
1.58e-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: 67.39 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV---------KIGYLSQ 404
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 NIfsSIKDETV----IETFRDVVNVTEGEARHILARFM-FYGYTVF--QKVSQLSGGERMRLRLAQLMYQDINLLILDEP 477
Cdd:cd03265 81 DL--SVDDELTgwenLYIHARLYGVPGAERRERIDELLdFVGLLEAadRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503253044 478 TNHLDIESR----EVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:cd03265 159 TIGLDPQTRahvwEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
344-508 |
1.75e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 67.73 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV-----------KIGYLSQNIFS--SI 410
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPismlssrqlarRLALLPQHHLTpeGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 411 KDETVIETFRDVVNVTEG----EARHILARFMFYGYTVF---QKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDI 483
Cdd:PRK11231 92 TVRELVAYGRSPWLSLWGrlsaEDNARVNQAMEQTRINHladRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190
....*....|....*....|....*....|....
gi 503253044 484 eSREV----LEEALEDFQGSLLAVSHD-----RY 508
Cdd:PRK11231 172 -NHQVelmrLMRELNTQGKTVVTVLHDlnqasRY 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
335-530 |
1.78e-12 |
|
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: 67.01 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDK----LLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV---------KIG 400
Cdd:cd03266 2 ITADALTKRFRDVkktvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVdGFDVvkepaearrRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 401 YLSQN--IFSSIKDETVIETFRDV--VNVTEGEAR-HILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILD 475
Cdd:cd03266 82 FVSDStgLYDRLTARENLEYFAGLygLKGDELTARlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 476 EPTNHLDIESREVLEEALE---DFQGSLLAVSHDRYFLNKLFDKIYWIEAKKIHcFEG 530
Cdd:cd03266 162 EPTTGLDVMATRALREFIRqlrALGKCILFSTHIMQEVERLCDRVVVLHRGRVV-YEG 218
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-232 |
1.83e-12 |
|
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: 66.75 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDaavGYLTQIPDYHDS---TSTKEVLKSA 90
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG---PLDFQRDSIARGllyLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 91 FSPLlqmeEKMEKLEAEMGVETDPNKLQKlmgeygelqdqyANNGGYEiesniekiahglniqmfiHSPFSQLSGGEKTK 170
Cdd:cd03231 88 LSVL----ENLRFWHADHSDEQVEEALAR------------VGLNGFE------------------DRPVAQLSAGQQRR 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 171 VGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHDRYFLDEVVNKVIDL 232
Cdd:cd03231 134 VALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHCargGMVVLTTHQDLGLSEAGARELDL 198
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1-194 |
1.85e-12 |
|
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: 67.14 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIICSVNKVAKmYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHlkkdaavgyltqIPDYHDS 80
Cdd:cd03263 1 LQIRNLTKTYK-KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY------------INGYSIR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 81 TSTKEVLKS--------AFSPLLQMEEKMEKleaemgvetdpnklqklmgeYGELQdqyanngGY---EIESNIEKIAHG 149
Cdd:cd03263 68 TDRKAARQSlgycpqfdALFDELTVREHLRF--------------------YARLK-------GLpksEIKEEVELLLRV 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503253044 150 LNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLD 194
Cdd:cd03263 121 LGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
337-506 |
1.92e-12 |
|
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: 67.36 E-value: 1.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLfEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV--------KIGYLSQN-- 405
Cdd:cd03299 3 VENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQNya 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 406 ------IFSSI------KDETVIETFRDVVNVTEG-EARHILARfmfygytvfqKVSQLSGGERMRLRLAQLMYQDINLL 472
Cdd:cd03299 82 lfphmtVYKNIayglkkRKVDKKEIERKVLEIAEMlGIDHLLNR----------KPETLSGGEQQRVAIARALVVNPKIL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 503253044 473 ILDEPTNHLDIESREVLEEAL----EDFQGSLLAVSHD 506
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELkkirKEFGVTVLHVTHD 189
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
5-238 |
2.02e-12 |
|
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: 65.53 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKkdaavgyltqipdyhdststk 84
Cdd:cd03216 2 ELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 evlksafspllqmeekmekleaemGVEtdpnklqklmgeygelqdqyannggYEIESNIEKIAHGlnIQMfIHspfsQLS 164
Cdd:cd03216 61 ------------------------GKE-------------------------VSFASPRDARRAG--IAM-VY----QLS 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 165 GGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDY--SG-TVLVISHdryFLDEVVN---KVIDLEDGEVT 238
Cdd:cd03216 85 VGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLraQGvAVIFISH---RLDEVFEiadRVTVLRDGRVV 161
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
364-507 |
2.33e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 69.99 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLiLQQLF-PDKGEVRI-GSN---VKIGYLSQNI---FS-------SIKDETVI----ETFRDVVN 424
Cdd:PRK13657 365 AIVGPTGAGKSTLINL-LQRVFdPQSGRILIdGTDirtVTRASLRRNIavvFQdaglfnrSIEDNIRVgrpdATDEEMRA 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 425 VTEGEARH--ILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEdfqgsllA 502
Cdd:PRK13657 444 AAERAQAHdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALD-------E 516
|
....*
gi 503253044 503 VSHDR 507
Cdd:PRK13657 517 LMKGR 521
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
14-62 |
2.43e-12 |
|
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: 65.48 E-value: 2.43e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI 61
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
346-496 |
2.69e-12 |
|
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: 66.79 E-value: 2.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------IGYLSQ--NIFS-SIK 411
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdGVDIRdlnlrwlrsqIGLVSQepVLFDgTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 412 -----------DETVIETFRDVvnvtegEARHILARFMfYGYT--VFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPT 478
Cdd:cd03249 95 enirygkpdatDEEVEEAAKKA------NIHDFIMSLP-DGYDtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEAT 167
|
170
....*....|....*...
gi 503253044 479 NHLDIESREVLEEALEDF 496
Cdd:cd03249 168 SALDAESEKLVQEALDRA 185
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
5-237 |
2.84e-12 |
|
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: 66.36 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNA----IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTG-------DIHLKKDAA------ 67
Cdd:cd03255 2 ELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGevrvdgtDISKLSEKElaafrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 68 --VGYLTQipDYHdststkevlksafspLLQMeekmekLEAEMGVEtdpnklqklmgeygeLQDQYANNGGYEIESNIEK 145
Cdd:cd03255 82 rhIGFVFQ--SFN---------------LLPD------LTALENVE---------------LPLLLAGVPKKERRERAEE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 146 IAHGLNIQMFIHSPFSQLSGGEKTKVGL--GLMLLKQPDLllLDEPTNHLD----LMAVEWLGSFLRDYSGTVLVISHDR 219
Cdd:cd03255 124 LLERVGLGDRLNHYPSELSGGQQQRVAIarALANDPKIIL--ADEPTGNLDsetgKEVMELLRELNKEAGTTIVVVTHDP 201
|
250
....*....|....*...
gi 503253044 220 yFLDEVVNKVIDLEDGEV 237
Cdd:cd03255 202 -ELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-62 |
4.48e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.84 E-value: 4.48e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 1 MIicSVNKVAKMY-GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:COG2884 1 MI--RFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV 61
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
365-511 |
5.25e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 66.02 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLkLILQQLFPDKGEVRI-GSNVKI----------GYLSQN--------IF--------SSIKDETVIE 417
Cdd:COG4138 27 LIGPNGAGKSTLL-ARMAGLLPGQGEILLnGRPLSDwsaaelarhrAYLSQQqsppfampVFqylalhqpAGASSEAVEQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 418 TFRDVVnvtegEARHI---LARfmfygytvfqKVSQLSGGERMRLRLAQLMYQ---DIN----LLILDEPTNHLDIESRE 487
Cdd:COG4138 106 LLAQLA-----EALGLedkLSR----------PLTQLSGGEWQRVRLAAVLLQvwpTINpegqLLLLDEPMNSLDVAQQA 170
|
170 180
....*....|....*....|....*..
gi 503253044 488 VLEEALEDF---QGSLLAVSHDryfLN 511
Cdd:COG4138 171 ALDRLLRELcqqGITVVMSSHD---LN 194
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
348-495 |
5.29e-12 |
|
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: 65.97 E-value: 5.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 348 LLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSN-----------VKIGYLSQN--IFS-SIKDE 413
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHdlaladpawlrRQVGVVLQEnvLFNrSIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 414 TVIE----TFRDVVNVTEGEARHILARFMFYGY--TVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESRE 487
Cdd:cd03252 96 IALAdpgmSMERVIEAAKLAGAHDFISELPEGYdtIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEH 175
|
....*...
gi 503253044 488 VLEEALED 495
Cdd:cd03252 176 AIMRNMHD 183
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
9-218 |
7.10e-12 |
|
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: 64.97 E-value: 7.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 9 VAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-KDaavgyLTQIPDYHDSTSTkeVL 87
Cdd:cd03301 6 VTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgRD-----VTDLPPKDRDIAM--VF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 88 KS-AFSPLLQMEEKMEKleaemgvetdPNKLQKLMGEygelqdqyannggyEIESNIEKIAHGLNIQMFIHSPFSQLSGG 166
Cdd:cd03301 79 QNyALYPHMTVYDNIAF----------GLKLRKVPKD--------------EIDERVREVAELLQIEHLLDRKPKQLSGG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 167 EKTKVGLGLMLLKQPDLLLLDEPTNHLDL-----MAVEwLGSFLRDYSGTVLVISHD 218
Cdd:cd03301 135 QRQRVALGRAIVREPKVFLMDEPLSNLDAklrvqMRAE-LKRLQQRLGTTTIYVTHD 190
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
346-517 |
8.67e-12 |
|
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: 8.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKlILQQLFP-DKGEVRIGSNVKIGYLSQnifssiKDETVIETFRDVVN 424
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFR-ALAGLWPwGSGRIGMPEGEDLLFLPQ------RPYLPLGTLREQLI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 425 vtegearhilarfmfygYTvFQKVsqLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSLLAVS 504
Cdd:cd03223 86 -----------------YP-WDDV--LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVG 145
|
170
....*....|...
gi 503253044 505 HdRYFLNKLFDKI 517
Cdd:cd03223 146 H-RPSLWKFHDRV 157
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
335-506 |
1.30e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 65.05 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRIG----SNVK-----IGYLS 403
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIagLER--PDSGTILFGgedaTDVPvqernVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 404 QNiFSSIKDETVIEtfrdvvNVTEG-EARHILARFMfyGYTVFQKV-----------------SQLSGGERMRLRLAQLM 465
Cdd:cd03296 81 QH-YALFRHMTVFD------NVAFGlRVKPRSERPP--EAEIRAKVhellklvqldwladrypAQLSGGQRQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503253044 466 YQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHD 506
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHD 196
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
6-237 |
1.41e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 64.67 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-KDAA--------VGYLTQipD 76
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgEDATdvpvqernVGFVFQ--H 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 77 Y----HdSTSTKEVlksAFSplLQMEEKMEKL-EAEMGVETdpNKLQKLMGEYGeLQDQYANnggyeiesniekiahgln 151
Cdd:cd03296 83 YalfrH-MTVFDNV---AFG--LRVKPRSERPpEAEIRAKV--HELLKLVQLDW-LADRYPA------------------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 152 iqmfihspfsQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLR----DYSGTVLVISHDRYFLDEVVN 227
Cdd:cd03296 136 ----------QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRrlhdELHVTTVFVTHDQEEALEVAD 205
|
250
....*....|
gi 503253044 228 KVIDLEDGEV 237
Cdd:cd03296 206 RVVVMNKGRI 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-230 |
1.49e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.14 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 25 EIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIhlKKDAAVGYLTQI--PDYHDSTStkEVLKSAFSpllqmeekme 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYikPDYDGTVE--DLLRSITD---------- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 103 kleaemgvetdpnklqKLMGEYgelqdqyannggYEIEsniekIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPD 182
Cdd:PRK13409 427 ----------------DLGSSY------------YKSE-----IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDAD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503253044 183 LLLLDEPTNHLD----LMAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVI 230
Cdd:PRK13409 474 LYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLM 525
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
335-490 |
1.71e-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: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRI-GSNV------------KI 399
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlLEE--PDSGTIIIdGLKLtddkkninelrqKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 400 GYLSQNiFSSIKDETVIEtfrdvvNVTEG--------------EARHILARFmfyGYTVFQKV--SQLSGGERMRLRLAQ 463
Cdd:cd03262 79 GMVFQQ-FNLFPHLTVLE------NITLApikvkgmskaeaeeRALELLEKV---GLADKADAypAQLSGGQQQRVAIAR 148
|
170 180
....*....|....*....|....*...
gi 503253044 464 LMYQDINLLILDEPTNHLDIE-SREVLE 490
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPElVGEVLD 176
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
349-505 |
1.73e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.22 E-value: 1.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 349 LFEGVNMHITYQ----NRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSN----------VKIGYLSQNIFSSIKDE 413
Cdd:PRK10771 10 LYHHLPMRFDLTvergERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDhtttppsrrpVSMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 414 TVIETFRD---VVNVTEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD----IESR 486
Cdd:PRK10771 90 QNIGLGLNpglKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEML 169
|
170
....*....|....*....
gi 503253044 487 EVLEEALEDFQGSLLAVSH 505
Cdd:PRK10771 170 TLVSQVCQERQLTLLMVSH 188
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-62 |
2.01e-11 |
|
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: 64.23 E-value: 2.01e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 1 MIicSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:COG1127 5 MI--EVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV 64
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-238 |
2.06e-11 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 65.90 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 21 EISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK----KDAAVGYLTQIPdyhdststkevlKSAFSPLLQ 96
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlFDSRKGIFLPPE------------KRRIGYVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 97 MEekmeKLEAEMGVEtdpnklQKLmgEYGelqdqYANNGGYEIESNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLM 176
Cdd:TIGR02142 83 EA----RLFPHLSVR------GNL--RYG-----MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 177 LLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGT----VLVISHDryfLDEV---VNKVIDLEDGEVT 238
Cdd:TIGR02142 146 LLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEfgipILYVSHS---LQEVlrlADRVVVLEDGRVA 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
5-63 |
2.06e-11 |
|
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: 66.47 E-value: 2.06e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 5 SVNKVAKMYGGNA-----IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:COG1123 262 EVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFD 325
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
364-506 |
2.14e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.81 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV-----------KIGYLSQNIFSSikdETVieTFRDVVNVTEGEARH 432
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPleswsskafarKVAYLPQQLPAA---EGM--TVRELVAIGRYPWHG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 433 ILARF------------MFYGYTVFQK--VSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR-EVLE--EALED 495
Cdd:PRK10575 116 ALGRFgaadrekveeaiSLVGLKPLAHrlVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQvDVLAlvHRLSQ 195
|
170
....*....|..
gi 503253044 496 FQG-SLLAVSHD 506
Cdd:PRK10575 196 ERGlTVIAVLHD 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
14-233 |
2.43e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 63.28 E-value: 2.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-KDAAvgylTQIPDYHDststkEVL----- 87
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgEPIR----RQRDEYHQ-----DLLylghq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 88 ---KSAFSPLlqmeekmEKLEAemgvetdpnkLQKLMGEYGElqdqyannggyeiesniEKIAHGL---NIQMFIHSPFS 161
Cdd:PRK13538 83 pgiKTELTAL-------ENLRF----------YQRLHGPGDD-----------------EALWEALaqvGLAGFEDVPVR 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 162 QLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHDRYFLDEVVNKVIDLE 233
Cdd:PRK13538 129 QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTHQDLPVASDKVRKLRLG 203
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
334-490 |
2.61e-11 |
|
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: 63.75 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDK----LLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRI-GSNV--------- 397
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCIngLER--PTSGSVLVdGTDLtllsgkelr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 ----KIGYLSQ--NIFSSikdETVIEtfrdvvNVT-------------EGEARHILArfmFYGYTVFQKV--SQLSGGER 456
Cdd:cd03258 79 karrRIGMIFQhfNLLSS---RTVFE------NVAlpleiagvpkaeiEERVLELLE---LVGLEDKADAypAQLSGGQK 146
|
170 180 190
....*....|....*....|....*....|....*
gi 503253044 457 MRLRLAQLMYQDINLLILDEPTNHLDIES-REVLE 490
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETtQSILA 181
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
346-505 |
2.62e-11 |
|
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: 63.64 E-value: 2.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNVKIGYLSQNIfSSIKDETVI--ETF 419
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDgkpiSQYEHKYLHSKV-SLVGQEPVLfaRSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 420 RD-------------VVNVTEGEARHILARFMFYGYT--VFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE 484
Cdd:cd03248 105 QDniayglqscsfecVKEAAQKAHAHSFISELASGYDteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180
....*....|....*....|...
gi 503253044 485 SREVLEEALEDF--QGSLLAVSH 505
Cdd:cd03248 185 SEQQVQQALYDWpeRRTVLVIAH 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
14-233 |
2.63e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 63.35 E-value: 2.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAvgyltqipdyhDSTSTKEVL-----K 88
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-----------DDPDVAEAChylghR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 89 SAFSPLLQMEEKMekleaemgvetdpnklqklmgeygELQDQYANNGGYEIESNIEkiahGLNIQMFIHSPFSQLSGGEK 168
Cdd:PRK13539 82 NAMKPALTVAENL------------------------EFWAAFLGGEELDIAAALE----AVGLAPLAHLPFGYLSAGQK 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 169 TKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHDRYFLDEvvNKVIDLE 233
Cdd:PRK13539 134 RRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLaqgGIVIAATHIPLGLPG--ARELDLG 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
337-518 |
2.66e-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: 64.00 E-value: 2.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK-----------IGYLSQ 404
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFdGEDITglppheiarlgIGRTFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 N--IFSSIkdeTVIE-----------------TFRDVVNVTEGEARHILARFMFYGYtVFQKVSQLSGGERMRLRLAQLM 465
Cdd:cd03219 83 IprLFPEL---TVLEnvmvaaqartgsglllaRARREEREARERAEELLERVGLADL-ADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 466 YQDINLLILDEPTNHLDIESREVLEEALEDF--QG-SLLAVSHDRYFLNKLFDKIY 518
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELreRGiTVLLVEHDMDVVMSLADRVT 214
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
13-62 |
2.69e-11 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 64.41 E-value: 2.69e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK13548 12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRL 61
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
364-518 |
2.89e-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: 62.95 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFP--DKGEVRI-GSNVK-------IGYLSQnifssikDETVIETFrdvvnvTEGEARHI 433
Cdd:cd03213 39 AIMGPSGAGKSTLLNALAGRRTGlgVSGEVLInGRPLDkrsfrkiIGYVPQ-------DDILHPTL------TVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 434 LArfmfygytvfqKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD-IESREVLE--EALEDFQGSLLAVSHD-RYF 509
Cdd:cd03213 106 AA-----------KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsSSALQVMSllRRLADTGRTIICSIHQpSSE 174
|
....*....
gi 503253044 510 LNKLFDKIY 518
Cdd:cd03213 175 IFELFDKLL 183
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-238 |
2.96e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.63 E-value: 2.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAvgyltqipdyhDSTSTK 84
Cdd:PRK09536 5 DVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-----------EALSAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 EVLKS-AFSP---LLQMEEKMEKLeAEMGVETDPNKLqklmgeygelqDQYANNGGYEIESNIEKIahglNIQMFIHSPF 160
Cdd:PRK09536 74 AASRRvASVPqdtSLSFEFDVRQV-VEMGRTPHRSRF-----------DTWTETDRAAVERAMERT----GVAQFADRPV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 161 SQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDL-MAVEWLGSF--LRDYSGTVLVISHD-----RYfLDEVVNkvidL 232
Cdd:PRK09536 138 TSLSGGERQRVLLARALAQATPVLLLDEPTASLDInHQVRTLELVrrLVDDGKTAVAAIHDldlaaRY-CDELVL----L 212
|
....*.
gi 503253044 233 EDGEVT 238
Cdd:PRK09536 213 ADGRVR 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
345-529 |
3.39e-11 |
|
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: 63.32 E-value: 3.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVK----IGY-----LS--QNI-----FS 408
Cdd:cd03220 33 GEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSsllgLGGgfnpeLTgrENIylngrLL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 409 SIKDETVIETFRDVVNVTE-GEARHilarfmfygytvfQKVSQLSGGERMRLRLAQLMYQDINLLILDEPT----NHLDI 483
Cdd:cd03220 113 GLSRKEIDEKIDEIIEFSElGDFID-------------LPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503253044 484 ESREVLEEALEDfQGSLLAVSHDRYFLNKLFDKIYWIEAKKIHCFE 529
Cdd:cd03220 180 KCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
14-238 |
3.47e-11 |
|
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: 65.93 E-value: 3.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI--------HLKKDA---AVGYLTQIPdY--HDS 80
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsDLDPASwrrQIAWVPQNP-YlfAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 81 ----------TSTKEvlksafspllQMEEKMEKLEAEMGVETDPNKLQKLMGEYGelqdqyannggyeiesniekiahgl 150
Cdd:COG4988 427 irenlrlgrpDASDE----------ELEAALEAAGLDEFVAALPDGLDTPLGEGG------------------------- 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 151 niqmfihspfSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSG--TVLVISHD 218
Cdd:COG4988 472 ----------RGLSGGQAQRLALArallrdapllLL----------DEPTAHLDAETEAEILQALRRLAKgrTVILITHR 531
|
250 260
....*....|....*....|
gi 503253044 219 RYFLDEvVNKVIDLEDGEVT 238
Cdd:COG4988 532 LALLAQ-ADRILVLDDGRIV 550
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-225 |
4.26e-11 |
|
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: 62.70 E-value: 4.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 21 EISFEIKEkERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL---------KK------DAAVGYLTQipdyhdststke 85
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsrKKinlppqQRKIGLVFQ------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 86 vlKSAFSPLLQMEEKMEkleaeMGVETDPNKlqklmgeygELQDQyannggyeiesnIEKIAHGLNIQMFIHSPFSQLSG 165
Cdd:cd03297 83 --QYALFPHLNVRENLA-----FGLKRKRNR---------EDRIS------------VDELLDLLGLDHLLNRYPAQLSG 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 166 GEKTKVGLGLMLLKQPDLLLLDEPTNHLD----LMAVEWLGSFLRDYSGTVLVISHDryfLDEV 225
Cdd:cd03297 135 GEKQRVALARALAAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTHD---LSEA 195
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
364-510 |
4.34e-11 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.24 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRIGSnvkigylsqnifssikdetvietfrdvvnvteGEARHILARFMFYGYT 443
Cdd:smart00382 6 LIVGPPGSGKTTLARALARELGPPGGGVIYID--------------------------------GEDILEEVLDQLLLII 53
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 444 VFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSLLAVSHDRYFL 510
Cdd:smart00382 54 VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI 120
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
5-238 |
4.86e-11 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 62.75 E-value: 4.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNA----IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-------KDAA------ 67
Cdd:COG1136 6 ELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisslSERElarlrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 68 --VGYLTQipDYH--DSTSTKE-VlksAFSPLLqmeekmekleAEMGVETDPNKLQKLMGEYGelqdqyannggyeiesn 142
Cdd:COG1136 86 rhIGFVFQ--FFNllPELTALEnV---ALPLLL----------AGVSRKERRERARELLERVG----------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 143 IEKIAHglniqmfiHSPfSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLD------LMAVewLGSFLR 206
Cdd:COG1136 134 LGDRLD--------HRP-SQLSGGQQQRVAIAralvnrpkliLA----------DEPTGNLDsktgeeVLEL--LRELNR 192
|
250 260 270
....*....|....*....|....*....|..
gi 503253044 207 DYSGTVLVISHDRyFLDEVVNKVIDLEDGEVT 238
Cdd:COG1136 193 ELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
335-517 |
5.30e-11 |
|
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: 63.09 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGD-KLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIGYL 402
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIdGEDIreqdpvelrrKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 403 SQNI-----------------FSSIKDETVIETFRDVVNVTEGEARHILARFmfygytvfqkVSQLSGGERMRLRLAQLM 465
Cdd:cd03295 81 IQQIglfphmtveenialvpkLLKWPKEKIRERADELLALVGLDPAEFADRY----------PHELSGGQQQRVGVARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 466 YQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHDRYFLNKLFDKI 517
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELgktiVFVTHDIDEAFRLADRI 206
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-525 |
6.44e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.16 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRIGSnvkiGYLSQnifssIKD 412
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLagLET--PSAGELLAGT----APLAE-----ARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 413 ETVIeTFRD---------VVNVTEG-------EARHILArfmfygytvfqKV----------SQLSGGERMRLRLAQLMY 466
Cdd:PRK11247 82 DTRL-MFQDarllpwkkvIDNVGLGlkgqwrdAALQALA-----------AVgladranewpAALSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 467 QDINLLILDEPTNHLD----IESREVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:PRK11247 150 HRPGLLLLDEPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
334-506 |
7.79e-11 |
|
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: 62.45 E-value: 7.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGD-----KLLfEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRI-GSNV-------- 397
Cdd:COG4181 8 IIELRGLTKTVGTgagelTIL-KGISLEVEAGESVAIVGASGSGKSTLLGLLagLDR--PTSGTVRLaGQDLfaldedar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 ------KIGYLSQNiFSSIKDETVIEtfrdvvNVT-----------EGEARHILARfmfygytvfqkV----------SQ 450
Cdd:COG4181 85 arlrarHVGFVFQS-FQLLPTLTALE------NVMlplelagrrdaRARARALLER-----------VglghrldhypAQ 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 451 LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDF---QGS-LLAVSHD 506
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnreRGTtLVLVTHD 206
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-237 |
8.17e-11 |
|
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: 62.21 E-value: 8.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIicSVNKVAKMYGGNA----IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLkkdaavgyltqipD 76
Cdd:cd03258 1 MI--ELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-------------D 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 77 YHDSTSTKevlksafspllqmEEKMEKLEAEMG-VETDPNKLQ-KLMGEYGELQDQYANNGGYEIESNIEKIAHGLNIQM 154
Cdd:cd03258 66 GTDLTLLS-------------GKELRKARRRIGmIFQHFNLLSsRTVFENVALPLEIAGVPKAEIEERVLELLELVGLED 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 155 FIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG----TVLVISHDRYFLDEVVNKVI 230
Cdd:cd03258 133 KADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRVA 212
|
....*..
gi 503253044 231 DLEDGEV 237
Cdd:cd03258 213 VMEKGEV 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-237 |
8.43e-11 |
|
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: 62.00 E-value: 8.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIhlkkdaavgyltQIPDYHDSTSTKEVLKsafspllqmee 99
Cdd:cd03266 22 DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA------------TVDGFDVVKEPAEARR----------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 100 KMEKLEAEMGVE---TDPNKLQKLMGEYGeLQdqyanngGYEIESNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLM 176
Cdd:cd03266 79 RLGFVSDSTGLYdrlTARENLEYFAGLYG-LK-------GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 177 LLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-71 |
9.01e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 63.20 E-value: 9.01e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK------KDAA-VGYL 71
Cdd:COG4152 3 ELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgepldpEDRRrIGYL 76
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
5-237 |
9.18e-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: 61.78 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIhlkkdaavgyltqIPDYHDSTSTK 84
Cdd:cd03262 2 EIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI-------------IIDGLKLTDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 evlksafspllqmeEKMEKLEAEMGV-----ETDPNK--LQKLMgeYGELQDQYANnggyeiESNIEKIAHGL----NIQ 153
Cdd:cd03262 69 --------------KNINELRQKVGMvfqqfNLFPHLtvLENIT--LAPIKVKGMS------KAEAEERALELlekvGLA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 154 MFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLD-LMAVEWLGSfLRD--YSG-TVLVISHDRYFLDEVVNKV 229
Cdd:cd03262 127 DKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpELVGEVLDV-MKDlaEEGmTMVVVTHEMGFAREVADRV 205
|
....*...
gi 503253044 230 IDLEDGEV 237
Cdd:cd03262 206 IFMDDGRI 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
364-522 |
9.60e-11 |
|
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: 61.72 E-value: 9.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRIGSnvKIGYLSQN--IFS-SIKD-------------ETVIET---FRDVVN 424
Cdd:cd03250 35 AIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEpwIQNgTIREnilfgkpfdeeryEKVIKAcalEPDLEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 425 VTEGEARHIlarfmfyGytvfQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE-SREVLEEALedfQGSLLA- 502
Cdd:cd03250 113 LPDGDLTEI-------G----EKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCI---LGLLLNn 178
|
170 180
....*....|....*....|....*
gi 503253044 503 -----VSHDRYFLNKlFDKIYWIEA 522
Cdd:cd03250 179 ktrilVTHQLQLLPH-ADQIVVLDN 202
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
345-495 |
1.08e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK------------IGYLsqnifSSIK 411
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRrqrdeyhqdllyLGHQ-----PGIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 412 DE-TVIE--TF--RDVVNVTEGEARHILARFmfyGYTVFQKV--SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE 484
Cdd:PRK13538 87 TElTALEnlRFyqRLHGPGDDEALWEALAQV---GLAGFEDVpvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
170
....*....|.
gi 503253044 485 SREVLEEALED 495
Cdd:PRK13538 164 GVARLEALLAQ 174
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
5-237 |
1.18e-10 |
|
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: 62.13 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-KDAA-------------VGY 70
Cdd:cd03261 2 ELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgEDISglseaelyrlrrrMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 71 LTQIPDYHDSTSTKEVLksAFsPLLQMEEK---------MEKLEAeMGVETDPNKLqklmgeygelqdqyannggyeies 141
Cdd:cd03261 82 LFQSGALFDSLTVFENV--AF-PLREHTRLseeeireivLEKLEA-VGLRGAEDLY------------------------ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 142 niekiahglniqmfihsPfSQLSGGEKTKVGLG---------LMllkqpdlllLDEPTNHLDLMAVEWLGSFLRD----Y 208
Cdd:cd03261 134 -----------------P-AELSGGMKKRVALAralaldpelLL---------YDEPTAGLDPIASGVIDDLIRSlkkeL 186
|
250 260
....*....|....*....|....*....
gi 503253044 209 SGTVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:cd03261 187 GLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-61 |
1.22e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 62.25 E-value: 1.22e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIH 61
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH 64
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
5-63 |
1.24e-10 |
|
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: 62.07 E-value: 1.24e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFD 60
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-62 |
1.51e-10 |
|
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: 61.82 E-value: 1.51e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 6 VNKVAKMYGGN-AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:cd03256 3 VENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI 60
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
334-525 |
1.73e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 61.65 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQLfpDKGEVRI------GSNVKIGYLSQ- 404
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCInkLEEI--TSGDLIVdglkvnDPKVDERLIRQe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 --------NIFSSIKD-ETVIETFRDVVNVTEGEARHiLARfmfygyTVFQKV----------SQLSGGERMRLRLAQLM 465
Cdd:PRK09493 79 agmvfqqfYLFPHLTAlENVMFGPLRVRGASKEEAEK-QAR------ELLAKVglaerahhypSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 466 YQDINLLILDEPTNHLDIESR-EVLE--EALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRhEVLKvmQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
364-506 |
1.94e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.41 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV----------KIGYL----SQNIFssikDETVIETF---RDVVNVT 426
Cdd:COG4586 52 GFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpfkrrkefarRIGVVfgqrSQLWW----DLPAIDSFrllKAIYRIP 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 427 EGEARHILARFMfygyTVF-------QKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIES----REVLEEALED 495
Cdd:COG4586 128 DAEYKKRLDELV----ELLdlgelldTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSkeaiREFLKEYNRE 203
|
170
....*....|.
gi 503253044 496 FQGSLLAVSHD 506
Cdd:COG4586 204 RGTTILLTSHD 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
5-62 |
1.97e-10 |
|
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: 60.91 E-value: 1.97e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRF 59
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
343-495 |
2.10e-10 |
|
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: 61.09 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 343 CFG---DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNVKIGYLSQNIfSSIKDETV 415
Cdd:cd03253 7 TFAydpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgqdiREVTLDSLRRAI-GVVPQDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 416 IetFRDVV---------NVTEGE------ARHILARFMFY--GYT--VFQKVSQLSGGERMRLRLAQLMYQDINLLILDE 476
Cdd:cd03253 86 L--FNDTIgynirygrpDATDEEvieaakAAQIHDKIMRFpdGYDtiVGERGLKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170
....*....|....*....
gi 503253044 477 PTNHLDIESREVLEEALED 495
Cdd:cd03253 164 ATSALDTHTEREIQAALRD 182
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
346-493 |
2.23e-10 |
|
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: 64.16 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHIT--------YQNRA---AIIGENGTGKSTLLKLILQQLFPDKGEVRigSNVKIGYLSQniFSSIKDET 414
Cdd:TIGR01271 427 DGLFFSNFSLYVTpvlknisfKLEKGqllAVAGSTGSGKSSLLMMIMGELEPSEGKIK--HSGRISFSPQ--TSWIMPGT 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 415 VIET-----------FRDVVNVTEGEARhiLARFMFYGYTVFQKVS-QLSGGERMRLRLAQLMYQDINLLILDEPTNHLD 482
Cdd:TIGR01271 503 IKDNiifglsydeyrYTSVIKACQLEED--IALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170
....*....|..
gi 503253044 483 IES-REVLEEAL 493
Cdd:TIGR01271 581 VVTeKEIFESCL 592
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
334-495 |
2.25e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 61.57 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDK--------------------GEVRi 393
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqregrlaRDIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 394 GSNVKIGYLSQNiFSSIKDETVIET---------------FRDVVNVTEGEARHILARFMFYGYTvFQKVSQLSGGERMR 458
Cdd:PRK09984 83 KSRANTGYIFQQ-FNLVNRLSVLENvligalgstpfwrtcFSWFTREQKQRALQALTRVGMVHFA-HQRVSTLSGGQQQR 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 503253044 459 LRLAQLMYQDINLLILDEPTNHLDIESREVLEEALED 495
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRD 197
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-586 |
2.41e-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: 63.28 E-value: 2.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQLFPDKGEV-----------------RIGS 395
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpsKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 396 NV---------------------------KIGYLSQNIFSSIKDETVIETFRDVVNVTEGEARHILAR------FMFYGY 442
Cdd:TIGR03269 81 PCpvcggtlepeevdfwnlsdklrrrirkRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRavdlieMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 443 TVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREV----LEEALEDFQGSLLAVSHDRYFLNKLFDKIY 518
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 519 WIEAKKIhCFEGNYTWAKEKMtkrrestLQLSLEKKKEVSLPKKEPI---KNKRKDAENLEEDLVKLEDSI 586
Cdd:TIGR03269 241 WLENGEI-KEEGTPDEVVAVF-------MEGVSEVEKECEVEVGEPIikvRNVSKRYISVDRGVVKAVDNV 303
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
5-62 |
2.41e-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: 2.41e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:cd03300 2 ELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL 59
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-171 |
2.59e-10 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 61.20 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIICSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL-KKD-----------AAV 68
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDithlpmhkrarLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 69 GYLTQIPdyhdststkevlkSAFSPL---------LQM-----EEKMEKLEAemgvetdpnklqkLMGEYGelqdqyann 134
Cdd:COG1137 81 GYLPQEA-------------SIFRKLtvednilavLELrklskKEREERLEE-------------LLEEFG--------- 125
|
170 180 190
....*....|....*....|....*....|....*..
gi 503253044 135 ggyeiesnIEKIAhglniqmfiHSPFSQLSGGEKTKV 171
Cdd:COG1137 126 --------ITHLR---------KSKAYSLSGGERRRV 145
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-60 |
2.75e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 2.75e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 1 MIICSVNKVAKMYGGNAIF---------EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV 69
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
345-493 |
3.56e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 59.81 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI---GSNVKIGYLSQNIF-----SSIKDE-TV 415
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggPLDFQRDSIARGLLylghaPGIKTTlSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 416 IE--TFRDVVNVTEG--EArhiLARFMFYGYTvFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEE 491
Cdd:cd03231 91 LEnlRFWHADHSDEQveEA---LARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
..
gi 503253044 492 AL 493
Cdd:cd03231 167 AM 168
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-60 |
3.71e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.87 E-value: 3.71e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
334-482 |
4.65e-10 |
|
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: 59.98 E-value: 4.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCF----GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDK---GEVRI-GSNVK------- 398
Cdd:cd03234 3 VLPWWDVGLKAknwnKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFnGQPRKpdqfqkc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 IGYLSQN--IFSSIkdeTVIETF----------------RDVVNVTEGEARhiLARFMFYGYtvfqKVSQLSGGERMRLR 460
Cdd:cd03234 83 VAYVRQDdiLLPGL---TVRETLtytailrlprkssdaiRKKRVEDVLLRD--LALTRIGGN----LVKGISGGERRRVS 153
|
170 180
....*....|....*....|..
gi 503253044 461 LAQLMYQDINLLILDEPTNHLD 482
Cdd:cd03234 154 IAVQLLWDPKVLILDEPTSGLD 175
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
6-60 |
4.85e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 60.46 E-value: 4.85e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL 69
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
5-238 |
4.92e-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: 59.51 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIkEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL-----KKD-----AAVGYLTQI 74
Cdd:cd03264 2 QLENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvLKQpqklrRRIGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 75 PDYHDSTSTKEVLksAFSPLLQ-MEEKMEKLEAEMGVETdpnklqklmgeygelqdqyannggyeiesniekiahgLNIQ 153
Cdd:cd03264 81 FGVYPNFTVREFL--DYIAWLKgIPSKEVKARVDEVLEL-------------------------------------VNLG 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 154 MFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVI--SHDRYFLDEVVNKVID 231
Cdd:cd03264 122 DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVIlsTHIVEDVESLCNQVAV 201
|
....*..
gi 503253044 232 LEDGEVT 238
Cdd:cd03264 202 LNKGKLV 208
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-237 |
5.03e-10 |
|
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: 58.77 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNA--IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLkkdaavgyltqipDYHDSTS 82
Cdd:cd03246 2 EVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-------------DGADISQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 83 TkevlksafspllqmeekmekleaemgvetDPNKLQKLMGEYgeLQDQYANNGgyEIESNIekiahglniqmfihspfsq 162
Cdd:cd03246 69 W-----------------------------DPNELGDHVGYL--PQDDELFSG--SIAENI------------------- 96
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 163 LSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHdRYFLDEVVNKVIDLEDGEV 237
Cdd:cd03246 97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKaagATRIVIAH-RPETLASADRILVLEDGRV 173
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
330-525 |
5.21e-10 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 60.55 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 330 SGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------- 397
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFdGENIpamsrsrlytv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 --KIGYLSQN--IFSsikDETVIEtfrdvvNVTEGEARHILARFMFYGYTVFQKV-------------SQLSGGERMRLR 460
Cdd:PRK11831 83 rkRMSMLFQSgaLFT---DMNVFD------NVAYPLREHTQLPAPLLHSTVMMKLeavglrgaaklmpSELSGGMARRAA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 461 LAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:PRK11831 154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKI 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
364-506 |
8.42e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 60.03 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV-----------KIGYLSQN-----IFSSIKD-------------ET 414
Cdd:PRK13635 37 AIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrQVGMVFQNpdnqfVGATVQDdvafglenigvprEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 415 VIETFRDVVNVTegearhilarfmfyGYTVF--QKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR-EVLE- 490
Cdd:PRK13635 117 MVERVDQALRQV--------------GMEDFlnREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRrEVLEt 182
|
170
....*....|....*...
gi 503253044 491 -EALEDFQG-SLLAVSHD 506
Cdd:PRK13635 183 vRQLKEQKGiTVLSITHD 200
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
353-493 |
9.30e-10 |
|
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: 59.87 E-value: 9.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 353 VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRigSNVKIGYLSQniFSSIKDETVIETFrdVVNVTEGEARH 432
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK--HSGRISFSSQ--FSWIMPGTIKENI--IFGVSYDEYRY 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 433 I-----------LARFMFYGYTVFQKVS-QLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIES-REVLEEAL 493
Cdd:cd03291 130 KsvvkacqleedITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTeKEIFESCV 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
344-525 |
1.19e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 59.75 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEgVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV---------------KIGYLSQNIFS 408
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 409 SIKDETVIetfRDVV------NVTEGEARHILARFM--------FYGYTVFqkvsQLSGGERMRLRLAQLMYQDINLLIL 474
Cdd:PRK13643 96 QLFEETVL---KDVAfgpqnfGIPKEKAEKIAAEKLemvgladeFWEKSPF----ELSGGQMRRVAIAGILAMEPEVLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503253044 475 DEPTNHLDIESR-EVLE--EALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:PRK13643 169 DEPTAGLDPKARiEMMQlfESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-496 |
1.20e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 59.74 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV------KIGYLsqn 405
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTV----PKgeifGLLGPNGAGKTTTIRIILGILAPDSGEVLWdGEPLdpedrrRIGYLpee 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 406 ifssiKDETVIETfrdVV------NVTEGEARH----ILARFMFYGYTvFQKVSQLSGGERMRLRLAQLMYQDINLLILD 475
Cdd:COG4152 80 r-glyPKMKVGEQ---LVylarlkGLSKAEAKRradeWLERLGLGDRA-NKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180
....*....|....*....|.
gi 503253044 476 EPTNHLDIESREVLEEALEDF 496
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIREL 175
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
33-237 |
1.31e-09 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 59.06 E-value: 1.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 33 GLVGRNGSGKTTLIRLLAGEETPDTGDIHLkkdAAVgyltqipDYHDSTSTKEVLKSAFspllqmeekmekleAEMGVET 112
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDL---AGV-------DLHGLSRRARARRVAL--------------VEQDSDT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 113 DPNKLQKLMGEYGELQdqYANNGGYEIESNIEKIAHGL---NIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEP 189
Cdd:TIGR03873 87 AVPLTVRDVVALGRIP--HRSLWAGDSPHDAAVVDRALartELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503253044 190 TNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:TIGR03873 165 TNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVLDGGRV 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
323-525 |
1.38e-09 |
|
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: 61.29 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 323 EMESTERSGNDVIMLK-DISKCFGDKLLfEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNV 397
Cdd:TIGR01193 463 KRTELNNLNGDIVINDvSYSYGYGSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslKDI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 K-------IGYLSQN--IFS-SI--------KDETVIETFRDVVNVTEGEArHILARFMFYGYTVFQKVSQLSGGERMRL 459
Cdd:TIGR01193 542 DrhtlrqfINYLPQEpyIFSgSIlenlllgaKENVSQDEIWAACEIAEIKD-DIENMPLGYQTELSEEGSSISGGQKQRI 620
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 460 RLAQLMYQDINLLILDEPTNHLD-IESREVLEEALEDFQGSLLAVSHdRYFLNKLFDKIYWIEAKKI 525
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKI 686
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
335-506 |
1.47e-09 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 58.79 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNV-----KIGYLSQN 405
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgkdiTNLpphkrPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 406 --------IFSSI----------KDET---VIETFrDVVNVTEGEARhilarfmfygytvfqKVSQLSGGERMRLRLAQL 464
Cdd:cd03300 81 yalfphltVFENIafglrlkklpKAEIkerVAEAL-DLVQLEGYANR---------------KPSQLSGGQQQRVAIARA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503253044 465 MYQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHD 506
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHD 190
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
339-525 |
1.66e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 59.74 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 339 DISKCFGDKLLfeGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV---------------KIGYLS 403
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 404 QN--IFSSIkdeTVIETFRDVVNVTEGEARHI----LARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEP 477
Cdd:TIGR02142 82 QEarLFPHL---SVRGNLRYGMKRARPSERRIsferVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503253044 478 TNHLDIESR-EV---LEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:TIGR02142 159 LAALDDPRKyEIlpyLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRV 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
335-525 |
1.75e-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: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRIGS----------------- 395
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlLEQ--PEAGTIRVGDitidtarslsqqkglir 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 396 --NVKIGYLSQNiFSSIKDETVIEtfrdvvNVTEG--------------EARHILARFMFYGY-TVFQKvsQLSGGERMR 458
Cdd:PRK11264 82 qlRQHVGFVFQN-FNLFPHRTVLE------NIIEGpvivkgepkeeataRARELLAKVGLAGKeTSYPR--RLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 459 LRLAQLMYQDINLLILDEPTNHLDIE-SREVLE--EALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPElVGEVLNtiRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-232 |
1.80e-09 |
|
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: 60.38 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI--------HLKKDA---AVGYLTQIPDYHDSTS 82
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIavngvplaDADADSwrdQIAWVPQHPFLFAGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 83 TKEVL--KSAFSPLlQMEEKMEKLEAEMGVETDPNKLQKLMGEYGelqdqyannggyeiesniekiahglniqmfihspf 160
Cdd:TIGR02857 413 AENIRlaRPDASDA-EIREALERAGLDEFVAALPQGLDTPIGEGG----------------------------------- 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 161 SQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG--TVLVISHDRYFLdEVVNKVIDL 232
Cdd:TIGR02857 457 AGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQgrTVLLVTHRLALA-ALADRIVVL 529
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
337-507 |
1.82e-09 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 59.73 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHItyqnRA----AIIGENGTGKSTLLKLI--LQQlfPDKGEVRIG----SNVK-----IGY 401
Cdd:COG3842 8 LENVSKRYGDVTALDDVSLSI----EPgefvALLGPSGCGKTTLLRMIagFET--PDSGRILLDgrdvTGLPpekrnVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 402 LSQN--IFSSIkdeTVIEtfrdvvNVTEG-------------EARHILARFmfyGYTVFQ--KVSQLSGGERMRLRLAQL 464
Cdd:COG3842 82 VFQDyaLFPHL---TVAE------NVAFGlrmrgvpkaeiraRVAELLELV---GLEGLAdrYPHQLSGGQQQRVALARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503253044 465 MYQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHDR 507
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgitfIYVTHDQ 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
344-512 |
1.85e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK------------IGYLSQ-NIFSS 409
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKkdlctyqkqlcfVGHRSGiNPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 410 IKDETV--IETFRDVVNVTEgearhiLARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESRE 487
Cdd:PRK13540 91 LRENCLydIHFSPGAVGITE------LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|....*...
gi 503253044 488 VLEEALEDFQ---GSLLAVSHDRYFLNK 512
Cdd:PRK13540 165 TIITKIQEHRakgGAVLLTSHQDLPLNK 192
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
22-60 |
1.86e-09 |
|
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: 58.29 E-value: 1.86e-09
10 20 30
....*....|....*....|....*....|....*....
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:cd03257 24 VSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSI 62
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-218 |
2.01e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.41 E-value: 2.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEeTPDTGDIHLKKDAAVGYltqipdyhdSTSTKEVLKSAFS----PLLQM 97
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAW---------SAAELARHRAYLSqqqtPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 98 EekmekleaemgvetdpnklqklMGEYGELQdQYANNGGYEIESNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLG--- 174
Cdd:PRK03695 85 P----------------------VFQYLTLH-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavv 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 175 -------------LMllkqpdlllLDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHD 218
Cdd:PRK03695 142 lqvwpdinpagqlLL---------LDEPMNSLDVAQQAALDRLLSELCqqgIAVVMSSHD 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-238 |
2.03e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 58.87 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL--------------KKdaaVGYLTQIPD--YHDSTSTKE 85
Cdd:PRK13635 26 VSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvlseetvwdvrRQ---VGMVFQNPDnqFVGATVQDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 86 VlksAFSpllqmeekmekLEaemgvetdpnklqklmgeygelqdqyanNGGYEIESNIEKIAHGL---NIQMFIHSPFSQ 162
Cdd:PRK13635 103 V---AFG-----------LE----------------------------NIGVPREEMVERVDQALrqvGMEDFLNREPHR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 163 LSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMA-VEWLGSF--LRDYSG-TVLVISHDryfLDEVV--NKVIDLEDGE 236
Cdd:PRK13635 141 LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGrREVLETVrqLKEQKGiTVLSITHD---LDEAAqaDRVIVMNKGE 217
|
..
gi 503253044 237 VT 238
Cdd:PRK13635 218 IL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
337-478 |
2.05e-09 |
|
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: 58.21 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMH-----ITyqnraAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK-----------I 399
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTvpegeIV-----ALLGRNGAGKTTLLKTIMGLLPPRSGSIRFdGRDITglppheraragI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 400 GYLSQ--NIFSSIkdeTVIETFR-DVVNVTEGEARHILARFmfygYTVF--------QKVSQLSGGERMRLRLAQLMYQD 468
Cdd:cd03224 78 GYVPEgrRIFPEL---TVEENLLlGAYARRRAKRKARLERV----YELFprlkerrkQLAGTLSGGEQQMLAIARALMSR 150
|
170
....*....|
gi 503253044 469 INLLILDEPT 478
Cdd:cd03224 151 PKLLLLDEPS 160
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-242 |
2.18e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.29 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK---------------KDAAVGYLTQ----IPDYh 78
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNgqpmsklssaakaelRNQKLGFIYQfhhlLPDF- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 79 dststkEVLKSAFSPLL-------QMEEKMEKLEAEMGvetdpnklqklmgeygelqdqyannggyeiesnIEKIAHgln 151
Cdd:PRK11629 103 ------TALENVAMPLLigkkkpaEINSRALEMLAAVG---------------------------------LEHRAN--- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 152 iqmfiHSPfSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAV----EWLGSFLRDYSGTVLVISHDRYfLDEVVN 227
Cdd:PRK11629 141 -----HRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAdsifQLLGELNRLQGTAFLVVTHDLQ-LAKRMS 213
|
250
....*....|....*
gi 503253044 228 KVIDLEDGEVTTYHT 242
Cdd:PRK11629 214 RQLEMRDGRLTAELS 228
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
337-506 |
2.56e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.17 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQN--IFssiKDET 414
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERgvVF---QNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 415 VIeTFRDVV-NVTEG--------EARHILARFMF--YGYTVFQK--VSQLSGGERMRLRLAQLMYQDINLLILDEPTNHL 481
Cdd:PRK11248 81 LL-PWRNVQdNVAFGlqlagvekMQRLEIAHQMLkkVGLEGAEKryIWQLSGGQRQRVGIARALAANPQLLLLDEPFGAL 159
|
170 180
....*....|....*....|....*....
gi 503253044 482 DIESREVLEEAL----EDFQGSLLAVSHD 506
Cdd:PRK11248 160 DAFTREQMQTLLlklwQETGKQVLLITHD 188
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
365-517 |
3.07e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.15 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLFPDKGevRIGSNVKI--------GYLSQNIFSSIKDETV--------------------- 415
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLG--KFDDPPDWdeildefrGSELQNYFTKLLEGDVkvivkpqyvdlipkavkgkvg 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 416 --------IETFRDVVNVTEgeARHILARfmfygytvfqKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR- 486
Cdd:cd03236 109 ellkkkdeRGKLDELVDQLE--LRHVLDR----------NIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRl 176
|
170 180 190
....*....|....*....|....*....|....
gi 503253044 487 ---EVLEEALEDfQGSLLAVSHDRYFLNKLFDKI 517
Cdd:cd03236 177 naaRLIRELAED-DNYVLVVEHDLAVLDYLSDYI 209
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
14-218 |
3.14e-09 |
|
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: 59.68 E-value: 3.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL-----------KKDAAVGYLTQIPDYHDSTS 82
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpvssldqdEVRRRVSVCAQDAHLFDTTV 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 83 TKEVLKSAfsPLLQMEEKMEKLEA---EMGVETDPNKLQKLMGEYGELqdqyannggyeiesniekiahglniqmfihsp 159
Cdd:TIGR02868 426 RENLRLAR--PDATDEELWAALERvglADWLRALPDGLDTVLGEGGAR-------------------------------- 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 160 fsqLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRD-YSG-TVLVISHD 218
Cdd:TIGR02868 472 ---LSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAaLSGrTVVLITHH 529
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-62 |
3.51e-09 |
|
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: 57.58 E-value: 3.51e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAG-----EETPDTGDIHL 62
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLL 64
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-219 |
3.73e-09 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 59.08 E-value: 3.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-KDaavgyLTQIPDYHdststk 84
Cdd:PRK11607 22 IRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVD-----LSHVPPYQ------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 evlksafSPLLQMEEKMeKLEAEMGVETDPnklqklmgEYGELQDQYANNggyEIESNIEKIAHGLNIQMFIHSPFSQLS 164
Cdd:PRK11607 91 -------RPINMMFQSY-ALFPHMTVEQNI--------AFGLKQDKLPKA---EIASRVNEMLGLVHMQEFAKRKPHQLS 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 165 GGEKTKVGLGLMLLKQPDLLLLDEPTNHLD-----LMAVEWLgSFLRDYSGTVLVISHDR 219
Cdd:PRK11607 152 GGQRQRVALARSLAKRPKLLLLDEPMGALDkklrdRMQLEVV-DILERVGVTCVMVTHDQ 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
332-507 |
3.90e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 58.58 E-value: 3.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 332 NDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI----------------------LQQ------ 383
Cdd:PRK11432 4 KNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVaglekptegqifidgedvthrsIQQrdicmv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 384 -----LFPdkgEVRIGSNVKIGYLSQNIFSSIKDETVIETFrDVVNVTEGEARHilarfmfygytvfqkVSQLSGGERMR 458
Cdd:PRK11432 84 fqsyaLFP---HMSLGENVGYGLKMLGVPKEERKQRVKEAL-ELVDLAGFEDRY---------------VDQISGGQQQR 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 503253044 459 LRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHDR 507
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFnitsLYVTHDQ 197
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
337-537 |
4.58e-09 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 57.27 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQlfpDKGEVRIGSnvkIGYLSQNIFSSIKDE--- 413
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGH---PSYEVTSGT---ILFKGQDLLELEPDErar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 414 ----------------TVIETFRDVVN-VTEGEARHILARFMFYgyTVFQKVSQL----------------SGGERMRLR 460
Cdd:TIGR01978 77 aglflafqypeeipgvSNLEFLRSALNaRRSARGEEPLDLLDFE--KLLKEKLALldmdeeflnrsvnegfSGGEKKRNE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 461 LAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG---SLLAVSHDRYFLNKLF-DKIYWIEAKKIhCFEGNYTWAK 536
Cdd:TIGR01978 155 ILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLNYIKpDYVHVLLDGRI-VKSGDVELAK 233
|
.
gi 503253044 537 E 537
Cdd:TIGR01978 234 E 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
335-490 |
5.14e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.72 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEG-----VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV------------ 397
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERralydVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVitagkknkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 ---KIGYLSQNIFSSIKDETVIetfRDVV------NVTEGEARHiLARFMFYGYTVFQKVSQ-----LSGGERMRLRLAQ 463
Cdd:PRK13634 83 lrkKVGIVFQFPEHQLFEETVE---KDICfgpmnfGVSEEDAKQ-KAREMIELVGLPEELLArspfeLSGGQMRRVAIAG 158
|
170 180
....*....|....*....|....*...
gi 503253044 464 LMYQDINLLILDEPTNHLDIESR-EVLE 490
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRkEMME 186
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
13-63 |
5.80e-09 |
|
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: 56.91 E-value: 5.80e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:COG0410 13 YGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFD 63
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
337-505 |
6.21e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGD-KLLfEGVNMHItyqnRA----AIIGENGTGKSTLLKLI--LQQlfPDKGEVRI-GSNVKigylsqniFS 408
Cdd:COG1129 7 MRGISKSFGGvKAL-DGVSLEL----RPgevhALLGENGAGKSTLMKILsgVYQ--PDSGEILLdGEPVR--------FR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 409 SIKD-----------E-------TVIE--------TFRDVVNV--TEGEARHILARFmfyGYTV--FQKVSQLSGGERMR 458
Cdd:COG1129 72 SPRDaqaagiaiihqElnlvpnlSVAEniflgrepRRGGLIDWraMRRRARELLARL---GLDIdpDTPVGDLSVAQQQL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 503253044 459 LRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDF--QG-SLLAVSH 505
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLkaQGvAIIYISH 198
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-62 |
6.37e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 58.49 E-value: 6.37e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 503253044 9 VAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:COG1129 10 ISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL 63
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
334-513 |
7.05e-09 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 56.59 E-value: 7.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLL----FEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG-------SNVKIGYL 402
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLdtrvLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNgqslsklSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 403 SQNIFSSI-------KDETVIEtfrDVV--------NVTEGE--ARHILARFMFyGYTVFQKVSQLSGGERMRLRLAQLM 465
Cdd:TIGR02211 81 RNKKLGFIyqfhhllPDFTALE---NVAmplligkkSVKEAKerAYEMLEKVGL-EHRINHRPSELSGGERQRVAIARAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 503253044 466 YQDINLLILDEPTNHLDIE-SREVLEEALE---DFQGSLLAVSHDRYFLNKL 513
Cdd:TIGR02211 157 VNQPSLVLADEPTGNLDNNnAKIIFDLMLElnrELNTSFLVVTHDLELAKKL 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
335-505 |
9.61e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 58.19 E-value: 9.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCF-GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNVKIGYLSQNIFSS 409
Cdd:PRK10790 341 IDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgrplSSLSHSVLRQGVAMV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 410 IKDETVI-ETFRDvvNVTEGeaRHI----------------LARFMFYG-YTVF-QKVSQLSGGERMRLRLAQLMYQDIN 470
Cdd:PRK10790 421 QQDPVVLaDTFLA--NVTLG--RDIseeqvwqaletvqlaeLARSLPDGlYTPLgEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 503253044 471 LLILDEPTNHLDIESREVLEEALEDF--QGSLLAVSH 505
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-225 |
1.09e-08 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 55.32 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQ---IPDyhdststkevlks 89
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrseVPD------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 90 AFsPLlQMEEKMEkleaeMGvetdpnklqkLMGEYGELQDQYANNggyeiESNIEKIAHGLNIQMFIHSPFSQLSGGEKT 169
Cdd:NF040873 69 SL-PL-TVRDLVA-----MG----------RWARRGLWRRLTRDD-----RAAVDDALERVGLADLAGRQLGELSGGQRQ 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 170 KVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDryfLDEV 225
Cdd:NF040873 127 RALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHArgaTVVVVTHD---LELV 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
339-477 |
1.35e-08 |
|
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: 55.63 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 339 DISKCFGDKLLFEGVNMHItyqNRAAII---GENGTGKSTLLKLILQQLFPDKGEVRIGSN------------VKIGYLS 403
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSV---KQGEIVgllGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklpmhkrarLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 404 Q--NIFSSIKDE----TVIETFRDVVNVTEGEARHILARFMFYgYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEP 477
Cdd:cd03218 82 QeaSIFRKLTVEenilAVLEIRGLSKKEREEKLEELLEEFHIT-HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
346-525 |
1.36e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.93 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLfPDKGEVRIgSNV------------KIGYLSQN---IFSSI 410
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKI-NGIelreldpeswrkHLSWVGQNpqlPHGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 411 KDETVIETfrdvVNVTEGEARHILAR-----F---MFYG--YTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNH 480
Cdd:PRK11174 440 RDNVLLGN----PDASDEQLQQALENawvseFlplLPQGldTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 503253044 481 LDIESREVLEEALED--FQGSLLAVSHDRYFLnKLFDKIYWIEAKKI 525
Cdd:PRK11174 516 LDAHSEQLVMQALNAasRRQTTLMVTHQLEDL-AQWDQIWVMQDGQI 561
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
334-507 |
1.40e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.65 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCF-GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG-------SNVKIGYLSQN 405
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditrlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 406 IFSSIKDETVI--ETFRDVVNV--------TEGEARHILARFMFYGytVFQKVS----QLSGGERMRLRLAQLMYQDINL 471
Cdd:PRK10908 81 IGMIFQDHHLLmdRTVYDNVAIpliiagasGDDIRRRVSAALDKVG--LLDKAKnfpiQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 503253044 472 LILDEPTNHLDIESREVLEEALEDFQG---SLLAVSHDR 507
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDI 197
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-171 |
1.57e-08 |
|
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: 55.63 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI------------HLKKDAAVGYLT 72
Cdd:cd03218 2 RAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmHKRARLGIGYLP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 73 QIPDYHDSTSTKEVLKSAFspllqmeEKMEKLEAEMgvetdPNKLQKLMGEYgelqdqyannggyeiesNIEKIAhglni 152
Cdd:cd03218 82 QEASIFRKLTVEENILAVL-------EIRGLSKKER-----EEKLEELLEEF-----------------HITHLR----- 127
|
170
....*....|....*....
gi 503253044 153 qmfiHSPFSQLSGGEKTKV 171
Cdd:cd03218 128 ----KSKASSLSGGERRRV 142
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
364-506 |
1.60e-08 |
|
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: 55.20 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRIGSN----------VKIGYLSQniFSSIKDE-TVIET------FRDVVNVT 426
Cdd:cd03263 32 GLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYsirtdrkaarQSLGYCPQ--FDALFDElTVREHlrfyarLKGLPKSE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 427 EGEARHILARFMfyGYTVFQ--KVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG--SLLA 502
Cdd:cd03263 110 IKEEVELLLRVL--GLTDKAnkRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKgrSIIL 187
|
....
gi 503253044 503 VSHD 506
Cdd:cd03263 188 TTHS 191
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
9-224 |
1.64e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 56.76 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 9 VAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIhlkkdAAVGylTQIPDYHDSTSTKEVLK 88
Cdd:PRK13536 47 VSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-----TVLG--VPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 89 SAFspllqmeekmEKLEAEMGVETdpNKLqkLMGEYGELQDQyannggyEIESNIEKIAHGLNIQMFIHSPFSQLSGGEK 168
Cdd:PRK13536 120 PQF----------DNLDLEFTVRE--NLL--VFGRYFGMSTR-------EIEAVIPSLLEFARLESKADARVSDLSGGMK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 169 TKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDY---SGTVLVISHdryFLDE 224
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLlarGKTILLTTH---FMEE 234
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
13-237 |
1.85e-08 |
|
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: 55.57 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNA--IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIhlkkdaavgyltqIPDYHD-STSTKEVLKS 89
Cdd:cd03252 10 YKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-------------LVDGHDlALADPAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 90 AFSPLLQMEEKMEKLEAEMGVETDPNKLQKLMGEYGELQDQYAnnggyeiesNIEKIAHGLNiqMFIHSPFSQLSGGEKT 169
Cdd:cd03252 77 QVGVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHD---------FISELPEGYD--TIVGEQGAGLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 170 KVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG--TVLVISHdRYFLDEVVNKVIDLEDGEV 237
Cdd:cd03252 146 RIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDICAgrTVIIIAH-RLSTVKNADRIIVMEKGRI 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
320-497 |
1.93e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 57.34 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 320 MNLEME------STERSGNDVImLKDISKCF--GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEV 391
Cdd:PRK11176 322 LDLEQEkdegkrVIERAKGDIE-FRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 392 RI-GSNVK----------IGYLSQNIfssikdetviETFRDVVNVTEGEARH--------ILARFMFYGYTVFQKVSQ-- 450
Cdd:PRK11176 401 LLdGHDLRdytlaslrnqVALVSQNV----------HLFNDTIANNIAYARTeqysreqiEEAARMAYAMDFINKMDNgl 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 451 ----------LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQ 497
Cdd:PRK11176 471 dtvigengvlLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ 527
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
9-62 |
2.07e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.49 E-value: 2.07e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 503253044 9 VAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK09452 20 ISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML 73
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-238 |
2.12e-08 |
|
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: 54.24 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNA--IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKkdaavgyltqipdyhdsts 82
Cdd:cd03247 2 SINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLD------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 83 tkevlksafspllqmeekmekleaemgvETDPNKLQKLMGEYGELQDQYANNGGYEIESNIEKiahglniqmfihspfsQ 162
Cdd:cd03247 63 ----------------------------GVPVSDLEKALSSLISVLNQRPYLFDTTLRNNLGR----------------R 98
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 163 LSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLD----LMAVEWLGSFLRDysGTVLVISHdRYFLDEVVNKVIDLEDGEVT 238
Cdd:cd03247 99 FSGGERQRLALARILLQDAPIVLLDEPTVGLDpiteRQLLSLIFEVLKD--KTLIWITH-HLTGIEHMDKILFLENGKII 175
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
345-505 |
2.33e-08 |
|
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: 57.07 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLfEGVNMHITYQNRAAIIGENGTGKSTLLKlILQQLFPDKGEVR-IGSNVKIGYLSQN------------IFSSIK 411
Cdd:TIGR00954 464 GDVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRLtKPAKGKLFYVPQRpymtlgtlrdqiIYPDSS 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 412 DETVIETFRD------VVNVtegEARHILARFMfyGYTVFQKVSQ-LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE 484
Cdd:TIGR00954 542 EDMKRRGLSDkdleqiLDNV---QLTHILEREG--GWSAVQDWMDvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVD 616
|
170 180
....*....|....*....|.
gi 503253044 485 SREVLEEALEDFQGSLLAVSH 505
Cdd:TIGR00954 617 VEGYMYRLCREFGITLFSVSH 637
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-62 |
2.50e-08 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 55.97 E-value: 2.50e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 3 ICSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISL 66
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
335-489 |
2.71e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 55.52 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEG-----VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV------------ 397
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 ---KIGYLSQNIFSSIKDETVIEtfrDV--------VNVTEGE--ARHILArFMFYGYTVFQKVS-QLSGGERMRLRLAQ 463
Cdd:PRK13649 83 irkKVGLVFQFPESQLFEETVLK---DVafgpqnfgVSQEEAEalAREKLA-LVGISESLFEKNPfELSGGQMRRVAIAG 158
|
170 180
....*....|....*....|....*.
gi 503253044 464 LMYQDINLLILDEPTNHLDIESREVL 489
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKEL 184
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
6-73 |
2.83e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 56.25 E-value: 2.83e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK---------KDAAVGYLTQ 73
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlhaRDRKVGFVFQ 81
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
333-491 |
3.41e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.92 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 333 DVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQLFPD---KGEVRIGSN-------VKIG 400
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnrLIELYPEarvSGEVYLDGQdifkmdvIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 401 YLSQNIF---SSIKDETVIETF-------RDVVNVTEGEARhilARFMFYGYTVFQKV--------SQLSGGERMRLRLA 462
Cdd:PRK14247 82 RRVQMVFqipNPIPNLSIFENValglklnRLVKSKKELQER---VRWALEKAQLWDEVkdrldapaGKLSGGQQQRLCIA 158
|
170 180
....*....|....*....|....*....
gi 503253044 463 QLMYQDINLLILDEPTNHLDIESREVLEE 491
Cdd:PRK14247 159 RALAFQPEVLLADEPTANLDPENTAKIES 187
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
6-237 |
3.80e-08 |
|
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: 56.67 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYG-GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI----HLKKD-------AAVGYLTQ 73
Cdd:TIGR01193 476 INDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEIllngFSLKDidrhtlrQFINYLPQ 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 74 IPdYHDSTSTKEVLksafspLLQMEEKMEKLEAEMGVETdpnklqklmgeygelqdqyannggYEIESNIEKIAHGLNIQ 153
Cdd:TIGR01193 556 EP-YIFSGSILENL------LLGAKENVSQDEIWAACEI------------------------AEIKDDIENMPLGYQTE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 154 MFIHSpfSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVE-WLGSFLRDYSGTVLVISHdRYFLDEVVNKVIDL 232
Cdd:TIGR01193 605 LSEEG--SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKkIVNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVL 681
|
....*
gi 503253044 233 EDGEV 237
Cdd:TIGR01193 682 DHGKI 686
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
14-237 |
4.45e-08 |
|
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: 54.26 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-KDAA--------VGYLTQipDYhdststk 84
Cdd:cd03299 10 WKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgKDITnlppekrdISYVPQ--NY------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 evlksAFSPLLQMEEKMEkleaeMGVetdpnKLQKLMGEygelqdqyannggyEIESNIEKIAHGLNIQMFIHSPFSQLS 164
Cdd:cd03299 81 -----ALFPHMTVYKNIA-----YGL-----KKRKVDKK--------------EIERKVLEIAEMLGIDHLLNRKPETLS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 165 GGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRD----YSGTVLVISHDryfLDEVV---NKVIDLEDGEV 237
Cdd:cd03299 132 GGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKirkeFGVTVLHVTHD---FEEAWalaDKVAIMLNGKL 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-60 |
4.62e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 55.09 E-value: 4.62e-08
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
334-477 |
4.76e-08 |
|
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: 54.20 E-value: 4.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK-----------IGY 401
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIdGQDIThlpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 402 LSQ--NIFssiKDETVIETFRDVVNVTEG--------EARHILARFMFyGYTVFQKVSQLSGGERMRLRLAQLMYQDINL 471
Cdd:TIGR04406 81 LPQeaSIF---RKLTVEENIMAVLEIRKDldraereeRLEALLEEFQI-SHLRDNKAMSLSGGERRRVEIARALATNPKF 156
|
....*.
gi 503253044 472 LILDEP 477
Cdd:TIGR04406 157 ILLDEP 162
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
365-530 |
5.81e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 52.96 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLFPDKGEVRIgSNVKIGYLSQNIfssikdetvietfrdvvnvtegearhilarfmfygytv 444
Cdd:cd03222 30 IVGPNGTGKTTAVKILAGQLIPNGDNDEW-DGITPVYKPQYI-------------------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 445 fqkvsQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR----EVLEEALEDFQGSLLAVSHDRYFLNKLFDkiywi 520
Cdd:cd03222 71 -----DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLSEEGKKTALVVEHDLAVLDYLSD----- 140
|
170
....*....|
gi 503253044 521 eakKIHCFEG 530
Cdd:cd03222 141 ---RIHVFEG 147
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-62 |
6.24e-08 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 55.11 E-value: 6.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 503253044 21 EISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRL 58
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
295-522 |
6.56e-08 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 55.58 E-value: 6.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 295 RRARNMERALERMEKLNRPIlnrtkmnlemESTERSGNDVIMLKDISKCFGD-KLLFEGVNMHITYQNRAAIIGENGTGK 373
Cdd:COG4178 333 DRLAGFEEALEAADALPEAA----------SRIETSEDGALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 374 STLLKLIlQQLFPD-KGEVRIGSNVKIGYLSQNIFssikdeTVIETFRDVV-------NVTEGEARHILarfmfygytvf 445
Cdd:COG4178 403 STLLRAI-AGLWPYgSGRIARPAGARVLFLPQRPY------LPLGTLREALlypataeAFSDAELREAL----------- 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 446 QKV----------------SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALED--FQGSLLAVSHdR 507
Cdd:COG4178 465 EAVglghlaerldeeadwdQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH-R 543
|
250
....*....|....*
gi 503253044 508 YFLNKLFDKIYWIEA 522
Cdd:COG4178 544 STLAAFHDRVLELTG 558
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
337-506 |
6.81e-08 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 53.89 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFG-----DkllfeGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGS---------------- 395
Cdd:COG0411 7 VRGLTKRFGglvavD-----DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrditglpphriarlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 396 -----------------NVKIGYLSQ---NIFSSIKDetvIETFRDVVNVTEGEARHILARFMFYGYtVFQKVSQLSGGE 455
Cdd:COG0411 82 artfqnprlfpeltvleNVLVAAHARlgrGLLAALLR---LPRARREEREARERAEELLERVGLADR-ADEPAGNLSYGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 456 RMRLRLAQLMYQDINLLILDEPT---NHLDIES-REVLEEALEDFQGSLLAVSHD 506
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAaglNPEETEElAELIRRLRDERGITILLIEHD 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
16-242 |
9.41e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 53.97 E-value: 9.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 16 NAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDA-----------AVGYLTQIPDYHDSTSTK 84
Cdd:PRK13650 20 KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKIGMVFQNPDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 EVlKSAFspllqmeekmekleaemGVEtdpnklqklmgeygelqdqyanNGGYEIESNIEKIAHGLNI---QMFIHSPFS 161
Cdd:PRK13650 100 ED-DVAF-----------------GLE----------------------NKGIPHEEMKERVNEALELvgmQDFKEREPA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 162 QLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLD----LMAVEWLGSFLRDYSGTVLVISHDryfLDEVV--NKVIDLEDG 235
Cdd:PRK13650 140 RLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD---LDEVAlsDRVLVMKNG 216
|
....*..
gi 503253044 236 EVTTYHT 242
Cdd:PRK13650 217 QVESTST 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
346-505 |
1.06e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.11 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLiLQQLF-PDKGEVRIgSNVKIG-----YLSQNIfSSIKDETVI--E 417
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAAL-LQNLYqPTGGQVLL-DGVPLVqydhhYLHRQV-ALVGQEPVLfsG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 418 TFRD-------------VVNVTEGEARHILARFMFYGY--TVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD 482
Cdd:TIGR00958 570 SVREniaygltdtpdeeIMAAAKAANAHDFIMEFPNGYdtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180
....*....|....*....|...
gi 503253044 483 IESREVLEEALEDFQGSLLAVSH 505
Cdd:TIGR00958 650 AECEQLLQESRSRASRTVLLIAH 672
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-237 |
1.17e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 53.46 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 2 IICSVNKVAKMYGG--NAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI-------------HLKKDa 66
Cdd:PRK13632 6 VMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkidgitiskenlkEIRKK- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 67 aVGYLTQIPDYHDSTSTKEVlKSAFSpllqMEEKMEkleaemgvetDPNKLQKLmgeygelqdqyannggyeiesnIEKI 146
Cdd:PRK13632 85 -IGIIFQNPDNQFIGATVED-DIAFG----LENKKV----------PPKKMKDI----------------------IDDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 147 AHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDY----SGTVLVISHDryfL 222
Cdd:PRK13632 127 AKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrktrKKTLISITHD---M 203
|
250
....*....|....*..
gi 503253044 223 DEVVN--KVIDLEDGEV 237
Cdd:PRK13632 204 DEAILadKVIVFSEGKL 220
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
351-506 |
1.46e-07 |
|
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: 52.85 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 351 EGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK---------------IGYLS--QNIFSSIKD 412
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQITepgpdrmvvfqnyslLPWLTvrENIALAVDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 413 ----------ETVIETFRDVVNVTEgeARHilarfmfygytvfQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD 482
Cdd:TIGR01184 82 vlpdlskserRAIVEEHIALVGLTE--AAD-------------KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180
....*....|....*....|....*...
gi 503253044 483 IESREVLEEAL----EDFQGSLLAVSHD 506
Cdd:TIGR01184 147 ALTRGNLQEELmqiwEEHRVTVLMVTHD 174
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-218 |
1.49e-07 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 52.97 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIICSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI------------HLKKDAAV 68
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 69 GYLTQIPdyhdststkevlkSAFSPLLQMEEKMEKLE--AEMGVETDPNKLQKLMGEYgelqdqyannggyeiesNIEKI 146
Cdd:PRK10895 81 GYLPQEA-------------SIFRRLSVYDNLMAVLQirDDLSAEQREDRANELMEEF-----------------HIEHL 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 147 AHGLNiqmfihspfSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAV---EWLGSFLRDYSGTVLVISHD 218
Cdd:PRK10895 131 RDSMG---------QSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVidiKRIIEHLRDSGLGVLITDHN 196
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-237 |
1.79e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 53.13 E-value: 1.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI---------------HLKKDaaVGYLTQIPDYH--DSTSTK 84
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditdkkvklsDIRKK--VGLVFQYPEYQlfEETIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 EVlksAFSPL---LQMEEKMEKLEAEMgvetdpnklqKLMG-EYGELQDQyannggyeiesniekiahglniqmfihSPF 160
Cdd:PRK13637 104 DI---AFGPInlgLSEEEIENRVKRAM----------NIVGlDYEDYKDK---------------------------SPF 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 161 sQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRD----YSGTVLVISHDRYFLDEVVNKVIDLEDGE 236
Cdd:PRK13637 144 -ELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
.
gi 503253044 237 V 237
Cdd:PRK13637 223 C 223
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
335-515 |
1.96e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 52.73 E-value: 1.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHItYQNR-AAIIGENGTGKSTLLKlILQQLFPDKGEVRIGSNVKigYLSQNIFSSikde 413
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEI-YQSKvTAIIGPSGCGKSTFLK-CLNRMNELESEVRVEGRVE--FFNQNIYER---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 414 tvietfRDVVNVTEGEARHILARFMFYGYTVFQKVS----------------------------------------QLSG 453
Cdd:PRK14258 80 ------RVNLNRLRRQVSMVHPKPNLFPMSVYDNVAygvkivgwrpkleiddivesalkdadlwdeikhkihksalDLSG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 454 GERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDF----QGSLLAVSHDRYFLNKLFD 515
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlrsELTMVIVSHNLHQVSRLSD 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
17-218 |
2.07e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 52.09 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 17 AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLkkdaaVGyltqipdyhdststkevlksafSPLLQ 96
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL-----VG----------------------QPLHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 97 M-EEKMEKLEAE---------MGVETdPNKLQK------LMGEygelQDQYANNGGYEIesnIEKIAHGlniQMFIHSPf 160
Cdd:PRK10584 77 MdEEARAKLRAKhvgfvfqsfMLIPT-LNALENvelpalLRGE----SSRQSRNGAKAL---LEQLGLG---KRLDHLP- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 161 SQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMA----VEWLGSFLRDYSGTVLVISHD 218
Cdd:PRK10584 145 AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTgdkiADLLFSLNREHGTTLILVTHD 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-75 |
2.34e-07 |
|
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: 51.00 E-value: 2.34e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQIP 75
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRP 73
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-237 |
2.62e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 52.52 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIhlkkdaavgyltQIPDYH--DSTSTKEV--LKSAFSPLL 95
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTI------------TIAGYHitPETGNKNLkkLRKKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 96 QMEEkmekleAEMGVETdpnKLQKLMgeYGELqdqyaNNGGYEIESNIEKIAH----GLNIQMFIHSPFsQLSGGEKTKV 171
Cdd:PRK13641 92 QFPE------AQLFENT---VLKDVE--FGPK-----NFGFSEDEAKEKALKWlkkvGLSEDLISKSPF-ELSGGQMRRV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 172 GLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
22-237 |
2.67e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.78 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTG-------DIHLKKDAAVG--YLTQI----PDYHDSTSTKEVLK 88
Cdd:PRK13651 26 VSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkDEKNKKKTKEKekVLEKLviqkTRFKKIKKIKEIRR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 89 SA-----FSPLLQMEEKMEKLEA----EMGVetDPNKLQKLMGEYGELQdqyannggyeiesniekiahGLNIQMFIHSP 159
Cdd:PRK13651 106 RVgvvfqFAEYQLFEQTIEKDIIfgpvSMGV--SKEEAKKRAAKYIELV--------------------GLDESYLQRSP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 160 FsQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAV-EWLGSF--LRDYSGTVLVISHDryfLDEVV---NKVIDLE 233
Cdd:PRK13651 164 F-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVkEILEIFdnLNKQGKTIILVTHD---LDNVLewtKRTIFFK 239
|
....
gi 503253044 234 DGEV 237
Cdd:PRK13651 240 DGKI 243
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
337-506 |
2.82e-07 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 52.77 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRIGSNV---------KIGYLSQ- 404
Cdd:COG3839 6 LENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIagLED--PTSGEILIGGRDvtdlppkdrNIAMVFQs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 -----------NIFSSIK----DETVIEtfRDVVNVtegeAR-----HILARfmfygytvfqKVSQLSGGERMRLRLAQL 464
Cdd:COG3839 84 yalyphmtvyeNIAFPLKlrkvPKAEID--RRVREA----AEllgleDLLDR----------KPKQLSGGQRQRVALGRA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 503253044 465 MYQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHD 506
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLgtttIYVTHD 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
20-242 |
2.90e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 52.50 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAA-----------VGYLTQIPDYHDSTSTKEvLK 88
Cdd:PRK13652 21 NNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItkenirevrkfVGLVFQNPDDQIFSPTVE-QD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 89 SAFSPLlqmeekmekleaEMGVETDpnklqklmgeygelqdqyannggyEIESNIEKIAHGLNIQMFIHSPFSQLSGGEK 168
Cdd:PRK13652 100 IAFGPI------------NLGLDEE------------------------TVAHRVSSALHMLGLEELRDRVPHHLSGGEK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 169 TKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRD----YSGTVLVISHDRYFLDEVVNKVIDLEDGEVTTYHT 242
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpetYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
332-506 |
3.02e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 52.43 E-value: 3.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 332 NDVIMLKDISKCF--GDKLLfEGVNMHITYQNRAAIIGENGTGKSTLLkLILQQLF-PDKGEVRI-GSNV---------- 397
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLL-LHLNGIYlPQRGRVKVmGREVnaenekwvrs 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 KIGYLSQN----IFSSIKDETV------IETFRDVVNVTEGEARHILARFMFYGYTVFqkvsQLSGGERMRLRLAQLMYQ 467
Cdd:PRK13647 80 KVGLVFQDpddqVFSSTVWDDVafgpvnMGLDKDEVERRVEEALKAVRMWDFRDKPPY----HLSYGQKKRVAIAGVLAM 155
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503253044 468 DINLLILDEPTNHLDIESREVLEEALEDF--QGSLLAVS-HD 506
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHD 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
336-505 |
3.09e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.95 E-value: 3.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 336 MLK-DISKCFGDKLLfeGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV---------------KI 399
Cdd:PRK11144 1 MLElNFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVlfdaekgiclppekrRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 400 GYLSQ------------NIFSSIKDETViETFRDVVNVTEGEarHILARFmfygytvfqkVSQLSGGERMRLRLAQLMYQ 467
Cdd:PRK11144 79 GYVFQdarlfphykvrgNLRYGMAKSMV-AQFDKIVALLGIE--PLLDRY----------PGSLSGGEKQRVAIGRALLT 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 503253044 468 DINLLILDEPTNHLDI-ESREV---LEEALEDFQGSLLAVSH 505
Cdd:PRK11144 146 APELLLMDEPLASLDLpRKRELlpyLERLAREINIPILYVSH 187
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
364-518 |
3.35e-07 |
|
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: 50.44 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYlsqnifssikdetvietfrdvvNVTEGEARHILARFmfygyt 443
Cdd:cd03227 25 IITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGC----------------------IVAAVSAELIFTRL------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 444 vfqkvsQLSGGERMRLRLAQLM----YQDINLLILDEPTNHLDIESREVLEEALEDF--QGSLLAV-SHDRYfLNKLFDK 516
Cdd:cd03227 77 ------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHlvKGAQVIViTHLPE-LAELADK 149
|
..
gi 503253044 517 IY 518
Cdd:cd03227 150 LI 151
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
332-507 |
3.39e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.64 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 332 NDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV----------KIG 400
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 401 YLSQNifSSIKDETVIETFR---DVVNVTEGEARHI--LARFMFYGYTVFQKVSQLSGGERMR---LRLAQLMYQdinLL 472
Cdd:PRK10247 85 YCAQT--PTLFGDTVYDNLIfpwQIRNQQPDPAIFLddLERFALPDTILTKNIAELSGGEKQRislIRNLQFMPK---VL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 503253044 473 ILDEPTNHLDIESR----EVLEEALEDFQGSLLAVSHDR 507
Cdd:PRK10247 160 LLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDK 198
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
352-510 |
3.47e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.78 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 352 GVNMHITYQNRAAIIGENGTGKSTLLklilQQLFPDKGEVRIGSNVKIGYLSQNIFssikdetvIETFRDVVNVTegear 431
Cdd:cd03238 13 NLDVSIPLNVLVVVTGVSGSGKSTLV----NEGLYASGKARLISFLPKFSRNKLIF--------IDQLQFLIDVG----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 432 hilarfmfYGY-TVFQKVSQLSGGERMRLRLAQLMYQDI--NLLILDEPTNHLDIESREVLEEALEDF--QG-SLLAVSH 505
Cdd:cd03238 76 --------LGYlTLGQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGLidLGnTVILIEH 147
|
....*
gi 503253044 506 DRYFL 510
Cdd:cd03238 148 NLDVL 152
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-234 |
4.00e-07 |
|
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: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEE--TPDTG-----DIHLKKDAAVgyLTQIPDYHDSTSTKEVLKSA 90
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGcvdvpDNQFGREASL--IDAIGRKGDFKDAVELLNAV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 91 fspllqmeekmekleaemgvetdpnklqklmgeygelqdqyannggyeiesniekiahGLNIQMFIHSPFSQLSGGEKTK 170
Cdd:COG2401 123 ----------------------------------------------------------GLSDAVLWLRRFKELSTGQKFR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 171 VGLGLMLLKQPDLLLLDEPTNHLD-LMAVEW---LGSFLRDYSGTVLVISHDryflDEVVNkviDLED 234
Cdd:COG2401 145 FRLALLLAERPKLLVIDEFCSHLDrQTAKRVarnLQKLARRAGITLVVATHH----YDVID---DLQP 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
9-60 |
4.09e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 52.34 E-value: 4.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 503253044 9 VAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK11000 9 VTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL 60
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
357-507 |
4.32e-07 |
|
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: 51.12 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 357 ITYQNRAAIIGENGTGKSTLLKLILQQLFpdkGEVRIGSNVKIGYlsqNIFSSIKDETVI-------------------- 416
Cdd:cd03279 25 LDNNGLFLICGPTGAGKSTILDAITYALY---GKTPRYGRQENLR---SVFAPGEDTAEVsftfqlggkkyrversrgld 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 417 -ETFRDVVNVTEGEARHILARfmfygytvfqKVSQLSGGER------MRLRLAQLMYQD----INLLILDEPTNHLDIES 485
Cdd:cd03279 99 yDQFTRIVLLPQGEFDRFLAR----------PVSTLSGGETflaslsLALALSEVLQNRggarLEALFIDEGFGTLDPEA 168
|
170 180
....*....|....*....|....*
gi 503253044 486 REVLEEALEDFQG---SLLAVSHDR 507
Cdd:cd03279 169 LEAVATALELIRTenrMVGVISHVE 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
9-60 |
4.63e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 52.41 E-value: 4.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 503253044 9 VAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK11432 12 ITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI 63
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
345-496 |
4.72e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 51.73 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 345 GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI------GSNVK-----IGYLSQN----IFSS 409
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepitKENIRevrkfVGLVFQNpddqIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 410 --------------IKDETVIETFRDVVNVTEGEarHILARFMFYgytvfqkvsqLSGGERMRLRLAQLMYQDINLLILD 475
Cdd:PRK13652 95 tveqdiafgpinlgLDEETVAHRVSSALHMLGLE--ELRDRVPHH----------LSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180
....*....|....*....|.
gi 503253044 476 EPTNHLDIESREVLEEALEDF 496
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDL 183
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
5-217 |
5.19e-07 |
|
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: 51.12 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTT-------LIRLLAGEETPDTGDI-----HLKKDAAVGYLT 72
Cdd:TIGR04406 3 VAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTsfymivgLVRPDAGKILIDGQDIthlpmHERARLGIGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 73 QIPDYHDSTSTKEVLKSAFspllqmeEKMEKLEAEmgvetdpnklqklmgeygelqdqyannggyEIESNIEKIAHGLNI 152
Cdd:TIGR04406 83 QEASIFRKLTVEENIMAVL-------EIRKDLDRA------------------------------EREERLEALLEEFQI 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 153 QMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAV---EWLGSFLRDYSGTVLVISH 217
Cdd:TIGR04406 126 SHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVgdiKKIIKHLKERGIGVLITDH 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
346-508 |
5.40e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.62 E-value: 5.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK-------IGYLSQniFSSIK-DETVI 416
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATrgdrsrfMAYLGH--LPGLKaDLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 417 ETFRDVVNVTEGEARHI----LARFMFYGYTVfQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEA 492
Cdd:PRK13543 101 ENLHFLCGLHGRRAKQMpgsaLAIVGLAGYED-TLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRM 179
|
170
....*....|....*....
gi 503253044 493 LEDF---QGSLLAVSHDRY 508
Cdd:PRK13543 180 ISAHlrgGGAALVTTHGAY 198
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
365-526 |
5.99e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 52.49 E-value: 5.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLFPDKGEVRIGsNVKIG------YlsQNIFSSIkdetvietFRDV----------VNVTEG 428
Cdd:COG4615 363 IVGGNGSGKSTLAKLLTGLYRPESGEILLD-GQPVTadnreaY--RQLFSAV--------FSDFhlfdrllgldGEADPA 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 429 EARHILARfmfygytvFQ---KVS---------QLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVL-EEALED 495
Cdd:COG4615 432 RARELLER--------LEldhKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRVFyTELLPE 503
|
170 180 190
....*....|....*....|....*....|....*
gi 503253044 496 F--QG-SLLAVSHD-RYFlnKLFDKIYWIEAKKIH 526
Cdd:COG4615 504 LkaRGkTVIAISHDdRYF--DLADRVLKMDYGKLV 536
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-60 |
6.20e-07 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 51.62 E-value: 6.20e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 1 MIicSVNKVAKMYGGNA----IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:COG1135 1 MI--ELENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV 62
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-224 |
6.29e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.33 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI-----HLKKDAAVgYLTQIPDYHDststkevl 87
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIlferqSIKKDLCT-YQKQLCFVGH-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 88 KSAFSPLLQMEEKMekleaemgvetdpnklqklmgeygeLQDQYANNGGYEIES--NIEKIAHglniqmFIHSPFSQLSG 165
Cdd:PRK13540 82 RSGINPYLTLRENC-------------------------LYDIHFSPGAVGITElcRLFSLEH------LIDYPCGLLSS 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 166 GEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFL---RDYSGTVLVISHDRYFLDE 224
Cdd:PRK13540 131 GQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIqehRAKGGAVLLTSHQDLPLNK 192
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
364-506 |
6.52e-07 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 50.39 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLL---------------KLILQQLFPDKGEVRIGSNVKIGYLS---------------------QNIF 407
Cdd:COG0419 27 LIVGPNGAGKSTILeairyalygkarsrsKLRSDLINVGSEEASVELEFEHGGKRyrierrqgefaefleakpserKEAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 408 SSIKDETVIETFRDVVNVTEGEARHILARF---------MFYGYTVFQKVSQLSGGERMRLRLAQLMYqdinlLILDepT 478
Cdd:COG0419 107 KRLLGLEIYEELKERLKELEEALESALEELaelqklkqeILAQLSGLDPIETLSGGERLRLALADLLS-----LILD--F 179
|
170 180
....*....|....*....|....*...
gi 503253044 479 NHLDIESREVLEEALEdfqgSLLAVSHD 506
Cdd:COG0419 180 GSLDEERLERLLDALE----ELAIITHV 203
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
329-542 |
6.82e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.20 E-value: 6.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 329 RSGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKlILQQLFpDKGEVRIGSNVKIGYLSQNIFS 408
Cdd:PRK14246 5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLK-VLNRLI-EIYDSKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 409 -----------------------SIKDETV-------IETFRDVVNVTEGEARHILARFMFYGyTVFQKVSQLSGGERMR 458
Cdd:PRK14246 83 idaiklrkevgmvfqqpnpfphlSIYDNIAyplkshgIKEKREIKKIVEECLRKVGLWKEVYD-RLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 459 LRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG--SLLAVSHDRYFLNKLFDKIYWI-EAKKIHCFEGN--YT 533
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLyNGELVEWGSSNeiFT 241
|
....*....
gi 503253044 534 WAKEKMTKR 542
Cdd:PRK14246 242 SPKNELTEK 250
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
19-235 |
6.83e-07 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 50.51 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 19 FEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAV-------------------GYLTQ----IP 75
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWvdlaqaspreilalrrrtiGYVSQflrvIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 76 dyhdSTSTKEVLKSafsPLLqmeekmekleaEMGVETDpnklqklmgeygelqdqyannggyEIESNIEKIAHGLNI-QM 154
Cdd:COG4778 107 ----RVSALDVVAE---PLL-----------ERGVDRE------------------------EARARARELLARLNLpER 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 155 FIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDY--SGTVLV-ISHDRYFLDEVVNKVID 231
Cdd:COG4778 145 LWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkaRGTAIIgIFHDEEVREAVADRVVD 224
|
....
gi 503253044 232 LEDG 235
Cdd:COG4778 225 VTPF 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-240 |
7.34e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 51.27 E-value: 7.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAA-----------VGYLTQIPD--YHDST 81
Cdd:PRK13647 17 GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnaenekwvrskVGLVFQDPDdqVFSST 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 82 STKEVlksAFSPLlqmeekmekleaEMGVETDpnklqklmgeygelqdqyannggyEIESNIEKIAHGLNIQMFIHSPFS 161
Cdd:PRK13647 97 VWDDV---AFGPV------------NMGLDKD------------------------EVERRVEEALKAVRMWDFRDKPPY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 162 QLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLD------LMAVEWLgsfLRDYSGTVLVISHDRYFLDEVVNKVIDLEDG 235
Cdd:PRK13647 138 HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDprgqetLMEILDR---LHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
....*
gi 503253044 236 EVTTY 240
Cdd:PRK13647 215 RVLAE 219
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
337-482 |
7.39e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 50.85 E-value: 7.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFG-----DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSnvkigylsqnifssik 411
Cdd:COG1101 4 LKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 412 detvietfRDVVNVTEGE-ARHIlARfmfygytVFQ-------------------------------------------- 446
Cdd:COG1101 68 --------KDVTKLPEYKrAKYI-GR-------VFQdpmmgtapsmtieenlalayrrgkrrglrrgltkkrrelfrell 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 503253044 447 -------------KVSQLSGGERMRLRLaqLM--YQDINLLILDEPTNHLD 482
Cdd:COG1101 132 atlglglenrldtKVGLLSGGQRQALSL--LMatLTKPKLLLLDEHTAALD 180
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-60 |
7.53e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.90 E-value: 7.53e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIICSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI 60
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-63 |
8.15e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 51.84 E-value: 8.15e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:PRK11288 6 SFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID 64
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-223 |
8.29e-07 |
|
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: 50.83 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 27 KEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDihlkkdaavgyltqipdYHDSTSTKEVLKSAFSPLLQmeEKMEKL-E 105
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-----------------FDDPPDWDEILDEFRGSELQ--NYFTKLlE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 106 AEMGVETDPNKLQKL----MGEYGELQDQYANNGgyeiesNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQP 181
Cdd:cd03236 85 GDVKVIVKPQYVDLIpkavKGKVGELLKKKDERG------KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503253044 182 DLLLLDEPTNHLDL---MAVEWLGSFLRDYSGTVLVISHDRYFLD 223
Cdd:cd03236 159 DFYFFDEPSSYLDIkqrLNAARLIRELAEDDNYVLVVEHDLAVLD 203
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
338-506 |
8.67e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 50.69 E-value: 8.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 338 KDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRigsnvkigYLSQNifssikdetviE 417
Cdd:PRK11701 10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH--------YRMRD-----------G 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 418 TFRDVVNVTEGEARHIL--------------------------ARFM-----FYG------YTVFQKV-----------S 449
Cdd:PRK11701 71 QLRDLYALSEAERRRLLrtewgfvhqhprdglrmqvsaggnigERLMavgarHYGdirataGDWLERVeidaariddlpT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 450 QLSGGERMRLRLAQLMYQDINLLILDEPTNHLD--IESR--EVLEEALEDFQGSLLAVSHD 506
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQARllDLLRGLVRELGLAVVIVTHD 211
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-505 |
9.04e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 23 SFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDihlkkdaavgyltqipdyHDSTSTKEVLKSaFSPLLQM-EEKM 101
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGE------------------RQSQFSHITRLS-FEQLQKLvSDEW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 102 EKLEAEMgVETDPNKLQKLMGEYgeLQDQYANNggyeieSNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQP 181
Cdd:PRK10938 84 QRNNTDM-LSPGEDDTGRTTAEI--IQDEVKDP------ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 182 DLLLLDEPTNHLDLMAVEWLGSFLRDYS--GTVLVISHDRYflDEV---VNKVIDLEDGEVTtyhtnftgfvkekeekll 256
Cdd:PRK10938 155 DLLILDEPFDGLDVASRQQLAELLASLHqsGITLVLVLNRF--DEIpdfVQFAGVLADCTLA------------------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 257 kefqayeEQQKKIKKMKEAI-------KRLRDwanrATPPNADlhrrarnmeralermEKLNRPILNrtkmnlemester 329
Cdd:PRK10938 215 -------ETGEREEILQQALvaqlahsEQLEG----VQLPEPD---------------EPSARHALP------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 330 SGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQ----------LFpdkGEVRiGS---- 395
Cdd:PRK10938 256 ANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDhpqgysndltLF---GRRR-GSgeti 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 396 -NVK--IGYLSqnifSSIK-DETVIETFRDVvnvtegearhILARFmFYGYTVFQKVSQ--------------------- 450
Cdd:PRK10938 332 wDIKkhIGYVS----SSLHlDYRVSTSVRNV----------ILSGF-FDSIGIYQAVSDrqqklaqqwldilgidkrtad 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503253044 451 -----LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALE----DFQGSLLAVSH 505
Cdd:PRK10938 397 apfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDvlisEGETQLLFVSH 460
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
13-239 |
9.29e-07 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 50.40 E-value: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYltqipdyhdstSTKEVLKS-AF 91
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISML-----------SSRQLARRlAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 92 SPllqmeekmEKLEAEMGVetdpnKLQKLMgEYGelQDQYANNGGY---EIESNIEKIAHGLNIQMFIHSPFSQLSGGEK 168
Cdd:PRK11231 81 LP--------QHHLTPEGI-----TVRELV-AYG--RSPWLSLWGRlsaEDNARVNQAMEQTRINHLADRRLTDLSGGQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 169 TKVGLGLMLLKQPDLLLLDEPTNHLDL-MAVEWLGSF--LRDYSGTVLVISHD-----RYFLDEVVnkvidLEDGEVTT 239
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDInHQVELMRLMreLNTQGKTVVTVLHDlnqasRYCDHLVV-----LANGHVMA 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
5-226 |
1.03e-06 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 50.47 E-value: 1.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMY----GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL------KKDAAVGYLTQi 74
Cdd:COG1116 9 ELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGVVFQ- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 75 pdyHDS-----TSTKEVlksAFSPLLQMEEKMEKLEaemgvetdpnKLQKLMGEYGeLQDqYANnggyeiesniekiahg 149
Cdd:COG1116 88 ---EPAllpwlTVLDNV---ALGLELRGVPKAERRE----------RARELLELVG-LAG-FED---------------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 150 lniqmfiHSPfSQLSGGEKTKVGL--------GLmllkqpdlLLLDEPTNHLD------LMavEWLGSFLRDYSGTVLVI 215
Cdd:COG1116 134 -------AYP-HQLSGGMRQRVAIaralandpEV--------LLMDEPFGALDaltrerLQ--DELLRLWQETGKTVLFV 195
|
250
....*....|.
gi 503253044 216 SHDryfLDEVV 226
Cdd:COG1116 196 THD---VDEAV 203
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
1.17e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 50.01 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIIcSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKkdaavgylTQIPDYHDS 80
Cdd:COG4161 1 MSI-QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIA--------GHQFDFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 81 TSTKEVLK------SAFS-----PLLQMEEKMekLEAemgvetdPNKLQKLMGEygELQDQyannggyeiesnIEKIAHG 149
Cdd:COG4161 72 PSEKAIRLlrqkvgMVFQqynlwPHLTVMENL--IEA-------PCKVLGLSKE--QAREK------------AMKLLAR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 150 LNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVV 226
Cdd:COG4161 129 LRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIVTHEVEFARKVA 208
|
250
....*....|....
gi 503253044 227 NKVIDLEDGEVTTY 240
Cdd:COG4161 209 SQVVYMEKGRIIEQ 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
14-237 |
1.18e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.45 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEE--TPDTGDIHLKKdaavgyltqipdyHDSTStkevlksaf 91
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKG-------------EDITD--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 92 splLQMEEKmekleAEMGVEtdpnklqklmgeygeLQDQYAnnggYEIEsniekiahGLNIQMFIHSPFSQLSGGEKTKV 171
Cdd:cd03217 69 ---LPPEER-----ARLGIF---------------LAFQYP----PEIP--------GVKNADFLRYVNEGFSGGEKKRN 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 172 GLGLMLLKQPDLLLLDEPTNHLDLMAVEWLG---SFLRDYSGTVLVISHDRYFLDEVV-NKVIDLEDGEV 237
Cdd:cd03217 114 EILQLLLLEPDLAILDEPDSGLDIDALRLVAeviNKLREEGKSVLIITHYQRLLDYIKpDRVHVLYDGRI 183
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
346-506 |
1.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 50.50 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG------SNV-----KIGYLSQN-----IFSS 409
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllteENVwdirhKIGMVFQNpdnqfVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 410 IKDETVIETFRDVVNVTEGEARHILArFMFYGYTVFQK--VSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR- 486
Cdd:PRK13650 99 VEDDVAFGLENKGIPHEEMKERVNEA-LELVGMQDFKErePARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRl 177
|
170 180
....*....|....*....|...
gi 503253044 487 ---EVLEEALEDFQGSLLAVSHD 506
Cdd:PRK13650 178 eliKTIKGIRDDYQMTVISITHD 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
364-518 |
1.31e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEV-RIGSNVKI-----GYLSQNIFSSIKDETV--------IETFRDVVNvteGE 429
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYdEEPSWDEVlkrfrGTELQDYFKKLANGEIkvahkpqyVDLIPKVFK---GT 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 430 ARHILAR------------FMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR----EVLEEAL 493
Cdd:COG1245 180 VRELLEKvdergkldelaeKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRlnvaRLIRELA 259
|
170 180
....*....|....*....|....*
gi 503253044 494 EDFQgSLLAVSHDRYFLNKLFDKIY 518
Cdd:COG1245 260 EEGK-YVLVVEHDLAILDYLADYVH 283
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
352-525 |
1.38e-06 |
|
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: 49.33 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 352 GVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG----SNVKIGYLSQNIFSSIKDETVIetfrdvvnvtE 427
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgidiSTIPLEDLRSSLTIIPQDPTLF----------S 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 428 GEARHILARFMFYG----YTVFqKVSQ----LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEAL-EDFQG 498
Cdd:cd03369 96 GTIRSNLDPFDEYSdeeiYGAL-RVSEgglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTIrEEFTN 174
|
170 180
....*....|....*....|....*...
gi 503253044 499 S-LLAVSHdRYFLNKLFDKIYWIEAKKI 525
Cdd:cd03369 175 StILTIAH-RLRTIIDYDKILVMDAGEV 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
349-506 |
1.46e-06 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 49.78 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 349 LFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVR-IGSNV-------KIGYLSQNIFSSIKDETVIETFR 420
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSlVGQPLhqmdeeaRAKLRAKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 421 DVVNV-------------TEGEARHILARFMFyGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESRE 487
Cdd:PRK10584 105 ALENVelpallrgessrqSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180
....*....|....*....|...
gi 503253044 488 VLEEAL----EDFQGSLLAVSHD 506
Cdd:PRK10584 184 KIADLLfslnREHGTTLILVTHD 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-208 |
1.48e-06 |
|
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: 49.58 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAG--EETPDT-GDI---------HLKKDAaVGYLTQIPDYHDSTSTKE 85
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrvEGGGTTsGQIlfngqprkpDQFQKC-VAYVRQDDILLPGLTVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 86 VLksAFSPLLQMEEKMEKLEAEMGVEtdpnklQKLMGEygelqdqyannggyeiesniekiahgLNIQMFIHSPFSQLSG 165
Cdd:cd03234 101 TL--TYTAILRLPRKSSDAIRKKRVE------DVLLRD--------------------------LALTRIGGNLVKGISG 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 503253044 166 GEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDY 208
Cdd:cd03234 147 GERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL 189
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
364-506 |
1.55e-06 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 49.81 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEV--------RIGS-------NVKIGYLSQnIFSSIKDETVIETFRD---VVNV 425
Cdd:PRK11629 39 AIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsKLSSaakaelrNQKLGFIYQ-FHHLLPDFTALENVAMpllIGKK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 426 TEGEARHiLARFMFYGYTVFQKV----SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDF---QG 498
Cdd:PRK11629 118 KPAEINS-RALEMLAAVGLEHRAnhrpSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnrlQG 196
|
....*....
gi 503253044 499 S-LLAVSHD 506
Cdd:PRK11629 197 TaFLVVTHD 205
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
335-507 |
1.63e-06 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 50.47 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRI-GSNV--------KIGYLS 403
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIagLEH--QTSGHIRFhGTDVsrlhardrKVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 404 QNiFSSIKDETVIEtfrdvvNVTEGeARHILARFMFYGYTVFQKV-----------------SQLSGGERMRLRLAQLMY 466
Cdd:PRK10851 81 QH-YALFRHMTVFD------NIAFG-LTVLPRRERPNAAAIKAKVtqllemvqlahladrypAQLSGGQKQRVALARALA 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 503253044 467 QDINLLILDEPTNHLDIESREVLEEAL----EDFQGSLLAVSHDR 507
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQ 197
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-60 |
1.63e-06 |
|
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: 50.95 E-value: 1.63e-06
10 20 30
....*....|....*....|....*....|....*....
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
344-518 |
1.66e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.01 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEV----RIGSNVKIGYLS-------------QNI 406
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgKPLDYSKRGLLAlrqqvatvfqdpeQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 407 FSSIKDETVIETFRDvVNVTEGE-ARHILARFMFYGYTVF--QKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDI 483
Cdd:PRK13638 91 FYTDIDSDIAFSLRN-LGVPEAEiTRRVDEALTLVDAQHFrhQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 503253044 484 ESREVLEEALEDF--QGSLLAV-SHDRYFLNKLFDKIY 518
Cdd:PRK13638 170 AGRTQMIAIIRRIvaQGNHVIIsSHDIDLIYEISDAVY 207
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
337-554 |
1.67e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 49.64 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI-------------------LQQLFPDKGE------- 390
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaykilegdilfkgesILDLEPEERAhlgifla 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 391 ---------------VRIGSNVKIGYLSQNIFSSIKDETVIETFRDVVNVTEgearHILARFMFYGYtvfqkvsqlSGGE 455
Cdd:CHL00131 90 fqypieipgvsnadfLRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDP----SFLSRNVNEGF---------SGGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 456 RMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDF---QGSLLAVSHDRYFLNklfdkiyWIEAKKIHCFEgny 532
Cdd:CHL00131 157 KKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLmtsENSIILITHYQRLLD-------YIKPDYVHVMQ--- 226
|
250 260
....*....|....*....|..
gi 503253044 533 twaKEKMTKRRESTLQLSLEKK 554
Cdd:CHL00131 227 ---NGKIIKTGDAELAKELEKK 245
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
363-506 |
2.12e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 49.50 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 363 AAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQNIFSSI-KDETVIETF----RDVV-----------NVT 426
Cdd:PRK15056 36 AALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVpQSEEVDWSFpvlvEDVVmmgryghmgwlRRA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 427 EGEARHI----LARFMFYGYTvFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDI--ESREV-LEEALEDFQGS 499
Cdd:PRK15056 116 KKRDRQIvtaaLARVDMVEFR-HRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVktEARIIsLLRELRDEGKT 194
|
....*..
gi 503253044 500 LLAVSHD 506
Cdd:PRK15056 195 MLVSTHN 201
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-63 |
2.20e-06 |
|
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: 48.20 E-value: 2.20e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 503253044 19 FEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD 60
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
332-506 |
2.23e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 49.60 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 332 NDVIMLKDISKCF----GDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNV---------- 397
Cdd:PRK13632 3 NKSVMIKVENVSFsypnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITiskenlkeir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 -KIGYLSQN-----IFSSIKDEtvIETFRDVVNVTEGEARHILarfmfygYTVFQKV----------SQLSGGERMRLRL 461
Cdd:PRK13632 83 kKIGIIFQNpdnqfIGATVEDD--IAFGLENKKVPPKKMKDII-------DDLAKKVgmedyldkepQNLSGGQKQRVAI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 503253044 462 AQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG----SLLAVSHD 506
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKtrkkTLISITHD 202
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
334-493 |
2.34e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.39 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQLFPdkgEVRIGSNVKigYLSQNIFSSIK 411
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNP---EVTITGSIV--YNGHNIYSPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 412 DETVIETFRDVV-------------NVTEG------EARHILARFM---FYGYTVFQKVSQ--------LSGGERMRLRL 461
Cdd:PRK14239 80 DTVDLRKEIGMVfqqpnpfpmsiyeNVVYGlrlkgiKDKQVLDEAVeksLKGASIWDEVKDrlhdsalgLSGGQQQRVCI 159
|
170 180 190
....*....|....*....|....*....|..
gi 503253044 462 AQLMYQDINLLILDEPTNHLDIESREVLEEAL 493
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETL 191
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
364-517 |
2.41e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEvRIGSNVKIGYLS----QNIFS-----------SIKDETVIETFRDVV-NVTE 427
Cdd:PRK10938 33 AFVGANGSGKSALARALAGELPLLSGE-RQSQFSHITRLSfeqlQKLVSdewqrnntdmlSPGEDDTGRTTAEIIqDEVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 428 GEAR-HILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSLLAVShd 506
Cdd:PRK10938 112 DPARcEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV-- 189
|
170
....*....|.
gi 503253044 507 rYFLNKlFDKI 517
Cdd:PRK10938 190 -LVLNR-FDEI 198
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
334-477 |
2.70e-06 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 48.87 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 334 VIMLKDISKCFGDKLLFEGVNMHItyqNRAAII---GENGTGKSTLLKLILQQLFPDKGEVRI-GSNVK----------- 398
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEV---NQGEIVgllGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 IGYLSQNifSSI-KDETV---IETFRDVVNVTEGEARHILARFMfygyTVF-------QKVSQLSGGERMRLRLAQLMYQ 467
Cdd:COG1137 80 IGYLPQE--ASIfRKLTVednILAVLELRKLSKKEREERLEELL----EEFgithlrkSKAYSLSGGERRRVEIARALAT 153
|
170
....*....|
gi 503253044 468 DINLLILDEP 477
Cdd:COG1137 154 NPKFILLDEP 163
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-62 |
2.72e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.86 E-value: 2.72e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 1 MIIcSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK11124 1 MSI-QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNI 61
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
332-525 |
2.92e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.20 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 332 NDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNVKI-----GYLSQ- 404
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINLvrdkdGQLKVa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 -------------------NIFSSIKD-ETVIETFRDVVNVTEGEARHilaRFMFY----GYTVFQKV---SQLSGGERM 457
Cdd:PRK10619 83 dknqlrllrtrltmvfqhfNLWSHMTVlENVMEAPIQVLGLSKQEARE---RAVKYlakvGIDERAQGkypVHLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 458 RLRLAQLMYQDINLLILDEPTNHLDIE-SREVLE--EALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKI 525
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPElVGEVLRimQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-237 |
3.01e-06 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 48.88 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIICSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-KD---------AAVGy 70
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRDitglpphriARLG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 71 LT---QIP----------------DYHDSTSTKEVLKSAFSPLLQMEEKMEKLEAemgvetdpnkLQKLMGeYGELQDQY 131
Cdd:COG0411 81 IArtfQNPrlfpeltvlenvlvaaHARLGRGLLAALLRLPRARREEREARERAEE----------LLERVG-LADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 132 ANNggyeiesniekiahglniqmfihspfsqLSGGEKTKVGLG---------LMllkqpdlllLDEPT---NHLDLMA-V 198
Cdd:COG0411 150 AGN----------------------------LSYGQQRRLEIAralatepklLL---------LDEPAaglNPEETEElA 192
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 503253044 199 EWLGSfLRDYSG-TVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:COG0411 193 ELIRR-LRDERGiTILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-62 |
3.15e-06 |
|
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: 48.52 E-value: 3.15e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV 59
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
6-247 |
3.15e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 49.24 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYGGNAIFE-----EISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI---------HLKK------- 64
Cdd:PRK13645 9 LDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdyaipaNLKKikevkrl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 65 DAAVGYLTQIPDYH--DSTSTKEVlksAFSPLLQMEEKMEKLEaemgvetdpnKLQKLMgEYGELQDQYANnggyeiesn 142
Cdd:PRK13645 89 RKEIGLVFQFPEYQlfQETIEKDI---AFGPVNLGENKQEAYK----------KVPELL-KLVQLPEDYVK--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 143 iekiahglniqmfiHSPFsQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVE-WLGSFLR---DYSGTVLVISHD 218
Cdd:PRK13645 146 --------------RSPF-ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdFINLFERlnkEYKKRIIMVTHN 210
|
250 260
....*....|....*....|....*....
gi 503253044 219 RYFLDEVVNKVIDLEDGEVTTYHTNFTGF 247
Cdd:PRK13645 211 MDQVLRIADEVIVMHEGKVISIGSPFEIF 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
337-497 |
3.16e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKlILQQLFPD---KGEVRI-GSNVKigylsqniFSSIKD 412
Cdd:PRK13549 8 MKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFeGEELQ--------ASNIRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 413 E------------------TVIETFRDVVNVTEG----------EARHILARFMFyGYTVFQKVSQLSGGERMRLRLAQL 464
Cdd:PRK13549 79 TeragiaiihqelalvkelSVLENIFLGNEITPGgimdydamylRAQKLLAQLKL-DINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190
....*....|....*....|....*....|...
gi 503253044 465 MYQDINLLILDEPTNHLDIESREVLEEALEDFQ 497
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLK 190
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
353-510 |
3.20e-06 |
|
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: 48.48 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 353 VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEV---------------RIGSNVKIGYLSQNifSSIKDETVIE 417
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesepsfeatRSRNRYSVAYAAQK--PWLLNATVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 418 --TFRDVVN------VTEGEARHILARFMFYG--YTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE-SR 486
Cdd:cd03290 98 niTFGSPFNkqrykaVTDACSLQPDIDLLPFGdqTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSD 177
|
170 180
....*....|....*....|....*...
gi 503253044 487 EVLEEA----LEDFQGSLLAVSHDRYFL 510
Cdd:cd03290 178 HLMQEGilkfLQDDKRTLVLVTHKLQYL 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
8-241 |
3.32e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 48.72 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 8 KVAKMY-GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTG-------DIHLKKDAAVGYLTQ----IP 75
Cdd:PRK10908 6 HVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGkiwfsghDITRLKNREVPFLRRqigmIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 76 DYHDSTSTKEVLKSAFSPLLQMEEKMEKLEAEMGVETDPnklqklMGeygeLQDQYANnggYEIesniekiahglniqmf 155
Cdd:PRK10908 86 QDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDK------VG----LLDKAKN---FPI---------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 156 ihspfsQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVNKVIDL 232
Cdd:PRK10908 137 ------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTL 210
|
....*....
gi 503253044 233 EDGEVTTYH 241
Cdd:PRK10908 211 SDGHLHGGV 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-63 |
3.34e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.03 E-value: 3.34e-06
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:COG3845 24 VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID 65
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
18-237 |
3.37e-06 |
|
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: 48.62 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAavgyltqIPDYHDSTSTKEVLKSAFSPLLQM 97
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKP-------ISQYEHKYLHSKVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 98 EEKMEKLEAEMGvetdpnklQKLMGEYGELQDqyanngGYEIESNIEKIAHGlnIQMFIHSPFSQLSGGEKTKVGLGLML 177
Cdd:cd03248 102 RSLQDNIAYGLQ--------SCSFECVKEAAQ------KAHAHSFISELASG--YDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 178 LKQPDLLLLDEPTNHLDLMAVEWLGSFLRDY--SGTVLVISHdRYFLDEVVNKVIDLEDGEV 237
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
353-506 |
3.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.06 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 353 VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV--------------KIGYLSQNIFSSIKDETVIE 417
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkklrkKVSLVFQFPEAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 418 tfrDV------VNVTEGEARHILARFMfygytvfQKVS-----------QLSGGERMRLRLAQLMYQDINLLILDEPTNH 480
Cdd:PRK13641 106 ---DVefgpknFGFSEDEAKEKALKWL-------KKVGlsedliskspfELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180
....*....|....*....|....*....
gi 503253044 481 LDIESREVLEEALEDFQG---SLLAVSHD 506
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKaghTVILVTHN 204
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
12-62 |
4.11e-06 |
|
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: 48.70 E-value: 4.11e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 12 MYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTL----IRLLAGEetpdtGDIHL 62
Cdd:cd03289 13 TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTE-----GDIQI 62
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
9-60 |
4.13e-06 |
|
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: 48.45 E-value: 4.13e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 503253044 9 VAKMYGGN-AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:cd03295 6 VTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEI 58
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-60 |
4.46e-06 |
|
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: 48.38 E-value: 4.46e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRI 59
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-237 |
5.27e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.43 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAvgYLTQIPDYHDSTSTK 84
Cdd:PRK10619 7 NVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTI--NLVRDKDGQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 85 EVLKSAFSPL------LQMEEKMEKLEAEMGVETDPNKLQKlmGEYGELQDQYANNGGYEIESNIEKIAHglniqmfihs 158
Cdd:PRK10619 85 NQLRLLRTRLtmvfqhFNLWSHMTVLENVMEAPIQVLGLSK--QEARERAVKYLAKVGIDERAQGKYPVH---------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 159 pfsqLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDlmaVEWLGSFLR------DYSGTVLVISHDRYFLDEVVNKVIDL 232
Cdd:PRK10619 153 ----LSGGQQQRVSIARALAMEPEVLLFDEPTSALD---PELVGEVLRimqqlaEEGKTMVVVTHEMGFARHVSSHVIFL 225
|
....*
gi 503253044 233 EDGEV 237
Cdd:PRK10619 226 HQGKI 230
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-62 |
5.41e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.18 E-value: 5.41e-06
10 20 30
....*....|....*....|....*....|....*...
gi 503253044 25 EIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEW 58
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
335-506 |
5.74e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 48.54 E-value: 5.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFE-----GVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQNIFSS 409
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElkaldNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 410 IKDETVIE--TFRDVVNVTEGEaRHILARFMFYGYTVFQK----------VS---------------------------- 449
Cdd:PRK13651 83 VLEKLVIQktRFKKIKKIKEIR-RRVGVVFQFAEYQLFEQtiekdiifgpVSmgvskeeakkraakyielvgldesylqr 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 450 ---QLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE-SREVLE--EALEDFQGSLLAVSHD 506
Cdd:PRK13651 162 spfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQgVKEILEifDNLNKQGKTIILVTHD 224
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
350-506 |
5.84e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.55 E-value: 5.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 350 FEGVNMHITYQNRAAIIGENGTGKSTLLKLI------LQQLFPDKGEVRIGSNV-----KIGYLSQN-----IFSSIKDE 413
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIdglfeeFEGKVKIDGELLTAENVwnlrrKIGMVFQNpdnqfVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 414 TVIETFRDVVNVTEGEAR---HILARFMFYGYTvfQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR---- 486
Cdd:PRK13642 103 VAFGMENQGIPREEMIKRvdeALLAVNMLDFKT--REPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRqeim 180
|
170 180
....*....|....*....|
gi 503253044 487 EVLEEALEDFQGSLLAVSHD 506
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHD 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
6-237 |
6.38e-06 |
|
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: 47.49 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 6 VNKVAKMYGGNAIFEEISFEikEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKkdaAVGYLTQIPdyhdstSTKE 85
Cdd:cd03298 3 LDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIN---GVDVTAAPP------ADRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 86 VlksafSPLLQMEEKMEKLEAEMGVETDPNKLQKLMGEygelqDQYAnnggyeiesnIEKIAHGLNIQMFIHSPFSQLSG 165
Cdd:cd03298 72 V-----SMLFQENNLFAHLTVEQNVGLGLSPGLKLTAE-----DRQA----------IEVALARVGLAGLEKRLPGELSG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 166 GEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFL----RDYSGTVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:cd03298 132 GERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVldlhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-60 |
6.82e-06 |
|
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: 47.61 E-value: 6.82e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQI 60
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-168 |
6.85e-06 |
|
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: 47.92 E-value: 6.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKD-----------AAVGYLTQIPDYHDSTSTKEV 86
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVdirdlnlrwlrSQIGLVSQEPVLFDGTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 87 LKSAFSPLLQMEEKMEKL-EAEMGVETDPNKLQKLMGEYGelqdqyannggyeiesniekiahglniqmfihspfSQLSG 165
Cdd:cd03249 98 RYGKPDATDEEVEEAAKKaNIHDFIMSLPDGYDTLVGERG-----------------------------------SQLSG 142
|
...
gi 503253044 166 GEK 168
Cdd:cd03249 143 GQK 145
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
5-73 |
7.27e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.80 E-value: 7.27e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQ 73
Cdd:PRK09544 6 SLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ 74
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
22-68 |
7.39e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 7.39e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAV 68
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAAL 89
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-60 |
7.53e-06 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 48.94 E-value: 7.53e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQI 389
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
327-507 |
7.67e-06 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 48.68 E-value: 7.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 327 TERSGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEV--------------- 391
Cdd:PRK11607 12 TRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlshvppyqr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 392 ---------------RIGSNVKIGyLSQNIFSSIKDETVIETFRDVVNVTEGEARhilarfmfygytvfqKVSQLSGGER 456
Cdd:PRK11607 92 pinmmfqsyalfphmTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKR---------------KPHQLSGGQR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 457 MRLRLAQLMYQDINLLILDEPTNHLDIESREVLE----EALEDFQGSLLAVSHDR 507
Cdd:PRK11607 156 QRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQ 210
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
365-493 |
7.69e-06 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 47.93 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLFPDKGEVRI------GSNVKIGYLSQnifssiKDE-----TVIEtfrdvvNVTEG----- 428
Cdd:COG4525 38 ALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVVFQ------KDAllpwlNVLD------NVAFGlrlrg 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 429 --------EARHILARFMFYGYTVfQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEAL 493
Cdd:COG4525 106 vpkaerraRAEELLALVGLADFAR-RRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
353-517 |
7.69e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 48.12 E-value: 7.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 353 VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV------------KIGYLSQNIFSSIKDETVietF 419
Cdd:PRK13637 26 VNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIdGVDItdkkvklsdirkKVGLVFQYPEYQLFEETI---E 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 420 RDV------VNVTEGEARHILARFMF---YGYTVFQKVS--QLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR-E 487
Cdd:PRK13637 103 KDIafgpinLGLSEEEIENRVKRAMNivgLDYEDYKDKSpfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRdE 182
|
170 180 190
....*....|....*....|....*....|...
gi 503253044 488 VLEEAL---EDFQGSLLAVSHDRYFLNKLFDKI 517
Cdd:PRK13637 183 ILNKIKelhKEYNMTIILVSHSMEDVAKLADRI 215
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
344-493 |
8.19e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.53 E-value: 8.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 344 FGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQLFPD---KGEVRI-GSNV------------KIGYLSQ- 404
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrLLELNEEarvEGEVRLfGRNIyspdvdpievrrEVGMVFQy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 -NIFS--SIKDETVIETFRDVVNVTEGEARHILaRFMFYGYTVFQKV--------SQLSGGERMRLRLAQLMYQDINLLI 473
Cdd:PRK14267 94 pNPFPhlTIYDNVAIGVKLNGLVKSKKELDERV-EWALKKAALWDEVkdrlndypSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180
....*....|....*....|
gi 503253044 474 LDEPTNHLDIESREVLEEAL 493
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELL 192
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-481 |
8.34e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 8.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEV------------RIGSNVKIGYL 402
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 403 SQNIfSSIKDETVIETF-------RDV--VNVTEGEARHILARFMF--YGYTVF--QKVSQLSGGERMRLRLAQLMYQDI 469
Cdd:PRK09700 86 YQEL-SVIDELTVLENLyigrhltKKVcgVNIIDWREMRVRAAMMLlrVGLKVDldEKVANLSISHKQMLEIAKTLMLDA 164
|
170
....*....|..
gi 503253044 470 NLLILDEPTNHL 481
Cdd:PRK09700 165 KVIIMDEPTSSL 176
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
346-499 |
9.00e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 346 DKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSN------------VKIGYLSQN--IFS--- 408
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkdinlkwwrSKIGVVSQDplLFSnsi 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 409 ---------SIKDETVIETF--------------------------------------------------RDVVNVTEGE 429
Cdd:PTZ00265 477 knnikyslySLKDLEALSNYynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdSEVVDVSKKV 556
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 430 ARHILARFM--FYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGS 499
Cdd:PTZ00265 557 LIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 628
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
318-507 |
9.72e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 48.02 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 318 TKMNLEMesteRSGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI--LQQlfPDKGEVRIGS 395
Cdd:PRK09452 2 KKLNKQP----SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIagFET--PDSGRIMLDG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 396 nvkigylsqnifssikdetvietfRDVVNVTeGEARHILARFMFYG----YTVF---------QKV-------------- 448
Cdd:PRK09452 76 ------------------------QDITHVP-AENRHVNTVFQSYAlfphMTVFenvafglrmQKTpaaeitprvmealr 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 449 ------------SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHDR 507
Cdd:PRK09452 131 mvqleefaqrkpHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgitfVFVTHDQ 205
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-75 |
1.03e-05 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 48.65 E-value: 1.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAVGYLTQIP 75
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRP 435
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-60 |
1.07e-05 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 47.18 E-value: 1.07e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIICSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI 62
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-75 |
1.14e-05 |
|
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: 46.69 E-value: 1.14e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKdaAVGYLTQIP 75
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEP 75
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
5-114 |
1.23e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI--------HLK--KDAAVG-YLT- 72
Cdd:PRK15439 13 CARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLeiggnpcaRLTpaKAHQLGiYLVp 92
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 503253044 73 QIPDYHDSTSTKEVLKSAFSPLLQMEEKMEKLEAEMGVETDP 114
Cdd:PRK15439 93 QEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDL 134
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
347-482 |
1.31e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 347 KLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRigSNVKIGYLSQ-----------NIFssIKDETV 415
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--AERSIAYVPQqawimnatvrgNIL--FFDEED 748
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 416 IETFRDVVNVTEGEARhiLARFMFYGYT-VFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD 482
Cdd:PTZ00243 749 AARLADAVRVSQLEAD--LAQLGGGLETeIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
353-506 |
1.36e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.47 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 353 VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGS---------------NVKIGYLSQNIFSSIKDETV-- 415
Cdd:PRK13646 26 VNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktkdkyirpvRKRIGMVFQFPESQLFEDTVer 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 416 -IE----TFRDVVNVTEGEARHILARFMFYGYTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLE 490
Cdd:PRK13646 106 eIIfgpkNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVM 185
|
170 180
....*....|....*....|
gi 503253044 491 EALEDFQ----GSLLAVSHD 506
Cdd:PRK13646 186 RLLKSLQtdenKTIILVSHD 205
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
324-394 |
1.37e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 1.37e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 324 MESTERSGNDVIMLKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG 394
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
14-52 |
1.40e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 48.37 E-value: 1.40e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTL----IRLLAGE 52
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLSTE 1272
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-218 |
1.42e-05 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 46.76 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEeTPDTGDIHL---------KKDAAV--GYLTQipdyHDStstkevlksa 90
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLngrplsdwsAAELARhrAYLSQ----QQS---------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 91 fsPLLQMeekmekleaemgvetdpnklqkLMGEYGELQdQYANNGGYEIESNIEKIAHGLNIQMFIHSPFSQLSGGEKTK 170
Cdd:COG4138 80 --PPFAM----------------------PVFQYLALH-QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQR 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 171 VGLG----------------LMllkqpdlllLDEPTNHLDLMAVEWLGSFLRDYS---GTVLVISHD 218
Cdd:COG4138 135 VRLAavllqvwptinpegqlLL---------LDEPMNSLDVAQQAALDRLLRELCqqgITVVMSSHD 192
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-237 |
1.48e-05 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 47.90 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKdaavgylTQIPDYHDSTstkevLKSAFSP 93
Cdd:PRK11160 351 QPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG-------QPIADYSEAA-----LRQAISV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 94 L--------------LQM------EEKMEKLEAEMGVET---DPNKLQKLMGEygelqdqyannGGyeiesniekiahgl 150
Cdd:PRK11160 419 VsqrvhlfsatlrdnLLLaapnasDEALIEVLQQVGLEKlleDDKGLNAWLGE-----------GG-------------- 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 151 niqmfihspfSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLD------LMAVewLGSFLRDysGTVLVISHDRYFLDE 224
Cdd:PRK11160 474 ----------RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDaeterqILEL--LAEHAQN--KTVLMITHRLTGLEQ 539
|
250
....*....|...
gi 503253044 225 vVNKVIDLEDGEV 237
Cdd:PRK11160 540 -FDRICVMDNGQI 551
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-46 |
1.55e-05 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 46.33 E-value: 1.55e-05
10 20 30
....*....|....*....|....*....|...
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLI 46
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLL 47
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
1.67e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 46.78 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIICSVNKVAKMYGGNA----IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL-------------- 62
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtgpgadrgv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 63 --KKDAAVGYLTQIpdyhDSTstkevlksAFSPLLQMEEKMEKLE-AEmgvetdpnKLQKLMGeygeLQDqyannggyei 139
Cdd:COG4525 81 vfQKDALLPWLNVL----DNV--------AFGLRLRGVPKAERRArAE--------ELLALVG----LAD---------- 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 140 esniekiahglniqmFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFL----RDYSGTVLVI 215
Cdd:COG4525 127 ---------------FARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLldvwQRTGKGVFLI 191
|
...
gi 503253044 216 SHD 218
Cdd:COG4525 192 THS 194
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-62 |
1.73e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.15 E-value: 1.73e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503253044 1 MIICSVNKVAKMY-GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWI 63
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-194 |
1.84e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI-----HLKKD-------AAVGYLTQIPDYHdSTSTKE 85
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsHNLKDinlkwwrSKIGVVSQDPLLF-SNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 86 VLKSAFSPLLQMEEKMEKLEaEMGVETDPNK------LQKLMGEYGELQDQYANNGGYEIESNIEKIAHG----LNIQMF 155
Cdd:PTZ00265 479 NIKYSLYSLKDLEALSNYYN-EDGNDSQENKnkrnscRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSevvdVSKKVL 557
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503253044 156 IH---------------SPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLD 194
Cdd:PTZ00265 558 IHdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
324-412 |
2.30e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.18 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 324 MESTERSGNDVIMLKDISKCFGDKLLFEGVNMHItYQNRA-AIIGENGTGKSTLLKLI--LQQLFPD---KGEVRI-GSN 396
Cdd:COG1117 1 MTAPASTLEPKIEVRNLNVYYGDKQALKDINLDI-PENKVtALIGPSGCGKSTLLRCLnrMNDLIPGarvEGEILLdGED 79
|
90 100 110
....*....|....*....|....*....|.
gi 503253044 397 V------------KIGYLSQ--NIF-SSIKD 412
Cdd:COG1117 80 IydpdvdvvelrrRVGMVFQkpNPFpKSIYD 110
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
450-533 |
2.47e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 450 QLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESR----EVLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKKi 525
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQaqilQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR- 234
|
....*...
gi 503253044 526 hCFEGNYT 533
Cdd:PRK15134 235 -CVEQNRA 241
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
17-60 |
2.91e-05 |
|
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: 45.23 E-value: 2.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503253044 17 AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAG--EETPDTGDI 60
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEV 68
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
15-237 |
3.42e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 45.84 E-value: 3.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDA-------------AVGYLTQIPDyhDST 81
Cdd:PRK13639 14 GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPikydkksllevrkTVGIVFQNPD--DQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 82 STKEVLKS-AFSPL---LQMEEKMEKLEaemgvetdpNKLQKLMGEygelqdqyanngGYEiesniEKIAHglniqmfih 157
Cdd:PRK13639 92 FAPTVEEDvAFGPLnlgLSKEEVEKRVK---------EALKAVGME------------GFE-----NKPPH--------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 158 spfsQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYS--GTVLVIS-HDRYFLDEVVNKVIDLED 234
Cdd:PRK13639 137 ----HLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNkeGITIIIStHDVDLVPVYADKVYVMSD 212
|
...
gi 503253044 235 GEV 237
Cdd:PRK13639 213 GKI 215
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-62 |
3.59e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 3.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-62 |
3.77e-05 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 45.85 E-value: 3.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL 60
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-62 |
3.79e-05 |
|
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: 45.10 E-value: 3.79e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI 67
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-237 |
3.82e-05 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 45.37 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIicSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL--------KKDAA----- 67
Cdd:COG1126 1 MI--EIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVdgedltdsKKDINklrrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 68 VGY----------LTQI------PDYHDSTSTKEVLKSAfspllqmeekMEKLEaEMGVetdpnklqklmgeyGELQDQY 131
Cdd:COG1126 79 VGMvfqqfnlfphLTVLenvtlaPIKVKKMSKAEAEERA----------MELLE-RVGL--------------ADKADAY 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 132 annggyeiesniekiahglniqmfihsPfSQLSGGEKTKVGLG--------LMLlkqpdlllLDEPTNHLDlmaVEWLGS 203
Cdd:COG1126 134 ---------------------------P-AQLSGGQQQRVAIAralamepkVML--------FDEPTSALD---PELVGE 174
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 503253044 204 FL---RD--YSG-TVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:COG1126 175 VLdvmRDlaKEGmTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
20-60 |
3.96e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.55 E-value: 3.96e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK15112 30 KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-60 |
4.35e-05 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 45.95 E-value: 4.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 1 MI-ICSVNKVAKMYGGNAI-FEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK11153 1 MIeLKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-237 |
5.12e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.42 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 17 AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLagEETPDTGDIHLKKDAAVGYLTQIPDYHDSTSTKEVLKSAFS---- 92
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVL--NRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQqpnp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 93 -PLLQMEEKMEKLEAEMGVEtDPNKLQKLMgeygelqdqyannggyeiESNIEKIAHGLNIQMFIHSPFSQLSGGEKTKV 171
Cdd:PRK14246 102 fPHLSIYDNIAYPLKSHGIK-EKREIKKIV------------------EECLRKVGLWKEVYDRLNSPASQLSGGQQQRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 172 GLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG--TVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:PRK14246 163 TIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-63 |
5.28e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 46.16 E-value: 5.28e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 503253044 19 FEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD 312
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-240 |
5.61e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 45.38 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 33 GLVGRNGSGKTTLIRLLAGEETPDTGdihlkkdaAVGYLTQIPDYHDSTstkevlksafspLLQMEEKMEKleaemgVET 112
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKG--------AVLWQGKPLDYSKRG------------LLALRQQVAT------VFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 113 DPNklQKLMgeYGELQDQYA---NNGGY---EIESNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLL 186
Cdd:PRK13638 85 DPE--QQIF--YTDIDSDIAfslRNLGVpeaEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 187 DEPTNHLDLMAVEWLGSFLRDYSGT---VLVISHDRYFLDEVVNKVIDLEDGEVTTY 240
Cdd:PRK13638 161 DEPTAGLDPAGRTQMIAIIRRIVAQgnhVIISSHDIDLIYEISDAVYVLRQGQILTH 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
14-60 |
5.84e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.14 E-value: 5.84e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
17-87 |
6.07e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 44.45 E-value: 6.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 17 AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAA--------VGYLTQIPDYHDSTSTKEVL 87
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgdrsrfMAYLGHLPGLKADLSTLENL 103
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
20-247 |
6.97e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 45.23 E-value: 6.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKkDAAVGYLTQIPDYHDSTSTKEV-----LKSAFSPL 94
Cdd:PRK13631 43 NNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG-DIYIGDKKNNHELITNPYSKKIknfkeLRRRVSMV 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 95 LQMEE-KMEKLEAEMGVETDPNKLQKLMGEYGELQDQYANNGGYEiESNIEKiahglniqmfihSPFsQLSGGEKTKVGL 173
Cdd:PRK13631 122 FQFPEyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD-DSYLER------------SPF-GLSGGQKRRVAI 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 174 GLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG---TVLVISHDRYFLDEVVNKVIDLEDGEVTTYHTNFTGF 247
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnnkTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIF 264
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
353-532 |
7.00e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 353 VNMHITYQNRAAIIGENGTGKSTLLKLILQQLFP-DKGEVRIGSNVkiGYLSQN--IFSSIKDETVI-------ETFRDV 422
Cdd:PLN03232 636 INLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaETSSVVIRGSV--AYVPQVswIFNATVRENILfgsdfesERYWRA 713
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 423 VNVTEgeARHILARFMFYGYT-VFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIE-SREVLEEALED-FQG- 498
Cdd:PLN03232 714 IDVTA--LQHDLDLLPGRDLTeIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDeLKGk 791
|
170 180 190
....*....|....*....|....*....|....
gi 503253044 499 SLLAVSHDRYFLnKLFDKIYWIEAKKIHcFEGNY 532
Cdd:PLN03232 792 TRVLVTNQLHFL-PLMDRIILVSEGMIK-EEGTF 823
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-62 |
8.75e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.82 E-value: 8.75e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPD--------TGDIHL 62
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTL 68
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
8-60 |
9.31e-05 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 44.31 E-value: 9.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 503253044 8 KVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDL 58
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
351-525 |
9.33e-05 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 44.02 E-value: 9.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 351 EGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRI-GSNV-KIG--YLSQNIfSSIKDETVIE--TFRDvvN 424
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDIsKIGlhDLRSRI-SIIPQDPVLFsgTIRS--N 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 425 V------TEGEARHILARFMFYGYTVFQKV----------SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREV 488
Cdd:cd03244 98 LdpfgeySDEELWQALERVGLKEFVESLPGgldtvveeggENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDAL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 503253044 489 LEEAL-EDFQGS-LLAVSHdRyfLNKL--FDKIYWIEAKKI 525
Cdd:cd03244 178 IQKTIrEAFKDCtVLTIAH-R--LDTIidSDRILVLDKGRV 215
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-62 |
1.01e-04 |
|
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: 42.75 E-value: 1.01e-04
10 20 30
....*....|....*....|....*....|....
gi 503253044 29 KERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY 35
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-63 |
1.10e-04 |
|
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: 44.66 E-value: 1.10e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAG---EETPDTGDIHLK 63
Cdd:COG0444 24 VSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFD 68
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-245 |
1.16e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 19 FEEISFEIKEKERVgLVGRNGSGKTTLIRLLA------GEETPDTGDIHLKKDAAV----------GYLTQIPDYHDSTS 82
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRlllgpsSSRKFDEEDFYLGDDPDLpeieieltfgSLLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 83 TKEVLKSAFspllqmEEKMEKLEAEMgvetdpNKLQKLMGEYGElqdQYANNGGYEIE---SNIEKIAHGLNIQMF--IH 157
Cdd:COG3593 93 DKEELEEAL------EELNEELKEAL------KALNELLSEYLK---ELLDGLDLELElslDELEDLLKSLSLRIEdgKE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 158 SPFSQLSGGEKTKVGLGLMLLKQPDLLLL-------DEPTNHLDLMAVEWLGSFLRDYSGT---VLVISHDRYFLDEV-V 226
Cdd:COG3593 158 LPLDRLGSGFQRLILLALLSALAELKRAPanpilliEEPEAHLHPQAQRRLLKLLKELSEKpnqVIITTHSPHLLSEVpL 237
|
250
....*....|....*....
gi 503253044 227 NKVIDLEDGEVTTYHTNFT 245
Cdd:COG3593 238 ENIRRLRRDSGGTTSTKLI 256
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-237 |
1.21e-04 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 44.23 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 3 ICSVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIR----LLAGEETPDT----------------GDIHl 62
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellgrtvqregrlaRDIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 63 KKDAAVGYLTQIPDYHDSTSTKE-VLKSAF--SPLLQMeekmekleaemgvetdpnklqkLMGEYGELQDQYANNGGYEI 139
Cdd:PRK09984 83 KSRANTGYIFQQFNLVNRLSVLEnVLIGALgsTPFWRT----------------------CFSWFTREQKQRALQALTRV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 140 esnieKIAHglniqmFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG----TVLVI 215
Cdd:PRK09984 141 -----GMVH------FAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndgiTVVVT 209
|
250 260
....*....|....*....|..
gi 503253044 216 SHDRYFLDEVVNKVIDLEDGEV 237
Cdd:PRK09984 210 LHQVDYALRYCERIVALRQGHV 231
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-51 |
1.25e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 45.22 E-value: 1.25e-04
10 20 30
....*....|....*....|....*....|
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAG 51
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG 398
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-237 |
1.25e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 44.36 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 3 ICSVNKVAKMYGGNAIF--EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHlkkdaavgYLTQIPDYHDS 80
Cdd:PRK13648 7 IIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIF--------YNNQAITDDNF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 81 TSTKEVLKSAF-SPLLQMEEKMEKLEAEMGVETDpnklqklMGEYGELQDQYAnnggyEIESNIEKIAHGlniqmfIHSP 159
Cdd:PRK13648 79 EKLRKHIGIVFqNPDNQFVGSIVKYDVAFGLENH-------AVPYDEMHRRVS-----EALKQVDMLERA------DYEP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 160 FSqLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLR----DYSGTVLVISHDryfLDEVV--NKVIDLE 233
Cdd:PRK13648 141 NA-LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRkvksEHNITIISITHD---LSEAMeaDHVIVMN 216
|
....
gi 503253044 234 DGEV 237
Cdd:PRK13648 217 KGTV 220
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-49 |
1.30e-04 |
|
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: 43.76 E-value: 1.30e-04
10 20 30
....*....|....*....|....*....|....*
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLL 49
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLL 47
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-80 |
1.36e-04 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 45.39 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 3 ICSVNKVAKMYGGNA--IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLkkdAAVGYLTQIPDYHDS 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV---AGKSILTNISDVHQN 2013
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-60 |
1.50e-04 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.95 E-value: 1.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-218 |
1.74e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 43.62 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 33 GLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAavgyltqIPDYHDSTSTKEVlksAFSPllqmeekmEKLEAEMGVet 112
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQP-------LESWSSKAFARKV---AYLP--------QQLPAAEGM-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 113 dpnKLQKL--MGEY---GELqdqyaNNGGYEIESNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVGLGLMLLKQPDLLLLD 187
Cdd:PRK10575 101 ---TVRELvaIGRYpwhGAL-----GRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLD 172
|
170 180 190
....*....|....*....|....*....|....*
gi 503253044 188 EPTNHLDLM-AVEWLG---SFLRDYSGTVLVISHD 218
Cdd:PRK10575 173 EPTSALDIAhQVDVLAlvhRLSQERGLTVIAVLHD 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
13-242 |
1.90e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 43.95 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEeISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL----------KKD-----AAVGYLTQIPDY 77
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskQKEikpvrKKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 78 H--DSTSTKEVlksAFSP--LLQMEEKMEKLEAEmgvetdpnKLQKLmgeygelqdqyannggyeiesniekiahGLNIQ 153
Cdd:PRK13643 96 QlfEETVLKDV---AFGPqnFGIPKEKAEKIAAE--------KLEMV----------------------------GLADE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 154 MFIHSPFsQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMA-VEWLGSF--LRDYSGTVLVISHDRYFLDEVVNKVI 230
Cdd:PRK13643 137 FWEKSPF-ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTHLMDDVADYADYVY 215
|
250
....*....|..
gi 503253044 231 DLEDGEVTTYHT 242
Cdd:PRK13643 216 LLEKGHIISCGT 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-62 |
1.94e-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: 1.94e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTL----IRLLAGEetpdtGDIHL 62
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLglalLRLIPSE-----GEIRF 344
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
18-66 |
2.31e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 42.74 E-value: 2.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGD-IHLKKDA 66
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEGDfIGLRGDA 51
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-237 |
2.43e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 44.33 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 17 AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTG-------DI-HLKKDAavgyLTQIPDYHdststkevlk 88
Cdd:PRK10535 22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVaTLDADA----LAQLRREH---------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 89 saFSPLLQMEEKMEKLEAEMGVEtdpnklqklmgeygeLQDQYANNGGYEIESNIEKIAHGLNIQMFIHSPFSQLSGGEK 168
Cdd:PRK10535 88 --FGFIFQRYHLLSHLTAAQNVE---------------VPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 169 TKVGLGLMLLKQPDLLLLDEPTNHLD------LMAVewLGSfLRDYSGTVLVISHDRYFLDEvVNKVIDLEDGEV 237
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDshsgeeVMAI--LHQ-LRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-237 |
2.48e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 44.33 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL--------------KKDAAVGyltQIPDYHDSTST 83
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLdgvplvqydhhylhRQVALVG---QEPVLFSGSVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 84 KEVLKS-AFSPLLQMEEKMEKLEAEMGVETDPNKLQKLMGEYGelqdqyannggyeiesniekiahglniqmfihspfSQ 162
Cdd:TIGR00958 573 ENIAYGlTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKG-----------------------------------SQ 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 163 LSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSGTVLVISHdRYFLDEVVNKVIDLEDGEV 237
Cdd:TIGR00958 618 LSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH-RLSTVERADQILVLKKGSV 691
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-237 |
2.49e-04 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 42.82 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 1 MIICsvNKVAKMYGGNAIfeEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK-KDaavgyLTQIPDYhd 79
Cdd:COG3840 1 MLRL--DDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgQD-----LTALPPA-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 80 ststkevlKSAFSPLLQmeekmE-KLEAEMGVET------DPN-KL---QKlmgeygelqdqyannggyeieSNIEKIAH 148
Cdd:COG3840 70 --------ERPVSMLFQ-----EnNLFPHLTVAQniglglRPGlKLtaeQR---------------------AQVEQALE 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 149 GLNIQMFIHSPFSQLSGGEKTKVGLG----------LMllkqpdllllDEPTNHLD--LMA--VEWLGSFLRDYSGTVLV 214
Cdd:COG3840 116 RVGLAGLLDRLPGQLSGGQRQRVALArclvrkrpilLL----------DEPFSALDpaLRQemLDLVDELCRERGLTVLM 185
|
250 260
....*....|....*....|....*.
gi 503253044 215 ISHDryfLDEVV---NKVIDLEDGEV 237
Cdd:COG3840 186 VTHD---PEDAAriaDRVLLVADGRI 208
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
444-510 |
2.58e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 2.58e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 444 VFQKVSQLSGGERM------RLRLAQLMYQDINLLILDEPTNHLDIESR----EVLEEALEDFQG--SLLAVSHDRYFL 510
Cdd:PRK01156 795 MVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRtnlkDIIEYSLKDSSDipQVIMISHHRELL 873
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-63 |
2.81e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 2.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 5 SVNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITIN 65
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
335-525 |
3.02e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 43.07 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDKLLFE-----GVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSnvkigylsQNIFSS 409
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEfkalnNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGD--------YAIPAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 410 IKDETVIETFRdvvnvtegeaRHILARFMFYGYTVFQKVSQ--------------------------------------- 450
Cdd:PRK13645 79 LKKIKEVKRLR----------KEIGLVFQFPEYQLFQETIEkdiafgpvnlgenkqeaykkvpellklvqlpedyvkrsp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 451 --LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESRE----VLEEALEDFQGSLLAVSHDRYFLNKLFDKIYWIEAKK 524
Cdd:PRK13645 149 feLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfinLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGK 228
|
.
gi 503253044 525 I 525
Cdd:PRK13645 229 V 229
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-237 |
3.23e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 43.05 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDaavgyltQIPDYhdstSTKEVLKSAfs 92
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE-------HIQHY----ASKEVARRI-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 93 pllqmeekmeKLEAEMGVETDPNKLQKLMGEYGELQDQYANNGGYEIESNIEKIAHGLNIQMFIHSPFSQLSGGEKTKVG 172
Cdd:PRK10253 84 ----------GLLAQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503253044 173 LGLMLLKQPDLLLLDEPTNHLDLM----AVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDIShqidLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKI 222
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
335-490 |
4.21e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 42.76 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 335 IMLKDISKCFGDK------LlfEGVNMHItyqNRA---AIIGENGTGKSTLLKLI--LQQlfPDKGEVRI-GSNV----- 397
Cdd:COG1135 2 IELENLSKTFPTKggpvtaL--DDVSLTI---EKGeifGIIGYSGAGKSTLIRCInlLER--PTSGSVLVdGVDLtalse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 398 --------KIGYLSQ--NIFSSikdETVIEtfrdvvNV--------TEGEARHilarfmfygytvfQKV----------- 448
Cdd:COG1135 75 relraarrKIGMIFQhfNLLSS---RTVAE------NValpleiagVPKAEIR-------------KRVaellelvglsd 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 449 ------SQLSGGERMRL---R-LAqlmyqdiN---LLILDEPTNHLDIES-REVLE 490
Cdd:COG1135 133 kadaypSQLSGGQKQRVgiaRaLA-------NnpkVLLCDEATSALDPETtRSILD 181
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-49 |
4.52e-04 |
|
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: 43.27 E-value: 4.52e-04
10 20 30
....*....|....*....|....*....|..
gi 503253044 18 IFEEISFEIKEKERVGLVGRNGSGKTTLIRLL 49
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
14-237 |
5.08e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 41.98 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAG--EETPDTGDIHLK-KD---------AAVG------YLTQIP 75
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDgEDilelspderARAGiflafqYPVEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 76 dyhdSTSTKEVLKSAfspllqmeeKMEKLEAEMGVETDPNKLQKLMGEYG---ELQDQYANNGgyeiesniekiahglni 152
Cdd:COG0396 91 ----GVSVSNFLRTA---------LNARRGEELSAREFLKLLKEKMKELGldeDFLDRYVNEG----------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 153 qmfihspfsqLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLG---SFLRDYSGTVLVISHDRYFLDEVV-NK 228
Cdd:COG0396 141 ----------FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAegvNKLRSPDRGILIITHYQRILDYIKpDF 210
|
....*....
gi 503253044 229 VIDLEDGEV 237
Cdd:COG0396 211 VHVLVDGRI 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-63 |
5.24e-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: 43.13 E-value: 5.24e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKT----TLIRLLAGEETPDTGDIHLK 63
Cdd:COG4172 29 VSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFD 74
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
14-62 |
5.52e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.78 E-value: 5.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK10790 352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL 400
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-62 |
5.69e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.88 E-value: 5.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 503253044 23 SFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHL 62
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL 58
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
443-483 |
5.92e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 5.92e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 503253044 443 TVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDI 483
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDV 437
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
364-482 |
6.57e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 42.73 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDkgeVRIGSNVKI--------------GYLSQ-NIFssIKDETVIET------FRDV 422
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKG---VKGSGSVLLngmpidakemraisAYVQQdDLF--IPTLTVREHlmfqahLRMP 129
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 423 VNVTEGEARHIL-----------ARFMFYGytVFQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD 482
Cdd:TIGR00955 130 RRVTKKEKRERVdevlqalglrkCANTRIG--VPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-95 |
6.93e-04 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 41.07 E-value: 6.93e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 34 LVGRNGSGKTTLIRLLAGEETPD--TGDIHL---KKDAA----VGYLTQIpDYHDSTST-KEVLKsaFSPLL 95
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGRKTAGviTGEILIngrPLDKNfqrsTGYVEQQ-DVHSPNLTvREALR--FSALL 106
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
17-237 |
8.48e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 41.71 E-value: 8.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 17 AIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGD--------IHLKKDAA------VGYLTQIPD--YHDS 80
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskitvdgITLTAKTVwdirekVGIVFQNPDnqFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 81 TSTKEV---LKSAFSPLLQMEEKMEKLEAEMGvetdpnklqklMGEYGELQDQYannggyeiesniekiahglniqmfih 157
Cdd:PRK13640 101 TVGDDVafgLENRAVPRPEMIKIVRDVLADVG-----------MLDYIDSEPAN-------------------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 158 spfsqLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAVEWLGSFLRDYSG----TVLVISHDryfLDEVV--NKVID 231
Cdd:PRK13640 144 -----LSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHD---IDEANmaDQVLV 215
|
....*.
gi 503253044 232 LEDGEV 237
Cdd:PRK13640 216 LDDGKL 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
13-63 |
9.02e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 41.51 E-value: 9.02e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 503253044 13 YGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:PRK11300 15 FGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLR 65
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
15-63 |
9.66e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 41.51 E-value: 9.66e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVS 62
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
354-489 |
1.13e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.63 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 354 NMHITYQNRAA--IIGENGTGKSTLLKLILQQLFPDKGEVRIgSNVKI--------GYLSQNIfsSIKDE-TVIETFR-- 420
Cdd:PRK13541 18 DLSITFLPSAItyIKGANGCGKSSLLRMIAGIMQPSSGNIYY-KNCNInniakpycTYIGHNL--GLKLEmTVFENLKfw 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503253044 421 -DVVNVTEgearHILARFMFYGYTVF--QKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVL 489
Cdd:PRK13541 95 sEIYNSAE----TLYAAIHYFKLHDLldEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
364-505 |
1.36e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 41.44 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKlIL---QQlfPDKGEVRIGSNvkigylsQNIFSSIKDE------------------TVIE----- 417
Cdd:PRK11288 34 ALMGENGAGKSTLLK-ILsgnYQ--PDAGSILIDGQ-------EMRFASTTAAlaagvaiiyqelhlvpemTVAEnlylg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 418 ---TFRDVVNVTE--GEARHILARFmfyGYTV--FQKVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLdiESREV-- 488
Cdd:PRK11288 104 qlpHKGGIVNRRLlnYEAREQLEHL---GVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL--SAREIeq 178
|
170 180
....*....|....*....|
gi 503253044 489 ---LEEALEDFQGSLLAVSH 505
Cdd:PRK11288 179 lfrVIRELRAEGRVILYVSH 198
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
36-240 |
1.50e-03 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 41.01 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 36 GRNGSGKTTLIRLLAGEETPDTGDIHLKK----DAA-----------VGYLTQ----IPDYhdstSTKEVLKSAFSPllQ 96
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfDAEkgiclppekrrIGYVFQdarlFPHY----KVRGNLRYGMAK--S 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 97 MEEKMEKLEAEMGVEtdpnklqKLMGEYgelqdqyannggyeiesniekiahglniqmfihsPFSqLSGGEKTKVGLG-- 174
Cdd:PRK11144 105 MVAQFDKIVALLGIE-------PLLDRY----------------------------------PGS-LSGGEKQRVAIGra 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 175 --------LMllkqpdllllDEPTNHLDLMAVEWLGSFLRDYSGTV----LVISHDryfLDEVV---NKVIDLEDGEVTT 239
Cdd:PRK11144 143 lltapellLM----------DEPLASLDLPRKRELLPYLERLAREInipiLYVSHS---LDEILrlaDRVVVLEQGKVKA 209
|
.
gi 503253044 240 Y 240
Cdd:PRK11144 210 F 210
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-46 |
1.73e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.69 E-value: 1.73e-03
10 20
....*....|....*....|....*
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLI 46
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLL 1353
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
162-506 |
2.04e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.99 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 162 QLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDL----MAVEWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGEV 237
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVtiqaQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 238 TTyhtnfTGFVkekeeklLKEFQAyeEQQKKIKKMKEAIKRLRDWANRATP---PNADLHRRARNMERALERMEKLNRPI 314
Cdd:PRK10261 248 VE-----TGSV-------EQIFHA--PQHPYTRALLAAVPQLGAMKGLDYPrrfPLISLEHPAKQEPPIEQDTVVDGEPI 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 315 LNrtKMNLEMESTERSGndviMLKDISKcfgDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEV--- 391
Cdd:PRK10261 314 LQ--VRNLVTRFPLRSG----LLNRVTR---EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifn 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 392 --RIG--SNVKIGYLSQNIFSSIKD------------ETVIETFRdVVNVTEGEARH-----ILARFMFYGYTVFQKVSQ 450
Cdd:PRK10261 385 gqRIDtlSPGKLQALRRDIQFIFQDpyasldprqtvgDSIMEPLR-VHGLLPGKAAAarvawLLERVGLLPEHAWRYPHE 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 451 LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQGSL----LAVSHD 506
Cdd:PRK10261 464 FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHD 523
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
337-511 |
2.07e-03 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 40.05 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLIL----------QQLFpdKGE---------------- 390
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghpkyevtsgSILL--DGEdilelspderaragif 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 391 ------VRIgSNVKIGYLSQNIFSSIKDETV-IETFRDVVNVTEGE---ARHILARFMFYGytvfqkvsqLSGGERMRLR 460
Cdd:COG0396 81 lafqypVEI-PGVSVSNFLRTALNARRGEELsAREFLKLLKEKMKElglDEDFLDRYVNEG---------FSGGEKKRNE 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 503253044 461 LAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG---SLLAVSHDRYFLN 511
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRILD 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-61 |
2.11e-03 |
|
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: 40.96 E-value: 2.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 503253044 6 VNKVAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDT--GDIH 61
Cdd:TIGR02633 4 MKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIY 61
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
337-494 |
3.08e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 337 LKDISKCF-GDKLLfEGVNMHITYQNRAAIIGENGTGKSTLLKlILQQLFPD---------KGEVRIGSNVK-------- 398
Cdd:NF040905 4 MRGITKTFpGVKAL-DDVNLSVREGEIHALCGENGAGKSTLMK-VLSGVYPHgsyegeilfDGEVCRFKDIRdsealgiv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 399 --------IGYLS--QNIF--SSIKDETVIETfrdvvNVTEGEARHILARfmfygytV------FQKVSQLSGGERMRLR 460
Cdd:NF040905 82 iihqelalIPYLSiaENIFlgNERAKRGVIDW-----NETNRRARELLAK-------VgldespDTLVTDIGVGKQQLVE 149
|
170 180 190
....*....|....*....|....*....|....*
gi 503253044 461 LAQLMYQDINLLILDEPTNHL-DIESREVLEEALE 494
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALnEEDSAALLDLLLE 184
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-52 |
3.31e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 3.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 503253044 14 GGNAIFEEISFEIKEKERVGLVGRNGSGKTT----LIRLLAGE 52
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ 339
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-237 |
3.44e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 39.69 E-value: 3.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK----KDA--------AVGYLTQIPDYHDSTSTKEVl 87
Cdd:PRK13633 27 DDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtSDEenlwdirnKAGMVFQNPDNQIVATIVEE- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 88 KSAFSPllqmeekmEKLeaemGVETDpnklqklmgeygelqdqyannggyEIESNIEKIAHGLNIQMFIHSPFSQLSGGE 167
Cdd:PRK13633 106 DVAFGP--------ENL----GIPPE------------------------EIRERVDESLKKVGMYEYRRHAPHLLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503253044 168 KTKVGLGLMLLKQPDLLLLDEPTNHLD----LMAVEWLGSFLRDYSGTVLVISHdryFLDEVV--NKVIDLEDGEV 237
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAVeaDRIIVMDSGKV 222
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
449-506 |
3.55e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 40.46 E-value: 3.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 449 SQLSGGERMRLRLAQLMYQDINLLILDEPTNHLDiesREVLEEAL-------EDFQGSLLAVSHD 506
Cdd:PRK15134 424 AEFSGGQRQRIAIARALILKPSLIILDEPTSSLD---KTVQAQILallkslqQKHQLAYLFISHD 485
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
339-482 |
3.95e-03 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 40.25 E-value: 3.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 339 DISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIGSN---------VKIGYLSQN---- 405
Cdd:PLN03211 73 DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANnrkptkqilKRTGFVTQDdily 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 406 ---------IFSSI--------KDE--TVIETFRDVVNVTEGEARHILARFmfygytvfqkVSQLSGGERMRLRLAQLMY 466
Cdd:PLN03211 153 phltvretlVFCSLlrlpksltKQEkiLVAESVISELGLTKCENTIIGNSF----------IRGISGGERKRVSIAHEML 222
|
170
....*....|....*.
gi 503253044 467 QDINLLILDEPTNHLD 482
Cdd:PLN03211 223 INPSLLILDEPTSGLD 238
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-237 |
4.18e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 39.45 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIH-------------LKKDAAVGYLTQIPDyHDST 81
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILfdgkpidysrkglMKLRESVGMVFQDPD-NQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 82 STKEVLKSAFSPL-LQMEEKmekleaemgvetdpnklqklmgeygelqdqyannggyEIESNIEKIAHGLNIQMFIHSPF 160
Cdd:PRK13636 97 SASVYQDVSFGAVnLKLPED-------------------------------------EVRKRVDNALKRTGIEHLKDKPT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 161 SQLSGGEKTKVGLGLMLLKQPDLLLLDEPTNHLDLMAV----EWLGSFLRDYSGTVLVISHDRYFLDEVVNKVIDLEDGE 236
Cdd:PRK13636 140 HCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVseimKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
.
gi 503253044 237 V 237
Cdd:PRK13636 220 V 220
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
20-235 |
4.25e-03 |
|
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: 39.37 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDaavgyltQI----PDyhdststKEVLKSAFSPLL 95
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-------QItepgPD-------RMVVFQNYSLLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 96 QMEEKMEKLEAEMGVETDPNKlqklmGEYGELqdqyannggyeIESNIEKIahglNIQMFIHSPFSQLSGGEKTKVGLGL 175
Cdd:TIGR01184 68 WLTVRENIALAVDRVLPDLSK-----SERRAI-----------VEEHIALV----GLTEAADKRPGQLSGGMKQRVAIAR 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503253044 176 MLLKQPDLLLLDEPTNHLDLMAVEWLGSFL----RDYSGTVLVISHDryfLDEVV---NKVIDLEDG 235
Cdd:TIGR01184 128 ALSIRPKVLLLDEPFGALDALTRGNLQEELmqiwEEHRVTVLMVTHD---VDEALllsDRVVMLTNG 191
|
|
| YeeP |
COG3596 |
Predicted GTPase [General function prediction only]; |
31-60 |
4.27e-03 |
|
Predicted GTPase [General function prediction only];
Pssm-ID: 442815 [Multi-domain] Cd Length: 318 Bit Score: 39.75 E-value: 4.27e-03
10 20 30
....*....|....*....|....*....|
gi 503253044 31 RVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:COG3596 41 VIALVGKTGAGKSSLINALFGAEVAEVGVG 70
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
365-482 |
4.54e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 38.78 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLfpdKGEVRIGSNVKIG----------YLSQNIFSSIKDE-----TVIETFRDVVNVTEGE 429
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRT---EGNVSVEGDIHYNgipykefaekYPGEIIYVSEEDVhfptlTVRETLDFALRCKGNE 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 503253044 430 ArhilarfmfygytvfqkVSQLSGGERMRLRLAQLMYQDINLLILDEPTNHLD 482
Cdd:cd03233 115 F-----------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
336-380 |
4.69e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 39.64 E-value: 4.69e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 503253044 336 MLKDIS----KCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLI 380
Cdd:COG1106 1 MLISFSienfRSFKDELTLSMVASGLRLLRVNLIYGANASGKSNLLEAL 49
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-60 |
4.90e-03 |
|
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: 39.45 E-value: 4.90e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 503253044 15 GNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDI 60
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI 94
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
364-393 |
4.98e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 39.39 E-value: 4.98e-03
10 20 30
....*....|....*....|....*....|
gi 503253044 364 AIIGENGTGKSTLLKLILQQLFPDKGEVRI 393
Cdd:PRK15112 43 AIIGENGSGKSTLAKMLAGMIEPTSGELLI 72
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-68 |
5.57e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 39.03 E-value: 5.57e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 503253044 20 EEISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLKKDAAV 68
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSV 89
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
9-51 |
5.85e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.53 E-value: 5.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 503253044 9 VAKMYGGNAIFEEISFEIKEKERVGLVGRNGSGKTTLIRLLAG 51
Cdd:PRK13549 11 ITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
338-506 |
5.87e-03 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 38.72 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 338 KDISKCFGDKLLFEGVNMHITYQNRAAIIGENGTGKSTLLKLILQQLFPDKGEVRIG------------SNVKIGYLSQ- 404
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisllplharARRGIGYLPQe 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 405 -NIFS--SIKDETV-IETFRDVVNVTEGEARHILARFMFYGYTVFQKVSQ-LSGGERMRLRLAQLMYQDINLLILDEPTN 479
Cdd:PRK10895 87 aSIFRrlSVYDNLMaVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQsLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190
....*....|....*....|....*....|.
gi 503253044 480 HLD----IESREVLEEaLEDFQGSLLAVSHD 506
Cdd:PRK10895 167 GVDpisvIDIKRIIEH-LRDSGLGVLITDHN 196
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
19-50 |
6.15e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.83 E-value: 6.15e-03
10 20 30
....*....|....*....|....*....|...
gi 503253044 19 FEEISFEIKEKERVG-LVGRNGSGKTTLIRLLA 50
Cdd:COG3950 14 FEDLEIDFDNPPRLTvLVGENGSGKTTLLEAIA 46
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
365-476 |
7.30e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 39.49 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503253044 365 IIGENGTGKSTLLKLILQQLFPDKGEVRIGSNVKIGYLSQNIFSSIKDETVIETFRDVVNVTEGEARHILAR---FMFYG 441
Cdd:PRK13545 55 IIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEiieFADIG 134
|
90 100 110
....*....|....*....|....*....|....*
gi 503253044 442 YTVFQKVSQLSGGERMRLRLAQLMYQDINLLILDE 476
Cdd:PRK13545 135 KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
451-506 |
7.51e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 39.28 E-value: 7.51e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503253044 451 LSGGERMRL----RLAQLMYQ--DINLLILDEPTNHLDIESREVLEEALEDFQGSL---LAVSHD 506
Cdd:PRK03918 789 LSGGERIALglafRLALSLYLagNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIpqvIIVSHD 853
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
451-517 |
8.70e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 8.70e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503253044 451 LSGGERMRLRLAQLMYQDINLLILDEPTNHLDIESREVLEEALEDFQG----SLLAVSHdRYFLNKLFDKI 517
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH-RIASIKRSDKI 1428
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-63 |
9.00e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 38.85 E-value: 9.00e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 503253044 22 ISFEIKEKERVGLVGRNGSGKTTLIRLLAGEETPDTGDIHLK 63
Cdd:COG3845 277 VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLD 318
|
|
| |
