|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-530 |
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: 697.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 4 IENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGEMAGRSAVA 83
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 84 EVMEGAGPVSAVAAELRELETAMsdpdrmDEMDAIVERYGEVQARYEELDGYALEGRAREVLAGLSFSQEMMDGDVAKLS 163
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKL------AEPDEDLERLAELQEEFEALGGWEAEARAEEILSGLGFPEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 164 GGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTYSGDY 243
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 244 GFYDEQRALNARQQQAQFERQQAMLAKEIKFIERFKARASHASQVQSRVKKLEKIDRVEPPRRRQTVAFEFLPAPRSGED 323
Cdd:COG0488 235 SAYLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAKQAQSRIKALEKLEREEPPRRDKTVEIRFPPPERLGKK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHSmDLLDGE 403
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ-EELDPD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 404 STILQWLEERFPKAGQAPLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIK 483
Cdd:COG0488 394 KTVLDELRDGAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 505055604 484 ALSAYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYGGGYSEYVER 530
Cdd:COG0488 474 ALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-527 |
5.22e-121 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 369.88 E-value: 5.22e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 14 RILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGEMAgRSAVAEVMEGAgpvs 93
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALP-QPALEYVIDGD---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 94 avaAELRELETAMSDPDRMDEMDAIVERYGEVQAryeeLDGYALEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALA 173
Cdd:PRK10636 89 ---REYRQLEAQLHDANERNDGHAIATIHGKLDA----IDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 174 RILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTYSGDYGFYDEQRALN 253
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 254 ARQQQAQFERQQAMLAKEIKFIERFKARASHASQVQSRVKKLEKIDRVEPPRRRQTVAFEF-----LPAPrsgedVVNLK 328
Cdd:PRK10636 242 LAQQQAMYESQQERVAHLQSYIDRFRAKATKAKQAQSRIKMLERMELIAPAHVDNPFHFSFrapesLPNP-----LLKME 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 329 SVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHSMDLLDGESTILQ 408
Cdd:PRK10636 317 KVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHQLEFLRADESPLQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 409 WLEERFPKAGQAPLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAY 488
Cdd:PRK10636 397 HLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 505055604 489 QGTMLFVSHDRRFLSALSNRvLELTPDG-INQYGGGYSEY 527
Cdd:PRK10636 477 EGALVVVSHDRHLLRSTTDD-LYLVHDGkVEPFDGDLEDY 515
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-534 |
2.10e-116 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 354.20 E-value: 2.10e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGEMAGRS 80
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQDQFAFEEFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEGAGPVSAVAAElRELETA---MSDPDRMdemdaiveRYGEVQARYEELDGYALEGRAREVLAGLSFSQEMMDG 157
Cdd:PRK15064 81 VLDTVIMGHTELWEVKQE-RDRIYAlpeMSEEDGM--------KVADLEVKFAEMDGYTAEARAGELLLGVGIPEEQHYG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 158 DVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALT 237
Cdd:PRK15064 152 LMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 238 TYSGDYGFYDEQRALNARQQQAQFERQQAMLAKEIKFIERFKARASHASQVQSRVKKLEKI--DRVEpPRRRQTVAFEFL 315
Cdd:PRK15064 232 VYPGNYDEYMTAATQARERLLADNAKKKAQIAELQSFVSRFSANASKAKQATSRAKQIDKIklEEVK-PSSRQNPFIRFE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 316 PAPRSGEDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQH 395
Cdd:PRK15064 311 QDKKLHRNALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQD 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 SMDLLDGESTILQWLEE-RFPKAGQAPLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLD 474
Cdd:PRK15064 391 HAYDFENDLTLFDWMSQwRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 475 LDTKEMLIKALSAYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYGGGYSEYVERTGQE 534
Cdd:PRK15064 471 MESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYEEYLRSQGIE 530
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
27-535 |
1.28e-115 |
|
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: 353.09 E-value: 1.28e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGEMAGRSAVAEVMEGAGPVSAVAAELRELETAM 106
Cdd:TIGR03719 31 GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTVRENVEEGVAEIKDALDRFNEISAKY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 107 SDPDrmDEMDAIVERYGEVQARYEELDGYALEGRAREVLAGLSFSQEmmDGDVAKLSGGWKMRVALARILLMRPDAMLLD 186
Cdd:TIGR03719 111 AEPD--ADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW--DADVTKLSGGERRRVALCRLLLSKPDMLLLD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 187 EPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTYSGDYGFYDEQRALNARQQQAQFERQQA 266
Cdd:TIGR03719 187 EPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKQKRLEQEEKEESARQK 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 267 MLAKEIKFIeRFKARASHASQvQSRVKKLEKIDRVEPPRRRQTVAFEFLPAPRSGEDVVNLKSVHKTYGSRTIYDGLDFM 346
Cdd:TIGR03719 267 TLKRELEWV-RQSPKGRQAKS-KARLARYEELLSQEFQKRNETAEIYIPPGPRLGDKVIEAENLTKAFGDKLLIDDLSFK 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 347 VRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQhSMDLLDGESTILQWLEE-----RFPKAgQAP 421
Cdd:TIGR03719 345 LPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQ-SRDALDPNKTVWEEISGgldiiKLGKR-EIP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 422 LRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQGTMLFVSHDRRF 501
Cdd:TIGR03719 423 SRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWF 502
|
490 500 510
....*....|....*....|....*....|....*....
gi 505055604 502 LSALSNRVLELTPDG-INQYGGGYSEYVE----RTGQEA 535
Cdd:TIGR03719 503 LDRIATHILAFEGDShVEWFEGNFSEYEEdkkrRLGEDA 541
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
27-535 |
4.98e-107 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 330.93 E-value: 4.98e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQ--------DVGEmagrsavaEVMEGAGPVSAVAAE 98
Cdd:PRK11819 33 GAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQepqldpekTVRE--------NVEEGVAEVKAALDR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 99 LRELETAMSDPDrmDEMDAIVERYGEVQARYEELDGYALEGR---AREVL---AGlsfsqemmDGDVAKLSGGWKMRVAL 172
Cdd:PRK11819 105 FNEIYAAYAEPD--ADFDALAAEQGELQEIIDAADAWDLDSQleiAMDALrcpPW--------DAKVTKLSGGERRRVAL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 173 ARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTYSGDYGFYDEQRAL 252
Cdd:PRK11819 175 CRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYSSWLEQKAK 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 253 NARQQQAQFERQQAMLAKEIKFIeRFKARASHASQvQSRVKKLEKIDRVEPPRRRQTVAFEFLPAPRSGEDVVNLKSVHK 332
Cdd:PRK11819 255 RLAQEEKQEAARQKALKRELEWV-RQSPKARQAKS-KARLARYEELLSEEYQKRNETNEIFIPPGPRLGDKVIEAENLSK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 333 TYGSRTIYDGLDFMVrrrERWCIMGI---NGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQhSMDLLDGESTIlqW 409
Cdd:PRK11819 333 SFGDRLLIDDLSFSL---PPGGIVGIigpNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQ-SRDALDPNKTV--W 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 410 lEE-----RFPKAG--QAPLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLI 482
Cdd:PRK11819 407 -EEisgglDIIKVGnrEIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALE 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 483 KALSAYQGTMLFVSHDRRFLSALSNRVLELTPDG-INQYGGGYSEY----VERTGQEA 535
Cdd:PRK11819 486 EALLEFPGCAVVISHDRWFLDRIATHILAFEGDSqVEWFEGNFQEYeedkKRRLGADA 543
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-527 |
2.31e-102 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 323.74 E-value: 2.31e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELpdEGqvaVEKGMTIGYFDQDVgemAGRSA 81
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAI--DG---IPKNCQILHVEQEV---VGDDT 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VA------------EVMEGAGPVSAVAAELR-ELETAMS--DPDRMDEMDAIVERYGEVQARYEELDGYALEGRAREVLA 146
Cdd:PLN03073 250 TAlqcvlntdiertQLLEEEAQLVAQQRELEfETETGKGkgANKDGVDKDAVSQRLEEIYKRLELIDAYTAEARAASILA 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 147 GLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVT 226
Cdd:PLN03073 330 GLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 227 KIIEIDGGALTTYSGDYGFYDEQRALNARQQQAQFERQQAMLAKEIKFIERFKARASHASQVQSRVKKLEKIDRVEPPRR 306
Cdd:PLN03073 410 DILHLHGQKLVTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRASLVQSRIKALDRLGHVDAVVN 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 307 RQTVAFEFlPAP--RSGEDVVNLKSVHKTY-GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL 383
Cdd:PLN03073 490 DPDYKFEF-PTPddRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFR 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 384 GASVKLGYFAQHSMDLLDGESTILQWLEERFPKAGQAPLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNF 463
Cdd:PLN03073 569 SAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 464 LVLDEPTNHLDLDTKEMLIKALSAYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYGGGYSEY 527
Cdd:PLN03073 649 LLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFHDY 712
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-524 |
7.02e-96 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 304.57 E-value: 7.02e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGEMAGRS 80
Cdd:PRK11147 3 LISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVEGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEGagpVSAVAAELRELEtAMSDPDRMDEMDAIVERYGEVQARYEELDGYALEGRAREVLAGLSFSQEMMdgdVA 160
Cdd:PRK11147 83 VYDFVAEG---IEEQAEYLKRYH-DISHLVETDPSEKNLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDPDAA---LS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTYS 240
Cdd:PRK11147 156 SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSYP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 241 GDYGFYDEQRALNARQQQAQFERQQAMLAKEIKFIER-FKARASHAsqvQSRVKKLEKIdRVEPPRRRQ---TVAFEFLP 316
Cdd:PRK11147 236 GNYDQYLLEKEEALRVEELQNAEFDRKLAQEEVWIRQgIKARRTRN---EGRVRALKAL-RRERSERREvmgTAKMQVEE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 317 APRSGEDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHS 396
Cdd:PRK11147 312 ASRSGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQHR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 ---------MD-LLDGESTI---------LQWLEErF---PKAGQAPLRAlagcfgfsgddvekrcrvLSGGEKARLVMA 454
Cdd:PRK11147 392 aeldpektvMDnLAEGKQEVmvngrprhvLGYLQD-FlfhPKRAMTPVKA------------------LSGGERNRLLLA 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 455 AMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQGTMLFVSHDRRFlsaLSNRVLE---LTPDG-INQYGGGY 524
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQF---VDNTVTEcwiFEGNGkIGRYVGGY 523
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-234 |
2.99e-55 |
|
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: 182.26 E-value: 2.99e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQdvgemagrsa 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 vaevmegagpvsavaaelreletamsdpdrmdemdaiverygevqaryeeldgyalegrarevlaglsfsqemmdgdvak 161
Cdd:cd03221 --------------------------------------------------------------------------------
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:cd03221 71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
325-516 |
6.20e-55 |
|
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: 181.49 E-value: 6.20e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQhsmdlldges 404
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 tilqwleerfpkagqaplralagcfgfsgddvekrcrvLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKA 484
Cdd:cd03221 71 --------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEA 112
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 485 LSAYQGTMLFVSHDRRFLSALSNRVLELTPDG 516
Cdd:cd03221 113 LKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-510 |
8.30e-38 |
|
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: 145.82 E-value: 8.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYI--EASAALNRGEKIGLVGPNGAGKTTLFRMITGqELPDEGQVAVEkgmtIGYFDQDVGEM-- 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAvdGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGGRISGE----VLLDGRDLLELse 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 AGRSA-VAEVMEGAG----PVSaVAAELRE-LETAMSDPDRMDEmdaiverygevqaryeeldgyalegRAREVLAGLSF 150
Cdd:COG1123 79 ALRGRrIGMVFQDPMtqlnPVT-VGDQIAEaLENLGLSRAEARA-------------------------RVLELLEAVGL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 151 sQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD----LESLIWLENFLKGYDGALLMTSHDREFMNRIVT 226
Cdd:COG1123 133 -ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDvttqAEILDLLRELQRERGTTVLLITHDLGVVAEIAD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 227 KIIEIDGGALttysgdygfydeqralnarqqqaqferqqamlakeikfIERFKARashasQVQSRVKKLEKIDRVEPPRR 306
Cdd:COG1123 212 RVVVMDDGRI--------------------------------------VEDGPPE-----EILAAPQALAAVPRLGAARG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 307 RQTvafeflPAPRSGEDVVNLKSVHKTYGSR-----TIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSV 381
Cdd:COG1123 249 RAA------PAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 382 SL-GASV-------------KLGYFAQHSMDLLDGESTILQWLEErfpkagqaPLRALAgcfGFSGDDVEKRC-----RV 442
Cdd:COG1123 323 LFdGKDLtklsrrslrelrrRVQMVFQDPYSSLNPRMTVGDIIAE--------PLRLHG---LLSRAERRERVaelleRV 391
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 443 -------------LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQ----GTMLFVSHDRRFLSAL 505
Cdd:COG1123 392 glppdladrypheLSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQrelgLTYLFISHDLAVVRYI 471
|
....*
gi 505055604 506 SNRVL 510
Cdd:COG1123 472 ADRVA 476
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-236 |
1.56e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.86 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigYFD-QDVGEMAG-- 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEI---------YLDgKPLSAMPPpe 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 -RSAVAevmegagpvsAVAAElreletamsdPDRMDEM--DAIVERYgevQARYEELDgyalEGRAREVLAGLSFSQEMM 155
Cdd:COG4619 72 wRRQVA----------YVPQE----------PALWGGTvrDNLPFPF---QLRERKFD----RERALELLERLGLPPDIL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 156 DGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES--LI--WLENFLKGYDGALLMTSHDREFMNRIVTKIIEI 231
Cdd:COG4619 125 DKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrRVeeLLREYLAEEGRAVLWVSHDPEQIERVADRVLTL 204
|
....*
gi 505055604 232 DGGAL 236
Cdd:COG4619 205 EAGRL 209
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-250 |
1.05e-33 |
|
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: 134.68 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGEMAGRSA 81
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPNKT 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VAEVMEGAgpvsavaaelreletamsdpdrMDEMdaiverygevqaryeELDGYALEGRAreVLAGLSFSQEMMDGDVAK 161
Cdd:TIGR03719 403 VWEEISGG----------------------LDII---------------KLGKREIPSRA--YVGRFNFKGSDQQKKVGQ 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDG-GALTTYS 240
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILAFEGdSHVEWFE 523
|
250
....*....|
gi 505055604 241 GDYGFYDEQR 250
Cdd:TIGR03719 524 GNFSEYEEDK 533
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
327-517 |
1.33e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.08 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV----------KLGYFAQH 395
Cdd:COG4619 3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLdGKPLsampppewrrQVAYVPQE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 SmDLLDGesTILQWLEERFPKAGQAP----LRALAGCFGFSGDDVEKRCRVLSGGEKARLVMA-AMLFDPpNFLVLDEPT 470
Cdd:COG4619 83 P-ALWGG--TVRDNLPFPFQLRERKFdrerALELLERLGLPPDILDKPVERLSGGERQRLALIrALLLQP-DVLLLDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 471 NHLDLDTKEMLIKALSAY----QGTMLFVSHDRRFLSALSNRVLELTPDGI 517
Cdd:COG4619 159 SALDPENTRRVEELLREYlaeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-236 |
8.72e-31 |
|
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: 119.96 E-value: 8.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmTIGYFDQDVGEMAGRS 80
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSI------LIDGEDVRKEPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAeVMEGAgpvsavaaelRELetamsdPDRMDemdaiVERYGEVQARYEELDGYALEGRAREVLAGLSFSqEMMDGDVA 160
Cdd:COG4555 75 QIG-VLPDE----------RGL------YDRLT-----VRENIRYFAELYGLFDEELKKRIEELIELLGLE-EFLDRRVG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:COG4555 132 ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-509 |
1.92e-30 |
|
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: 124.53 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQE--LPDEGQVAVEKGM--TIGYFDqdVGEMA 77
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHVALceKCGYVE--RPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRsavaevmegagPVSAVAAELRELET---AMSDPDRMDEMDAIVERYGEVQARYEE---LD---------GYALE---G 139
Cdd:TIGR03269 79 GE-----------PCPVCGGTLEPEEVdfwNLSDKLRRRIRKRIAIMLQRTFALYGDdtvLDnvlealeeiGYEGKeavG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 140 RAREVLAGLSFSQEMMDgdVAK-LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES--LI--WLENFLKGYDGALLMT 214
Cdd:TIGR03269 148 RAVDLIEMVQLSHRITH--IARdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTakLVhnALEEAVKASGISMVLT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 215 SHDREFMNRIVTKIIEIDGGALTtysgDYGFYDEQRAlnarqqqaqferqqamlakeiKFIERFKArashasqvqsrvkk 294
Cdd:TIGR03269 226 SHWPEVIEDLSDKAIWLENGEIK----EEGTPDEVVA---------------------VFMEGVSE-------------- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 295 LEKIDRVEpprrrqtvafeflpaprSGEDVVNLKSVHKTY-----GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKL 369
Cdd:TIGR03269 267 VEKECEVE-----------------VGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKI 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 370 VTGTTNPDKGS--VSLGAS----VKLGYF----AQHSMDLLDGE------STILQWLEE----RFPKAgQAPLRAL--AG 427
Cdd:TIGR03269 330 IAGVLEPTSGEvnVRVGDEwvdmTKPGPDgrgrAKRYIGILHQEydlyphRTVLDNLTEaiglELPDE-LARMKAVitLK 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 428 CFGFSGDDVE----KRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLD----LDTKEMLIKALSAYQGTMLFVSHDR 499
Cdd:TIGR03269 409 MVGFDEEKAEeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFIIVSHDM 488
|
570
....*....|
gi 505055604 500 RFLSALSNRV 509
Cdd:TIGR03269 489 DFVLDVCDRA 498
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-250 |
8.51e-30 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 123.31 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGEMAGRSA 81
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPNKT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VAEVmegagpVSavaaelreletamsdpdrmDEMDAIverygevqaryeELDGYALEGRAreVLAGLSFSqemmDGD--- 158
Cdd:PRK11819 405 VWEE------IS-------------------GGLDII------------KVGNREIPSRA--YVGRFNFK----GGDqqk 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 159 -VAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDG-GAL 236
Cdd:PRK11819 442 kVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILAFEGdSQV 521
|
250
....*....|....
gi 505055604 237 TTYSGDYGFYDEQR 250
Cdd:PRK11819 522 EWFEGNFQEYEEDK 535
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-295 |
2.00e-29 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 122.75 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 4 IENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQdvgemagrsava 83
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKLEVAYFDQ------------ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 84 evmegagpvsaVAAELreletamsDPDRMdEMDAIVERYGEVQaryeeldgyaLEGRAREVLAGLS---FSQEMMDGDVA 160
Cdd:PRK11147 390 -----------HRAEL--------DPEKT-VMDNLAEGKQEVM----------VNGRPRHVLGYLQdflFHPKRAMTPVK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 161 KLSGGWKMRVALARILLmRPDAML-LDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTK--IIEIDGGaLT 237
Cdd:PRK11147 440 ALSGGERNRLLLARLFL-KPSNLLiLDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTEcwIFEGNGK-IG 517
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 238 TYSGdyGFYD--EQRAlnarqqqaQFERQQAMLAKEIKfierfKARASHASQVQSRVKKL 295
Cdd:PRK11147 518 RYVG--GYHDarQQQA--------QYLALKQPAVKKKE-----EAAAPKAETVKRSSKKL 562
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
327-512 |
1.59e-28 |
|
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: 110.80 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLDGESTI 406
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI-----------------LIDGKDIA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 LQWLEERfpkagqapLRALAGCFGfsgddvekrcrvLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALS 486
Cdd:cd00267 65 KLPLEEL--------RRRIGYVPQ------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
|
170 180
....*....|....*....|....*....
gi 505055604 487 AYQG---TMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd00267 125 ELAEegrTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
325-512 |
1.66e-28 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 111.34 E-value: 1.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVS-LGASV---------KLGYFAQ 394
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvLGKDIkkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 395 HSMdlLDGESTILQWLEerfpkagqaplralagcfgfsgddvekrcrvLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLD 474
Cdd:cd03230 81 EPS--LYENLTVRENLK-------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505055604 475 LDTKEM---LIKALSAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd03230 128 PESRREfweLLRELKKEGKTILLSSHILEEAERLCDRVAIL 168
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-236 |
1.70e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 113.23 E-value: 1.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGEMagrs 80
Cdd:COG1131 1 IEVRGLTKRyGDKTALD-GVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRV--------LGEDVARD---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 avaevmegagpvsavAAELRELETAMSDPDRMDEmDAIVERYGEVQARYEELDGYALEGRAREVLA--GLSfsqEMMDGD 158
Cdd:COG1131 68 ---------------PAEVRRRIGYVPQEPALYP-DLTVRENLRFFARLYGLPRKEARERIDELLElfGLT---DAADRK 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 159 VAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHDREFMNRIVTKIIEIDGGA 235
Cdd:COG1131 129 VGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELaaeGKTVLLSTHYLEEAERLCDRVAIIDKGR 208
|
.
gi 505055604 236 L 236
Cdd:COG1131 209 I 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-234 |
2.93e-27 |
|
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: 107.87 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGE--MAG 78
Cdd:cd03230 1 IEVRNLSKRyGKKTALD-DISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--------LGKDIKKepEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 RSAVAEVMEGAGPvsavaaelreletamsdpdrmdemdaiverygevqarYEELdgyalegRAREVLaglsfsqemmdgd 158
Cdd:cd03230 72 KRRIGYLPEEPSL-------------------------------------YENL-------TVRENL------------- 94
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 159 vaKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:cd03230 95 --KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRELkkeGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-236 |
3.37e-27 |
|
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: 109.34 E-value: 3.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS--NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGEMAGR 79
Cdd:COG1122 1 IELENLSFSypGGTPALD-DVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV--------DGKDITKKNLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 SAVAEVmegaGPVsavaaelreletaMSDPDRMdemdaIVERygEVqarYEE---------LDGYALEGRAREVLA--GL 148
Cdd:COG1122 72 ELRRKV----GLV-------------FQNPDDQ-----LFAP--TV---EEDvafgpenlgLPREEIRERVEEALElvGL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 149 SfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGA---LLMTSHDREFMNRIV 225
Cdd:COG1122 125 E---HLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEgktVIIVTHDLDLVAELA 201
|
250
....*....|.
gi 505055604 226 TKIIEIDGGAL 236
Cdd:COG1122 202 DRVIVLDDGRI 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
326-534 |
3.78e-26 |
|
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: 106.87 E-value: 3.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 326 NLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG--ASVKLGYFAQHSMDLLDGE 403
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgeDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 404 S------TILQWLE------ERFPKAGQAPLRALAGCFGFSgDDVEKRCRVLSGGEKARLVMAAMLF-DPPNfLVLDEPT 470
Cdd:COG4555 83 RglydrlTVRENIRyfaelyGLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVhDPKV-LLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 471 NHLDLDTKEML---IKALSAYQGTMLFVSHDRRFLSALSNRVLELTpDGINQYGGGYSEYVERTGQE 534
Cdd:COG4555 161 NGLDVMARRLLreiLRALKKEGKTVLFSSHIMQEVEALCDRVVILH-KGKVVAQGSLDELREEIGEE 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
325-510 |
4.22e-26 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 106.69 E-value: 4.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVS-LGASV---------KLGYFAQ 394
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRvLGEDVardpaevrrRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 395 HSMdlLDGESTILQWleerfpkagqapLRALAGCFGFSGDDVEKR-----------------CRVLSGGEKARLVMA-AM 456
Cdd:COG1131 81 EPA--LYPDLTVREN------------LRFFARLYGLPRKEARERidellelfgltdaadrkVGTLSGGMKQRLGLAlAL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 457 LFDPPnFLVLDEPTNHLD-LDTKEM--LIKALSAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:COG1131 147 LHDPE-LLILDEPTSGLDpEARRELweLLRELAAEGKTVLLSTHYLEEAERLCDRVA 202
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
327-510 |
9.38e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 104.05 E-value: 9.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG----ASVKLGYFAQHSmdlldg 402
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDgkdlASLSPKELARKI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 eSTILQWLEerfpkagqaplraLAGCFGFSgddvEKRCRVLSGGEKARlVMAAMLF--DPPnFLVLDEPTNHLDLDTK-E 479
Cdd:cd03214 76 -AYVPQALE-------------LLGLAHLA----DRPFNELSGGERQR-VLLARALaqEPP-ILLLDEPTSHLDIAHQiE 135
|
170 180 190
....*....|....*....|....*....|....
gi 505055604 480 ML--IKALSAYQG-TMLFVSHDRRFLSALSNRVL 510
Cdd:cd03214 136 LLelLRRLARERGkTVVMVLHDLNLAARYADRVI 169
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-217 |
1.17e-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: 104.48 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVGEmaGRS 80
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVL--------WNGEPIRD--ARE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEGAGPVSAVAAELreleTAmsdpdrMDEMDAIVERYGEVQARyeeldgyaleGRAREVLA--GLsfsQEMMDGD 158
Cdd:COG4133 72 DYRRRLAYLGHADGLKPEL----TV------RENLRFWAALYGLRADR----------EAIDEALEavGL---AGLADLP 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 159 VAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHD 217
Cdd:COG4133 129 VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHlarGGAVLLTTHQ 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
24-190 |
1.27e-25 |
|
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: 102.73 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGM-----------TIGYFDQDVGEMAGRSAVAEVMEGAgpv 92
Cdd:pfam00005 8 LNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDltdderkslrkEIGYVFQDPQLFPRLTVRENLRLGL--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 93 savaaelreLETAMSDPDRMDEMDAIVERYGEVQARYEELDGYalegrarevlaglsfsqemmdgdVAKLSGGWKMRVAL 172
Cdd:pfam00005 85 ---------LLKGLSKREKDARAEEALEKLGLGDLADRPVGER-----------------------PGTLSGGQRQRVAI 132
|
170
....*....|....*...
gi 505055604 173 ARILLMRPDAMLLDEPSN 190
Cdd:pfam00005 133 ARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
322-512 |
1.98e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 104.79 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG------ASVKLGYFAQH 395
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFgkpprrARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 S----------MDL----LDGESTILQWL--EERfpkagQAPLRALA--GCFGFSGddveKRCRVLSGGEKARLVMAAML 457
Cdd:COG1121 84 AevdwdfpitvRDVvlmgRYGRRGLFRRPsrADR-----EAVDEALErvGLEDLAD----RPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 458 FDPPNFLVLDEPTNHLDLDTKEM---LIKALSAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEAlyeLLRELRREGKTILVVTHDLGAVREYFDRVLLL 212
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-234 |
1.28e-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: 101.77 E-value: 1.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGqvavekgmTIGYFDQDVGEmagrSAVAEVMEGAGpvsavaaelr 100
Cdd:cd03225 21 SLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSG--------EVLVDGKDLTK----LSLKELRRKVG---------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 eleTAMSDPDRM-------DEMdAI-VERYGevqaryeeLDGYALEGRAREVLAGLSFsQEMMDGDVAKLSGGWKMRVAL 172
Cdd:cd03225 79 ---LVFQNPDDQffgptveEEV-AFgLENLG--------LPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAI 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 173 ARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGA---LLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:cd03225 146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEgktIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
332-514 |
1.38e-24 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 101.40 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 332 KTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVK---------LGYFAQHsmDLLD 401
Cdd:COG4133 10 CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWnGEPIRdaredyrrrLAYLGHA--DGLK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 402 GESTILQWLeeRF-------PKAGQAPLRALAGcFGFSGDDvEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLD 474
Cdd:COG4133 88 PELTVRENL--RFwaalyglRADREAIDEALEA-VGLAGLA-DLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505055604 475 LDTKEMLIKALSAY--QGTM-LFVSHDRRFLSALsnRVLELTP 514
Cdd:COG4133 164 AAGVALLAELIAAHlaRGGAvLLTTHQPLELAAA--RVLDLGD 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
327-512 |
2.21e-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: 101.00 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIY--DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLDGES 404
Cdd:cd03225 2 LKNLSFSYPDGARPalDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEV-----------------LVDGKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 TILQWLEERFPKAG---QAP----------------LRALagcfGFSGDDVEKR-----------------CRVLSGGEK 448
Cdd:cd03225 65 LTKLSLKELRRKVGlvfQNPddqffgptveeevafgLENL----GLPEEEIEERveealelvgleglrdrsPFTLSGGQK 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 449 ARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML---IKALSAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd03225 141 QRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELlelLKKLKAEGKTIIIVTHDLDLLLELADRVIVL 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
327-509 |
3.46e-24 |
|
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: 100.66 E-value: 3.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIY--DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG----------ASVKLGYFAQ 394
Cdd:cd03263 3 IRNLTKTYKKGTKPavDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirtdrkaARQSLGYCPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 395 HsmDLLDGESTILQWLeeRFpkagQAPLR------------ALAGCFGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPN 462
Cdd:cd03263 83 F--DALFDELTVREHL--RF----YARLKglpkseikeeveLLLRVLGLT-DKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505055604 463 FLVLDEPTNHLDLDTKEMLIKALSAYQG--TMLFVSHDRRFLSALSNRV 509
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKgrSIILTTHSMDEAEALCDRI 202
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
327-498 |
7.70e-24 |
|
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: 100.50 E-value: 7.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV----------KLGYFAQH 395
Cdd:COG1120 4 AENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLdGRDLaslsrrelarRIAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 SMDLLD---------GestilqwleeRFPKAG----------QAPLRALA--GCFGFSgddvEKRCRVLSGGEKARlVMA 454
Cdd:COG1120 84 PPAPFGltvrelvalG----------RYPHLGlfgrpsaedrEAVEEALErtGLEHLA----DRPVDELSGGERQR-VLI 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505055604 455 AMLF--DPPnFLVLDEPTNHLD-------LDtkemLIKALSAYQG-TMLFVSHD 498
Cdd:COG1120 149 ARALaqEPP-LLLLDEPTSHLDlahqlevLE----LLRRLARERGrTVVMVLHD 197
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-254 |
1.06e-23 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 105.25 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRIlyIEASAALN--RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQdvgemag 78
Cdd:PRK10636 312 LLKMEKVSAGYGDRI--ILDSIKLNlvPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQ------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 rsavaevmegagpvsavaaelRELETAMSDPDRMDEMDAIVERygevqaryeeldgyALEGRAREVLAGLSFSQEMMDGD 158
Cdd:PRK10636 383 ---------------------HQLEFLRADESPLQHLARLAPQ--------------ELEQKLRDYLGGFGFQGDKVTEE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 159 VAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTT 238
Cdd:PRK10636 428 TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEP 507
|
250 260
....*....|....*....|.
gi 505055604 239 YSGDYGFY-----DEQRALNA 254
Cdd:PRK10636 508 FDGDLEDYqqwlsDVQKQENQ 528
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
325-512 |
2.78e-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: 98.17 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTY-GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLDGE 403
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEV-----------------LVDGK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 404 STILQWLEERFPKAG---QAP----------------LRALagcfGFSGDDVEKRCR-----------------VLSGGE 447
Cdd:COG1122 64 DITKKNLRELRRKVGlvfQNPddqlfaptveedvafgPENL----GLPREEIRERVEealelvglehladrpphELSGGQ 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 448 KARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG---TMLFVSHDRRFLSALSNRVLEL 512
Cdd:COG1122 140 KQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVL 207
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
330-512 |
5.91e-23 |
|
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: 96.94 E-value: 5.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 330 VHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV--------KLGYFAQHSMDLLD 401
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrkSIGYVMQDVDYQLF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 402 GESTilqWLEERF----PKAGQAPLRALAGCFGFSGDDvEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDT 477
Cdd:cd03226 86 TDSV---REELLLglkeLDAGNEQAETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161
|
170 180 190
....*....|....*....|....*....|....*...
gi 505055604 478 KEM---LIKALSAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd03226 162 MERvgeLIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
322-497 |
1.31e-22 |
|
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: 97.08 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKG-SVSL------GASV-----KL 389
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrgGEDVwelrkRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 390 GYFAQHSMDLLDGESTILQ------------WLEerfPKAGQAPL-RALAGCFGFSgDDVEKRCRVLSGGEKARLVMA-A 455
Cdd:COG1119 81 GLVSPALQLRFPRDETVLDvvlsgffdsiglYRE---PTDEQRERaRELLELLGLA-HLADRPFGTLSQGEQRRVLIArA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505055604 456 MLFDPPnFLVLDEPTNHLDLDTKEMLIKALS--AYQG--TMLFVSH 497
Cdd:COG1119 157 LVKDPE-LLILDEPTAGLDLGARELLLALLDklAAEGapTLVLVTH 201
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
333-512 |
1.58e-22 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 95.68 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 333 TYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL------GASVKLGYFAQHS---------- 396
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgkpleKERKRIGYVPQRRsidrdfpisv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 MDL----LDGESTILQWL-EERFPKAgqapLRALA--GCFGFSgddvEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEP 469
Cdd:cd03235 88 RDVvlmgLYGHKGLFRRLsKADKAKV----DEALErvGLSELA----DRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505055604 470 TNHLDLDTKEMLIKALSAYQG---TMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLL 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-237 |
1.65e-22 |
|
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: 96.80 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-----NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGE 75
Cdd:COG1124 1 MLEVRNLSVSygqggRRVPVLK-DVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFD--------GRPVTR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 76 MAGRSAVAEV-MEGAGPVSAVAAELReLETAMSDPDRmdemdaiVERYGEVQARYEELdgyalegrAREVlaGLSfsQEM 154
Cdd:COG1124 72 RRRKAFRRRVqMVFQDPYASLHPRHT-VDRILAEPLR-------IHGLPDREERIAEL--------LEQV--GLP--PSF 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 155 MDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL----ESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIE 230
Cdd:COG1124 132 LDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVsvqaEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAV 211
|
....*..
gi 505055604 231 IDGGALT 237
Cdd:COG1124 212 MQNGRIV 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-234 |
2.43e-22 |
|
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: 93.46 E-value: 2.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 3 RIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGRSAV 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID--------GKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 83 AEVmegagpvsavaaelreletamsdpdrmdemdaiverygevqaryeeldGYalegrarevlaglsfsqemmdgdVAKL 162
Cdd:cd00267 73 RRI------------------------------------------------GY-----------------------VPQL 81
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 163 SGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:cd00267 82 SGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELaeeGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-217 |
8.89e-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: 94.73 E-value: 8.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGR 79
Cdd:COG1120 1 MLEAENLSVGyGGRPVLD-DVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLD--------GRDLASLSRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 sAVAEVM-------EGAGPVSAvaaelREL--------ETAMSDPDRMDEmdAIVERygevqaryeeldgyALEgrarev 144
Cdd:COG1120 72 -ELARRIayvpqepPAPFGLTV-----RELvalgryphLGLFGRPSAEDR--EAVEE--------------ALE------ 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 145 LAGLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL----ESLIWLENFLKGYDGALLMTSHD 217
Cdd:COG1120 124 RTGLE---HLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLahqlEVLELLRRLARERGRTVVMVLHD 197
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-237 |
9.59e-22 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.58 E-value: 9.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS--NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGEMaG 78
Cdd:COG2884 1 MIRFENVSKRypGGREALS-DVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLV--------NGQDLSRL-K 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 RSAVAE-------------------VMEGagpvsaVAAELRELETamsDPDRMDEmdaiverygevqaryeeldgyaleg 139
Cdd:COG2884 71 RREIPYlrrrigvvfqdfrllpdrtVYEN------VALPLRVTGK---SRKEIRR------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 140 RAREVLA--GLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLK-----GydGALL 212
Cdd:COG2884 117 RVREVLDlvGLS---DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEeinrrG--TTVL 191
|
250 260
....*....|....*....|....*
gi 505055604 213 MTSHDREFMNRIVTKIIEIDGGALT 237
Cdd:COG2884 192 IATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-237 |
1.28e-21 |
|
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: 93.09 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 3 RIENISKSNSH--RILYIEaSAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKgmtigyfdQDVGEMAGRS 80
Cdd:cd03226 1 RIENISFSYKKgtEILDDL-SLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG--------KPIKAKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEgagpvsavaaelreletamsDPDRMDEMDAIverygevqarYEEL-----DGYALEGRAREVLAGLSFSqEMM 155
Cdd:cd03226 72 SIGYVMQ--------------------DVDYQLFTDSV----------REELllglkELDAGNEQAETVLKDLDLY-ALK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 156 DGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD---LESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEID 232
Cdd:cd03226 121 ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDyknMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLA 200
|
....*
gi 505055604 233 GGALT 237
Cdd:cd03226 201 NGAIV 205
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
229-314 |
1.03e-20 |
|
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: 86.47 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 229 IEIDGGALTTYSGDYGFYDEQRALNARQQQAQFERQQAMLAKEIKFIERFKARASHASQVQSRVKKLEKIDRVEPPRRRQ 308
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAKQAQSRIKALEKMERIEKPERDK 80
|
....*.
gi 505055604 309 tVAFEF 314
Cdd:pfam12848 81 -PKLRF 85
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
327-497 |
1.07e-20 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 89.02 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHSMDLldGESTI 406
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRA--GIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 LQwleerfpkagqaplralagcfgfsgddvekrcrvLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML---IK 483
Cdd:cd03216 81 YQ----------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLfkvIR 126
|
170
....*....|....*
gi 505055604 484 ALSAyQG-TMLFVSH 497
Cdd:cd03216 127 RLRA-QGvAVIFISH 140
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
325-497 |
1.37e-20 |
|
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: 89.97 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL--GASVKLGYFAQHSMDLLDG 402
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 EStilqWLEERfpkAGQAPLRALAGCFGFSGDDVE-------------KRCRVLSGGEKARLVMAAMLFDPPNFLVLDEP 469
Cdd:cd03268 81 PG----FYPNL---TARENLRLLARLLGIRKKRIDevldvvglkdsakKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190
....*....|....*....|....*....|.
gi 505055604 470 TNHLDLD-TKEM--LIKALSAYQGTMLFVSH 497
Cdd:cd03268 154 TNGLDPDgIKELreLILSLRDQGITVLISSH 184
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
340-471 |
1.41e-20 |
|
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: 88.09 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 340 YDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG-----------ASVKLGYFAQHsmDLLDGESTILQ 408
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDgqdltdderksLRKEIGYVFQD--PQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 409 WLEERFP---------KAGQAPLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTN 471
Cdd:pfam00005 79 NLRLGLLlkglskrekDARAEEALEKLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
1.55e-20 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 90.92 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV------EKGMTIGYFDQdv 73
Cdd:COG1121 6 AIELENLTVSyGGRPVLE-DVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 74 gemagRSAVAEVMegagPVSAvaaelreLETAMSdpdrmdemdaivERYGEV-------QARYEeldgyalegRAREVLA 146
Cdd:COG1121 83 -----RAEVDWDF----PITV-------RDVVLM------------GRYGRRglfrrpsRADRE---------AVDEALE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 147 --GLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKG---YDGALLMTSHDREFM 221
Cdd:COG1121 126 rvGLE---DLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElrrEGKTILVVTHDLGAV 202
|
250
....*....|...
gi 505055604 222 NRIVTKIIEIDGG 234
Cdd:COG1121 203 REYFDRVLLLNRG 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
3-234 |
3.07e-20 |
|
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: 88.26 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 3 RIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGEMAGRsAV 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILL--------DGKDLASLSPK-EL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 83 AEVMegagpvsAVaaelreLETAMsdpdrmdemdaiverygevqaryEELDGYALEGRarevlaglsfsqemmdgDVAKL 162
Cdd:cd03214 72 ARKI-------AY------VPQAL-----------------------ELLGLAHLADR-----------------PFNEL 98
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 163 SGGWKMRVALARILLMRPDAMLLDEPSNHLDL----ESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:cd03214 99 SGGERQRVLLARALAQEPPILLLDEPTSHLDIahqiELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDG 174
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-219 |
4.88e-20 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 88.73 E-value: 4.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigYFDqdvgemaGRsa 81
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEI---------LID-------GR-- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 vaevmegagPVSAVAAELRELETAMSDPDRMDEMDaiVER---YGEVQARYEELDgyaLEGRAREVLAGLSFSqEMMDGD 158
Cdd:cd03259 63 ---------DVTGVPPERRNIGMVFQDYALFPHLT--VAEniaFGLKLRGVPKAE---IRARVRELLELVGLE-GLLNRY 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 159 VAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGAL----LMTSHDRE 219
Cdd:cd03259 128 PHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELQRELgittIYVTHDQE 192
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-236 |
4.90e-20 |
|
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: 88.43 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGEMAGRSA 81
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF--------DGKSYQKNIEALR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VaevmegagpvsavaaelreletamsdpdrmdeMDAIVER---YGEVQARyEELDGYAL-----EGRAREVLAGLSFSQE 153
Cdd:cd03268 73 R--------------------------------IGALIEApgfYPNLTAR-ENLRLLARllgirKKRIDEVLDVVGLKDS 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 154 MmDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENF---LKGYDGALLMTSHDREFMNRIVTKIIE 230
Cdd:cd03268 120 A-KKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELilsLRDQGITVLISSHLLSEIQKVADRIGI 198
|
....*.
gi 505055604 231 IDGGAL 236
Cdd:cd03268 199 INKGKL 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-234 |
7.06e-20 |
|
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: 88.88 E-value: 7.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGEMaGR 79
Cdd:COG1127 5 MIEVRNLTKSfGDRVVLD-GVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILV--------DGQDITGL-SE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 SAVAEVMEGAGPV---SA----------VAAELRELeTAMSDpdrmDEMDAIVErygevqaryeeldgYALEgrarevLA 146
Cdd:COG1127 75 KELYELRRRIGMLfqgGAlfdsltvfenVAFPLREH-TDLSE----AEIRELVL--------------EKLE------LV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 147 GLSFSQEMMDGDvakLSGGWKMRVALARILLMRPDAMLLDEPSNHLD------LESLIwlENFLKGYDGALLMTSHDREF 220
Cdd:COG1127 130 GLPGAADKMPSE---LSGGMRKRVALARALALDPEILLYDEPTAGLDpitsavIDELI--RELRDELGLTSVVVTHDLDS 204
|
250
....*....|....
gi 505055604 221 MNRIVTKIIEIDGG 234
Cdd:COG1127 205 AFAIADRVAVLADG 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
3-234 |
8.35e-20 |
|
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: 87.97 E-value: 8.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 3 RIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVeKGMTIGYFDQDVGEMAGRSA 81
Cdd:cd03235 1 EVEDLTVSyGGHPVLE-DVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV-FGKPLEKERKRIGYVPQRRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VAEVMegagPVSAvaaelreLETAMSDPDRMDEMDAIVERygevqARYEELDgYALEgrarevLAGLSfsqEMMDGDVAK 161
Cdd:cd03235 79 IDRDF----PISV-------RDVVLMGLYGHKGLFRRLSK-----ADKAKVD-EALE------RVGLS---ELADRQIGE 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES---LIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:cd03235 133 LSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTqedIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
324-497 |
8.65e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 90.25 E-value: 8.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL----------GASVKLGYFA 393
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpsrarHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 394 QhsMDLLDGESTI---LQWLEERFPKAGQAPLRALAGCFGFSG--DDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDE 468
Cdd:PRK13537 87 Q--FDNLDPDFTVrenLLVFGRYFGLSAAAARALVPPLLEFAKleNKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 469 PTNHLDLDTKEML---IKALSAYQGTMLFVSH 497
Cdd:PRK13537 165 PTTGLDPQARHLMwerLRSLLARGKTILLTTH 196
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-236 |
1.95e-19 |
|
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: 87.16 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-----NSHRILYIeASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEM 76
Cdd:cd03255 1 IELKNLSKTyggggEKVQALKG-VSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVD--------GTDISKL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 AGRsavaevmegagpvsavaaELRELetamsdpdRMDEMDAIVERYG-----------EVQARYEELDGYALEGRAREVL 145
Cdd:cd03255 72 SEK------------------ELAAF--------RRRHIGFVFQSFNllpdltalenvELPLLLAGVPKKERRERAEELL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 146 --AGLsfsQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES--LIW--LENFLKGYDGALLMTSHDRE 219
Cdd:cd03255 126 erVGL---GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkEVMelLRELNKEAGTTIVVVTHDPE 202
|
250
....*....|....*..
gi 505055604 220 fMNRIVTKIIEIDGGAL 236
Cdd:cd03255 203 -LAEYADRIIELRDGKI 218
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
325-512 |
2.01e-19 |
|
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: 85.51 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRT--IYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVK----------LGY 391
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdGVDLRdldleslrknIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 FAQHSMdLLDGesTIlqwleerfpkagqaplralagcfgfsgddvekRCRVLSGGEKARLVMA-AMLFDPPnFLVLDEPT 470
Cdd:cd03228 81 VPQDPF-LFSG--TI--------------------------------RENILSGGQRQRIAIArALLRDPP-ILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505055604 471 NHLDLDTKEMLIKALSAYQG--TMLFVSHDrrfLSALSN--RVLEL 512
Cdd:cd03228 125 SALDPETEALILEALRALAKgkTVIVIAHR---LSTIRDadRIIVL 167
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
325-510 |
2.30e-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: 85.70 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLDGES 404
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI-----------------LIDGED 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 tiLQWLEERFPkagqaPLRALAGC----FG-FSGDDVEKRCR-VLSGGEKARLVMA-AMLFDPPnFLVLDEPTNHLDLDT 477
Cdd:cd03229 64 --LTDLEDELP-----PLRRRIGMvfqdFAlFPHLTVLENIAlGLSGGQQQRVALArALAMDPD-VLLLDEPTSALDPIT 135
|
170 180 190
....*....|....*....|....*....|....*..
gi 505055604 478 K---EMLIKALSAYQG-TMLFVSHDRRFLSALSNRVL 510
Cdd:cd03229 136 RrevRALLKSLQAQLGiTVVLVTHDLDEAARLADRVV 172
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
325-512 |
2.78e-19 |
|
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: 86.39 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGS----RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV------------ 387
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVdGTDIsklsekelaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 388 --KLGY-FAQHSmdLLdGESTILQWLEerFP------KAGQAPLRA--LAGCFGFsGDDVEKRCRVLSGGEKARLVMA-A 455
Cdd:cd03255 81 rrHIGFvFQSFN--LL-PDLTALENVE--LPlllagvPKKERRERAeeLLERVGL-GDRLNHYPSELSGGQQQRVAIArA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 456 MLFDPPnFLVLDEPTNHLDLDTKEM---LIKALSAYQG-TMLFVSHDRRFLSaLSNRVLEL 512
Cdd:cd03255 155 LANDPK-IILADEPTGNLDSETGKEvmeLLRELNKEAGtTIVVVTHDPELAE-YADRIIEL 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
327-510 |
3.36e-19 |
|
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: 86.03 E-value: 3.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV--------KLGYFAQH-- 395
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVtgvpperrNIGMVFQDya 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 ---SMDLLDgesTILQWLEERFPKAGQAPLRALAGCFGFSGDDVEKRcRV--LSGGEKARLVMAAMLFDPPNFLVLDEPT 470
Cdd:cd03259 83 lfpHLTVAE---NIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNR-YPheLSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505055604 471 NHLDLDTKE---MLIKALSAYQG-TMLFVSHDRRFLSALSNRVL 510
Cdd:cd03259 159 SALDAKLREelrEELKELQRELGiTTIYVTHDQEEALALADRIA 202
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
324-510 |
3.42e-19 |
|
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: 86.41 E-value: 3.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTY----GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVS------LGASVKL---- 389
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIfdgkdlLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 390 ----GYFAQHSMDLLDGESTILQWLEERF------PKAGQAPLRALAGCFGFSGDD--VEKRCRVLSGGEKARLVMA-AM 456
Cdd:cd03257 81 rkeiQMVFQDPMSSLNPRMTIGEQIAEPLrihgklSKKEARKEAVLLLLVGVGLPEevLNRYPHELSGGQRQRVAIArAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 457 LFDPPnFLVLDEPTNHLDLDTK----EMLIKALSAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:cd03257 161 ALNPK-LLIADEPTSALDVSVQaqilDLLKKLQEELGLTLLFITHDLGVVAKIADRVA 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-236 |
5.09e-19 |
|
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: 85.88 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS---NSHRILYIEA-SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtiGYfdqDVgem 76
Cdd:cd03266 1 MITADALTKRfrdVKKTVQAVDGvSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVD-----GF---DV--- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 agRSAVAEVMEGAGPVSAvaaelreletAMSDPDRMD--EMdaiVERYGevqaRYEELDGYALEGRAREVLAGLSFsQEM 154
Cdd:cd03266 70 --VKEPAEARRRLGFVSD----------STGLYDRLTarEN---LEYFA----GLYGLKGDELTARLEELADRLGM-EEL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 155 MDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDG---ALLMTSHDREFMNRIVTKIIEI 231
Cdd:cd03266 130 LDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlgkCILFSTHIMQEVERLCDRVVVL 209
|
....*
gi 505055604 232 DGGAL 236
Cdd:cd03266 210 HRGRV 214
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
282-530 |
5.12e-19 |
|
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: 90.21 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 282 ASHASQVQSRVKKLEKIDRVEPPrrrqtVAFEFLPAPRSGEDVVNLKSVHKTY--GSRTIYDGLDFMVRRRERWCIMGIN 359
Cdd:COG4987 296 AQHLGRVRAAARRLNELLDAPPA-----VTEPAEPAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPS 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 360 GAGKSTLLKLVTGTTNPDKGSVSL-GASVK----------LGYFAQHSmDLLDGesTILQWLeeRF--PKAGQAPLRA-- 424
Cdd:COG4987 371 GSGKSTLLALLLRFLDPQSGSITLgGVDLRdldeddlrrrIAVVPQRP-HLFDT--TLRENL--RLarPDATDEELWAal 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 425 -LAGCfgfsGDDVEKR-----CRV------LSGGEKARLVMA-AMLFDPPnFLVLDEPTNHLDLDTKEMLIKAL-SAYQG 490
Cdd:COG4987 446 eRVGL----GDWLAALpdgldTWLgeggrrLSGGERRRLALArALLRDAP-ILLLDEPTEGLDAATEQALLADLlEALAG 520
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 505055604 491 -TMLFVSHDRRFLsALSNRVLEL---------TPDGINQYGGGYSEYVER 530
Cdd:COG4987 521 rTVLLITHRLAGL-ERMDRILVLedgriveqgTHEELLAQNGRYRQLYQR 569
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-231 |
5.31e-19 |
|
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: 86.02 E-value: 5.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVGEM 76
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAlddvSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSII--------FDGKDLLKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 AGRsavaevmegagpvsavaaELRELETAMS----DPD-----RMDEMDAIVERYgevQARYEELDGYALEGRAREVLAG 147
Cdd:cd03257 73 SRR------------------LRKIRRKEIQmvfqDPMsslnpRMTIGEQIAEPL---RIHGKLSKKEARKEAVLLLLVG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 148 LSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKG----YDGALLMTSHD----RE 219
Cdd:cd03257 132 VGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHDlgvvAK 211
|
250
....*....|....*.
gi 505055604 220 FMNRIVT----KIIEI 231
Cdd:cd03257 212 IADRVAVmyagKIVEE 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-193 |
1.22e-18 |
|
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: 84.83 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV------EKGMTIGYFDQ 71
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTAlediSLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 72 DVGEMAGRSAVAEVmegagpvsAVAAELREletaMSDPDRMDEMDAIVERYGevqaryeeldgyaLEGRARevlaglSFS 151
Cdd:cd03293 81 QDALLPWLTVLDNV--------ALGLELQG----VPKAEARERAEELLELVG-------------LSGFEN------AYP 129
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505055604 152 QEmmdgdvakLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:cd03293 130 HQ--------LSGGMRQRVALARALAVDPDVLLLDEPFSALD 163
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-236 |
1.46e-18 |
|
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: 84.94 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEM 76
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTAlkdvSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVD--------GTDLTLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 AGRsavaevmegagpvsavaaELREL--ETAMsdpdrmdemdaIVERYGEVQAR--YE------ELDGYA---LEGRARE 143
Cdd:cd03258 73 SGK------------------ELRKArrRIGM-----------IFQHFNLLSSRtvFEnvalplEIAGVPkaeIEERVLE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 144 VLA--GLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES----LIWLENFLKGYDGALLMTSHD 217
Cdd:cd03258 124 LLElvGLE---DKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsiLALLRDINRELGLTIVLITHE 200
|
250
....*....|....*....
gi 505055604 218 REFMNRIVTKIIEIDGGAL 236
Cdd:cd03258 201 MEVVKRICDRVAVMEKGEV 219
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
305-497 |
2.63e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 86.42 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 305 RRRQTVAFEFLPAPRSGEDV-VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVS- 382
Cdd:PRK13536 21 RKHQGISEAKASIPGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITv 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 383 LGASV---------KLGYFAQhsMDLLDGESTIlqwleerfpkagQAPLRALAGCFGFSGDDVEK--------------- 438
Cdd:PRK13536 101 LGVPVpararlaraRIGVVPQ--FDNLDLEFTV------------RENLLVFGRYFGMSTREIEAvipsllefarleska 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 439 --RCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML---IKALSAYQGTMLFVSH 497
Cdd:PRK13536 167 daRVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIwerLRSLLARGKTILLTTH 230
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-219 |
2.68e-18 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 86.35 E-value: 2.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVgeMAGRSA 81
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLN--------GRDL--FTNLPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 -------------------VAEvmegagpvsAVAAELReletaMSDPDRmDEMDAIVERY-GEVQaryeeLDGyaLEGRA 141
Cdd:COG1118 73 rerrvgfvfqhyalfphmtVAE---------NIAFGLR-----VRPPSK-AEIRARVEELlELVQ-----LEG--LADRY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 142 revlaglsfsqemmdgdVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD------LESliWLENFLKGYDGALLMTS 215
Cdd:COG1118 131 -----------------PSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDakvrkeLRR--WLRRLHDELGGTTVFVT 191
|
....
gi 505055604 216 HDRE 219
Cdd:COG1118 192 HDQE 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-194 |
4.05e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 4.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVG-----E 75
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR--------LNGRPLAdwspaE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 76 MAGRSA-------------VAEVME-GAGPVSAVAAELRELetamsdpdrmdemdaiverygeVQARYEELDGYALEGRa 141
Cdd:PRK13548 74 LARRRAvlpqhsslsfpftVEEVVAmGRAPHGLSRAEDDAL----------------------VAAALAQVDLAHLAGR- 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 142 revlaglsfsqemmdgDVAKLSGGWKMRVALARIL--LMRPDA----MLLDEPSNHLDL 194
Cdd:PRK13548 131 ----------------DYPQLSGGEQQRVQLARVLaqLWEPDGpprwLLLDEPTSALDL 173
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
298-512 |
4.11e-18 |
|
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: 87.51 E-value: 4.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 298 IDRVEPPRRRQTVafeflPAPRSGEDVVNLKSVHKTY-GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNP 376
Cdd:COG4988 315 LDAPEPAAPAGTA-----PLPAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 377 DKGSVSL-GASV----------KLGYFAQHSMdLLDGesTILQWLeeRF--PKAGQAPLRA---LAGCFGF-----SGDD 435
Cdd:COG4988 390 YSGSILInGVDLsdldpaswrrQIAWVPQNPY-LFAG--TIRENL--RLgrPDASDEELEAaleAAGLDEFvaalpDGLD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 436 --VEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAY-QG-TMLFVSHDRRFLsALSNRVLE 511
Cdd:COG4988 465 tpLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLaKGrTVILITHRLALL-AQADRILV 543
|
.
gi 505055604 512 L 512
Cdd:COG4988 544 L 544
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-237 |
4.83e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 83.17 E-value: 4.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-----NSHRILYIeASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGE 75
Cdd:COG1136 4 LLELRNLTKSygtgeGEVTALRG-VSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLID--------GQDISS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 76 MAGRSAvaevmegagpvsavaAELR-----------ELetamsdpdrMDEMDAI--VErygeVQARYEELDGYALEGRAR 142
Cdd:COG1136 75 LSEREL---------------ARLRrrhigfvfqffNL---------LPELTALenVA----LPLLLAGVSRKERRERAR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 143 EVLA--GLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES------LiwLENFLKGYDGALLMT 214
Cdd:COG1136 127 ELLErvGLG---DRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevleL--LRELNRELGTTIVMV 201
|
250 260
....*....|....*....|...
gi 505055604 215 SHDREFMNRiVTKIIEIDGGALT 237
Cdd:COG1136 202 THDPELAAR-ADRVIRLRDGRIV 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-225 |
4.87e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 85.52 E-value: 4.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQvavekgmtIGYFDQDVGEMAGRSa 81
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGH--------IRFHGTDVSRLHARD- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 vaevmEGAGPVSAVAAELREletamsdpdrMDEMDAIVerYG-EVQARYEELDGYALEGRAREVLAGLSFSQeMMDGDVA 160
Cdd:PRK10851 74 -----RKVGFVFQHYALFRH----------MTVFDNIA--FGlTVLPRRERPNAAAIKAKVTQLLEMVQLAH-LADRYPA 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTS----HDR----EFMNRIV 225
Cdd:PRK10851 136 QLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSvfvtHDQeeamEVADRVV 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
27-236 |
5.37e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 83.02 E-value: 5.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDqdvgemagrsaVAEVMEGAGPVSA----VAAELREl 102
Cdd:cd03245 30 GEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD-GTDIRQLD-----------PADLRRNIGYVPQdvtlFYGTLRD- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 103 ETAMSDPDRMDE-MDAIVERYGEVQARYEELDGYALEGRARevlaglsfsqemmdGDvaKLSGGWKMRVALARILLMRPD 181
Cdd:cd03245 97 NITLGAPLADDErILRAAELAGVTDFVNKHPNGLDLQIGER--------------GR--GLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 182 AMLLDEPSNHLDLESLIWLENFLKGY--DGALLMTSHdREFMNRIVTKIIEIDGGAL 236
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLlgDKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
24-236 |
6.75e-18 |
|
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: 82.87 E-value: 6.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigYFD-QDVGEMA---------GRS----------AVA 83
Cdd:cd03219 23 VRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV---------LFDgEDITGLPpheiarlgiGRTfqiprlfpelTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 84 E-VMegagpvsaVAAELRELETAMSDPDRmDEMDAIVErygevqaryeeldgyalegRAREVLA--GLSfsqEMMDGDVA 160
Cdd:cd03219 94 EnVM--------VAAQARTGSGLLLARAR-REEREARE-------------------RAEELLErvGLA---DLADRPAG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPS---NHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:cd03219 143 ELSYGQQRRLEIARALATDPKLLLLDEPAaglNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-236 |
7.53e-18 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 82.46 E-value: 7.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEA-SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGRs 80
Cdd:cd03292 1 IEFINVTKTYPNGTAALDGiNISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVN--------GQDVSDLRGR- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 avaevmegagpvsAVAAELRELETAMSD----PDR------MDEMDAIVERYGEVQARYEE-LDGYALEGRAREVLAGls 149
Cdd:cd03292 72 -------------AIPYLRRKIGVVFQDfrllPDRnvyenvAFALEVTGVPPREIRKRVPAaLELVGLSHKHRALPAE-- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 150 fsqemmdgdvakLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGA---LLMTSHDREFMNRIVT 226
Cdd:cd03292 137 ------------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAgttVVVATHAKELVDTTRH 204
|
250
....*....|
gi 505055604 227 KIIEIDGGAL 236
Cdd:cd03292 205 RVIALERGKL 214
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-241 |
7.90e-18 |
|
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: 82.24 E-value: 7.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGeKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV------EKGM----TIGYFDQ 71
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlKQPQklrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 72 DVGEMAGRSAVAEVmegagpvsAVAAELREletaMSDPDRMDEMDAIVERYGevqaryeeldgyaLEGRArevlaglsfs 151
Cdd:cd03264 80 EFGVYPNFTVREFL--------DYIAWLKG----IPSKEVKARVDEVLELVN-------------LGDRA---------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 152 qemmDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLK--GYDGALLMTSHDREFMNRIVTKII 229
Cdd:cd03264 125 ----KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSelGEDRIVILSTHIVEDVESLCNQVA 200
|
250
....*....|..
gi 505055604 230 EIDGGALtTYSG 241
Cdd:cd03264 201 VLNKGKL-VFEG 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
335-512 |
9.52e-18 |
|
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: 80.72 E-value: 9.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLDGEsTILQWLEERF 414
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRV-----------------RLDGA-DISQWDPNEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 415 pkagqaplRALAGCFG-----FSGDDVEKrcrVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML---IKALS 486
Cdd:cd03246 75 --------GDHVGYLPqddelFSGSIAEN---ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALnqaIAALK 143
|
170 180
....*....|....*....|....*.
gi 505055604 487 AYQGTMLFVSHdRRFLSALSNRVLEL 512
Cdd:cd03246 144 AAGATRIVIAH-RPETLASADRILVL 168
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
21-236 |
1.30e-17 |
|
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: 82.78 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVGEMA---------GRS----------A 81
Cdd:COG0411 24 SLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL--------FDGRDITGLPphriarlgiARTfqnprlfpelT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VAE-VMegagpvsaVAAELRELETAMSDPDRMDemdaiverygevQARYEEldgYALEGRAREVLA--GLSfsqEMMDGD 158
Cdd:COG0411 96 VLEnVL--------VAAHARLGRGLLAALLRLP------------RARREE---REARERAEELLErvGLA---DRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 159 VAKLSGGWKMRVALARILLMRPDAMLLDEPS---NHLDLESLIWLENFLKGYDG-ALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAaglNPEETEELAELIRRLRDERGiTILLIEHDMDLVMGLADRIVVLDFG 229
|
..
gi 505055604 235 AL 236
Cdd:COG0411 230 RV 231
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-193 |
1.31e-17 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 82.35 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVGEMAGR 79
Cdd:COG1126 1 MIEIENLHKSfGDLEVLK-GISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVD-GEDLTDSKKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 --------------SAVAEVMEGagPVsavaaelreletamsdpdrmdemdaIVERYGEVQAryeeldgyalEGRAREVL 145
Cdd:COG1126 79 vgmvfqqfnlfphlTVLENVTLA--PI-------------------------KVKKMSKAEA----------EERAMELL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 146 A--GLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG1126 122 ErvGLA---DKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
335-512 |
1.44e-17 |
|
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: 82.55 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHS---MDLLDGESTILQWLE 411
Cdd:TIGR03873 12 GGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAGVDLHGLSRRARarrVALVEQDSDTAVPLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 412 ERFPKA-GQAPLRALAGcfGFSGDDVE--KRC--------------RVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLD 474
Cdd:TIGR03873 92 VRDVVAlGRIPHRSLWA--GDSPHDAAvvDRAlartelshladrdmSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505055604 475 LDTKEMLIKALS---AYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:TIGR03873 170 VRAQLETLALVRelaATGVTVVAALHDLNLAASYCDHVVVL 210
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-188 |
2.21e-17 |
|
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: 81.55 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGE--MAGR 79
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILID--------GQDITHlpMHER 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 SAVaevmeGAGPVSAVAAELRELETAmsdpdrmDEMDAIVErygevqaRYEELDGYALEGRAREVLAGLSFSQeMMDGDV 159
Cdd:TIGR04406 74 ARL-----GIGYLPQEASIFRKLTVE-------ENIMAVLE-------IRKDLDRAEREERLEALLEEFQISH-LRDNKA 133
|
170 180
....*....|....*....|....*....
gi 505055604 160 AKLSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:TIGR04406 134 MSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-193 |
2.34e-17 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 82.06 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-----NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVGe 75
Cdd:COG1116 7 ALELRGVSKRfptggGGVTALD-DVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVD-GKPVTGPGPDRG- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 76 MAG--------RSAVAEVMEGAGPVSAVAAELREletamsdpdrmdemdaiverygevqaryeeldgyalegRAREVLA- 146
Cdd:COG1116 84 VVFqepallpwLTVLDNVALGLELRGVPKAERRE--------------------------------------RARELLEl 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505055604 147 -GLSfsqemmdgDVAK-----LSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG1116 126 vGLA--------GFEDayphqLSGGMRQRVAIARALANDPEVLLMDEPFGALD 170
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-188 |
2.87e-17 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 81.23 E-value: 2.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE--------------KGmtI 66
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDgedithlpmhkrarLG--I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 67 GYFDQD--------VGE--MAgrsavaevmegagpvsavAAELRELetamSDPDRMDEMDAIVERYGevqaryeeldgya 136
Cdd:COG1137 81 GYLPQEasifrkltVEDniLA------------------VLELRKL----SKKEREERLEELLEEFG------------- 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505055604 137 LEGRaREVLAGLsfsqemmdgdvakLSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:COG1137 126 ITHL-RKSKAYS-------------LSGGERRRVEIARALATNPKFILLDEP 163
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-234 |
2.96e-17 |
|
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: 81.01 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGEMAG--- 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLI--------DGEDISGLSEael 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 ---RSAVAEVMEGAGPVSA------VAAELRElETAMSDPdrmdEMDAIVErygevqaryEELDgyalegrarevLAGLS 149
Cdd:cd03261 73 yrlRRRMGMLFQSGALFDSltvfenVAFPLRE-HTRLSEE----EIREIVL---------EKLE-----------AVGLR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 150 FSQEMMdgdVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD------LESLIWLENflKGYDGALLMTSHDREFMNR 223
Cdd:cd03261 128 GAEDLY---PAELSGGMKKRVALARALALDPELLLYDEPTAGLDpiasgvIDDLIRSLK--KELGLTSIMVTHDLDTAFA 202
|
250
....*....|.
gi 505055604 224 IVTKIIEIDGG 234
Cdd:cd03261 203 IADRIAVLYDG 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-235 |
3.31e-17 |
|
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: 80.94 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS------NSHRILYIE-ASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV--EKGM------- 64
Cdd:COG4778 4 LLEVENLSKTftlhlqGGKRLPVLDgVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWvdlaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 65 ----------TIGYFDQDVGEMAGRSAVAEVMEGagpvsavaaeLRELEtamsdpdrMDEMDAiverygevqaryeeldg 134
Cdd:COG4778 84 preilalrrrTIGYVSQFLRVIPRVSALDVVAEP----------LLERG--------VDREEA----------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 135 yalEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES---LIWLENFLKGYDGAL 211
Cdd:COG4778 129 ---RARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANravVVELIEEAKARGTAI 205
|
250 260
....*....|....*....|....
gi 505055604 212 LMTSHDREFMNRIVTKIIEIDGGA 235
Cdd:COG4778 206 IGIFHDEEVREAVADRVVDVTPFS 229
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
330-510 |
4.21e-17 |
|
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: 80.84 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 330 VHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV----KLGYFAQhsMDLLDGEST 405
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRR--IGVVFGQKT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 406 ILQW----------------LEERFPKAGQAPLRALAGCfgfsGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEP 469
Cdd:cd03267 105 QLWWdlpvidsfyllaaiydLPPARFKKRLDELSELLDL----EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505055604 470 TNHLDLDTKEMLIKALSAY----QGTMLFVSHDRRFLSALSNRVL 510
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVL 225
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
295-530 |
5.20e-17 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 84.50 E-value: 5.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 295 LEKIDRV--EPPRRRQTVAFEFLPAPRsGEdvVNLKSVHKTYG--SRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLV 370
Cdd:COG2274 445 LERLDDIldLPPEREEGRSKLSLPRLK-GD--IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 371 TGTTNPDKGSVSLG---------ASV--KLGYFAQHSMdLLDGesTILQ----WLeerfPKAGQAPLRA---LAGCFGF- 431
Cdd:COG2274 522 LGLYEPTSGRILIDgidlrqidpASLrrQIGVVLQDVF-LFSG--TIREnitlGD----PDATDEEIIEaarLAGLHDFi 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 432 ----SGDD--VEKRCRVLSGGEKARLVMA-AMLFDPPnFLVLDEPTNHLDLDTKEMLIKALSAYQG--TMLFVSHDrrfL 502
Cdd:COG2274 595 ealpMGYDtvVGEGGSNLSGGQRQRLAIArALLRNPR-ILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR---L 670
|
250 260 270
....*....|....*....|....*....|....*....
gi 505055604 503 SALSN--RVLEL---------TPDGINQYGGGYSEYVER 530
Cdd:COG2274 671 STIRLadRIIVLdkgrivedgTHEELLARKGLYAELVQQ 709
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
322-516 |
5.24e-17 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 80.09 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTYGS----RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV--------- 387
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIdGQDIsslserela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 388 -----KLGY-FAQHSmdLLDgESTILQ------WLEERFPKAGQAPLRALAGCFGFsGDDVEKRCRVLSGGEKARLVMA- 454
Cdd:COG1136 82 rlrrrHIGFvFQFFN--LLP-ELTALEnvalplLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIAr 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 455 AMLFDPPnfLVL-DEPTNHLDLDTKEM---LIKALSAYQG-TMLFVSHDRRfLSALSNRVLELTpDG 516
Cdd:COG1136 158 ALVNRPK--LILaDEPTGNLDSKTGEEvleLLRELNRELGtTIVMVTHDPE-LAARADRVIRLR-DG 220
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-236 |
5.51e-17 |
|
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: 80.11 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqdvgemAGRSA 81
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV----------------AGHDV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VAEVMEGAGPVSAVAAELrELETAMSDPDRMdemdaiverygEVQARYEELDGYALEGRAREVLAGLSFSqEMMDGDVAK 161
Cdd:cd03265 65 VREPREVRRRIGIVFQDL-SVDDELTGWENL-----------YIHARLYGVPGAERRERIDELLDFVGLL-EAADRLVKT 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESL--IW--LENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:cd03265 132 YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRahVWeyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRI 210
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-194 |
9.00e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.16 E-value: 9.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVG-----E 75
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVR--------LNGRPLAawspwE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 76 MAGRSAV-------------AEVME-GAGPVSAVAAELREL-ETAMsdpDRMDemdaiverygevqaryeeLDGYAleGR 140
Cdd:COG4559 73 LARRRAVlpqhsslafpftvEEVVAlGRAPHGSSAAQDRQIvREAL---ALVG------------------LAHLA--GR 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 141 arevlaglSFSQemmdgdvakLSGGWKMRVALARIL--LMRPDA-----MLLDEPSNHLDL 194
Cdd:COG4559 130 --------SYQT---------LSGGEQQRVQLARVLaqLWEPVDggprwLFLDEPTSALDL 173
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-234 |
1.13e-16 |
|
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: 83.34 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGM------------TIGYFDQDVgemagrsavaEVMEGAgp 91
Cdd:COG2274 498 IKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILID-GIdlrqidpaslrrQIGVVLQDV----------FLFSGT-- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 92 vsavaaeLRE-LetAMSDPDRmdEMDAIVErygevqaryeeldgyALEgrarevLAGL-SFSQEMMDG-------DVAKL 162
Cdd:COG2274 565 -------IREnI--TLGDPDA--TDEEIIE---------------AAR------LAGLhDFIEALPMGydtvvgeGGSNL 612
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 163 SGGWKMRVALARILLMRPDAMLLDEPSNHLD--LESLIwLENFLKGYDGA-LLMTSHDREFMnRIVTKIIEIDGG 234
Cdd:COG2274 613 SGGQRQRLAIARALLRNPRILILDEATSALDaeTEAII-LENLRRLLKGRtVIIIAHRLSTI-RLADRIIVLDKG 685
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-234 |
1.25e-16 |
|
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: 77.42 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYI--EASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmTIGyfDQDVGEMAG- 78
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVlkDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEI------LID--GVDLRDLDLe 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 --RSAVAEVmegagpvsavaaelreletamsdpdrmdemdaiverygevqaryeeldgyalegrarevlaglsfSQE--M 154
Cdd:cd03228 73 slRKNIAYV-----------------------------------------------------------------PQDpfL 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 155 MDGDVAK--LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES-LIWLENFLKGYDGA-LLMTSHdREFMNRIVTKIIE 230
Cdd:cd03228 88 FSGTIREniLSGGQRQRIAIARALLRDPPILILDEATSALDPETeALILEALRALAKGKtVIVIAH-RLSTIRDADRIIV 166
|
....
gi 505055604 231 IDGG 234
Cdd:cd03228 167 LDDG 170
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
2-234 |
1.46e-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: 79.47 E-value: 1.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqdvgemagrsa 81
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDL--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 vaevmeGAGPVSAVAAELRELETAMSDPDRMDEMDAIVErygEVQA--RYEELDGYALE-----GRAREVLAGLSFSqEM 154
Cdd:TIGR03873 61 ------AGVDLHGLSRRARARRVALVEQDSDTAVPLTVR---DVVAlgRIPHRSLWAGDsphdaAVVDRALARTELS-HL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 155 MDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDG---ALLMTSHDREFMNRIVTKIIEI 231
Cdd:TIGR03873 131 ADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAAtgvTVVAALHDLNLAASYCDHVVVL 210
|
...
gi 505055604 232 DGG 234
Cdd:TIGR03873 211 DGG 213
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-249 |
1.66e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.03 E-value: 1.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqdVGEmagrsa 81
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV------------LGV------ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 vaevmegagPVSAVAAELRELETAMSDPDRMDEMDAIVE------RYGEVQARYEE------LDGYALEGRArevlagls 149
Cdd:PRK13536 104 ---------PVPARARLARARIGVVPQFDNLDLEFTVREnllvfgRYFGMSTREIEavipslLEFARLESKA-------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 150 fsqemmDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES--LIW--LENFL-KGydGALLMTSHDREFMNRI 224
Cdd:PRK13536 167 ------DARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHArhLIWerLRSLLaRG--KTILLTTHFMEEAERL 238
|
250 260
....*....|....*....|....*
gi 505055604 225 VTKIIEIDGGALTTYSGDYGFYDEQ 249
Cdd:PRK13536 239 CDRLCVLEAGRKIAEGRPHALIDEH 263
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-234 |
1.71e-16 |
|
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: 77.23 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVGEMagRSA 81
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-GEDLTDLEDELPPL--RRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VAEVMEGAGPVSavaaelreletamsdpdRMDEMDAIVERygevqaryeeldgyalegrarevlaglsfsqemmdgdvak 161
Cdd:cd03229 78 IGMVFQDFALFP-----------------HLTVLENIALG---------------------------------------- 100
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLK------GYdgALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:cd03229 101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKslqaqlGI--TVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
341-510 |
2.00e-16 |
|
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: 78.40 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVK----------LGYFAQHSMdLLDGesTILQW 409
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLdGTDIRqldpadlrrnIGYVPQDVT-LFYG--TLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 410 LEERFPKAG-QAPLRA--LAGCFGFSGDD-------VEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKE 479
Cdd:cd03245 98 ITLGAPLADdERILRAaeLAGVTDFVNKHpngldlqIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEE 177
|
170 180 190
....*....|....*....|....*....|...
gi 505055604 480 MLIKALSAYQG--TMLFVSHDRRFLSaLSNRVL 510
Cdd:cd03245 178 RLKERLRQLLGdkTLIIITHRPSLLD-LVDRII 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
26-237 |
2.11e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 78.53 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqdvgemAGRsavaevmegagpvsavaaelreleta 105
Cdd:cd03267 46 KGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV----------------AGL-------------------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 106 msDPdrMDEMDAIVERYGEVQARYEEL-------DGYAL--------EGRAREVLAGLSFS---QEMMDGDVAKLSGGWK 167
Cdd:cd03267 84 --VP--WKRRKKFLRRIGVVFGQKTQLwwdlpviDSFYLlaaiydlpPARFKKRLDELSELldlEELLDTPVRQLSLGQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 168 MRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY----DGALLMTSHDREFMNRIVTKIIEIDGGALT 237
Cdd:cd03267 160 MRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnrerGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
2.49e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 79.85 E-value: 2.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGqvavekgmTIGYFDQDVGEMAgRSA 81
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAG--------SISLCGEPVPSRA-RHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VAEVmegagpvsAVAAELRELetamsDPD-RMDEMDAIVERY-----GEVQARYEELDGYA-LEGRArevlaglsfsqem 154
Cdd:PRK13537 79 RQRV--------GVVPQFDNL-----DPDfTVRENLLVFGRYfglsaAAARALVPPLLEFAkLENKA------------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 155 mDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES--LIW--LENFLkGYDGALLMTSHDREFMNRIVTKIIE 230
Cdd:PRK13537 133 -DAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQArhLMWerLRSLL-ARGKTILLTTHFMEEAERLCDRLCV 210
|
....
gi 505055604 231 IDGG 234
Cdd:PRK13537 211 IEEG 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
320-514 |
2.60e-16 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 78.98 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 320 SGEDVVNLKSVHKTY----GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL------GASVKL 389
Cdd:COG1116 3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 390 GYFAQhsmdlldgESTILQWL-----------------EERFPKAgqaplRALAGCFGFSGdDVEKRCRVLSGGEKARLV 452
Cdd:COG1116 83 GVVFQ--------EPALLPWLtvldnvalglelrgvpkAERRERA-----RELLELVGLAG-FEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 453 MA-AMLFDPPnFLVLDEPTNHLDLDTKEM----LIKALSAYQGTMLFVSHDrrfLS---ALSNRVLELTP 514
Cdd:COG1116 149 IArALANDPE-VLLMDEPFGALDALTRERlqdeLLRLWQETGKTVLFVTHD---VDeavFLADRVVVLSA 214
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
334-498 |
2.92e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.27 E-value: 2.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 334 YGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHSM--DLLdgESTILQWLE 411
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRSEvpDSL--PLTVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 412 -ERFPKAGqaPLR--------ALAGCFGFSG-DDVEKR-CRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEM 480
Cdd:NF040873 80 mGRWARRG--LWRrltrddraAVDDALERVGlADLAGRqLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|.
gi 505055604 481 ---LIKALSAYQGTMLFVSHD 498
Cdd:NF040873 158 iiaLLAEEHARGATVVVVTHD 178
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-217 |
3.39e-16 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 77.99 E-value: 3.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITG-----QELPDEGQVAVEkGMTIgyFDQDVGE 75
Cdd:cd03260 1 IELRDLNVYyGDKHALK-DISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLD-GKDI--YDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 76 MAGRSAVAEVMEGAGPVsavaaelreletamsdpdRMDEMDAIveRYGeVQARyEELDGYALEGRAREVLAGLSFSQEMM 155
Cdd:cd03260 77 LELRRRVGMVFQKPNPF------------------PGSIYDNV--AYG-LRLH-GIKLKEELDERVEEALRKAALWDEVK 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 156 DG-DVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD------LESLIwLEnfLKGyDGALLMTSHD 217
Cdd:cd03260 135 DRlHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDpistakIEELI-AE--LKK-EYTIVIVTHN 199
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
355-522 |
3.41e-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: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV---------------KLGY-FAQHSmdlLDGESTILQWLEERFPKAG 418
Cdd:cd03297 28 IFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlfdsrkkinlppqqrKIGLvFQQYA---LFPHLNVRENLAFGLKRKR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 419 QAPLR----ALAGCFGFSGDdVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKAL----SAYQG 490
Cdd:cd03297 105 NREDRisvdELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNI 183
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 491 TMLFVSHDRRFLSALSNRVLELTpDGINQYGG 522
Cdd:cd03297 184 PVIFVTHDLSEAEYLADRIVVME-DGRLQYIG 214
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-188 |
4.19e-16 |
|
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: 77.58 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigYFD-QDVG--EMA 77
Cdd:cd03218 1 LRAENLSKRyGKRKVVN-GVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKI---------LLDgQDITklPMH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRSAVaevmeGAGPVSAVAAELRELETAmsdpdrmDEMDAIVERYGEVQARYEEldgyalegRAREVLAGLSFsQEMMDG 157
Cdd:cd03218 71 KRARL-----GIGYLPQEASIFRKLTVE-------ENILAVLEIRGLSKKEREE--------KLEELLEEFHI-THLRKS 129
|
170 180 190
....*....|....*....|....*....|.
gi 505055604 158 DVAKLSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:cd03218 130 KASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
327-514 |
4.30e-16 |
|
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: 77.51 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSR----TIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL------GASVKLGYFAQhs 396
Cdd:cd03293 3 VRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVdgepvtGPGPDRGYVFQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 mdlldgESTILQW----------LEERFPKAGQAPLRALA-----GCFGFSGddveKRCRVLSGGEKARLVMA-AMLFDP 460
Cdd:cd03293 81 ------QDALLPWltvldnvalgLELQGVPKAEARERAEEllelvGLSGFEN----AYPHQLSGGMRQRVALArALAVDP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 461 PnFLVLDEPTNHLDLDTKEM----LIKALSAYQGTMLFVSHDrrfLS---ALSNRVLELTP 514
Cdd:cd03293 151 D-VLLLDEPFSALDALTREQlqeeLLDIWRETGKTVLLVTHD---IDeavFLADRVVVLSA 207
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
325-510 |
5.10e-16 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 77.54 E-value: 5.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV-------------KLG 390
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdGEDIsglseaelyrlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 391 YFAQH-----SMDLLDgesTILQWLEERFpKAGQAPLRALA----GCFGFSGdDVEKRCRVLSGGEKARLVMA-AMLFDP 460
Cdd:cd03261 81 MLFQSgalfdSLTVFE---NVAFPLREHT-RLSEEEIREIVleklEAVGLRG-AEDLYPAELSGGMKKRVALArALALDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505055604 461 PnFLVLDEPTNHLDLDTKEM---LIKALS-AYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:cd03261 156 E-LLLYDEPTAGLDPIASGViddLIRSLKkELGLTSIMVTHDLDTAFAIADRIA 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-237 |
5.22e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.44 E-value: 5.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIgyfdqdvgeMAGRS 80
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVD-GLKV---------NDPKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEGAGPVSA---VAAELRELETAMSDPDRmdemdaiVERYGEVQAryeeldgyalEGRAREVLA--GLSfsqEMM 155
Cdd:PRK09493 71 DERLIRQEAGMVFQqfyLFPHLTALENVMFGPLR-------VRGASKEEA----------EKQARELLAkvGLA---ERA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 156 DGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLE---SLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEID 232
Cdd:PRK09493 131 HHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPElrhEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFID 210
|
....*
gi 505055604 233 GGALT 237
Cdd:PRK09493 211 KGRIA 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
327-510 |
6.16e-16 |
|
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: 77.77 E-value: 6.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL------GAS-------------- 386
Cdd:COG0411 7 VRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFdgrditGLPphriarlgiartfq 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 387 -------------VKLGYFAQHSMDLLDGESTILQWLEERfpKAGQAPLRALAGCFGFsGDDVEKRCRVLSGGEKARLVM 453
Cdd:COG0411 87 nprlfpeltvlenVLVAAHARLGRGLLAALLRLPRARREE--REARERAEELLERVGL-ADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 454 A-AMLFDPPnFLVLDEPT---NHldLDTKEM--LIKALSAYQG-TMLFVSHDRRFLSALSNRVL 510
Cdd:COG0411 164 ArALATEPK-LLLLDEPAaglNP--EETEELaeLIRRLRDERGiTILLIEHDMDLVMGLADRIV 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
327-516 |
8.16e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.41 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVsLGASVKLGYfAQHSMDLLDGESTI 406
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAE-AREDTRLMFQDARL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 LQWlEERFPKAG--------QAPLRALAGCfGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK 478
Cdd:PRK11247 93 LPW-KKVIDNVGlglkgqwrDAALQALAAV-GLA-DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505055604 479 -EM--LIKALSAYQG-TMLFVSHDRRFLSALSNRVLeLTPDG 516
Cdd:PRK11247 170 iEMqdLIESLWQQHGfTVLLVTHDVSEAVAMADRVL-LIEEG 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
327-498 |
8.64e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 78.23 E-value: 8.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRErwcIMGI---NGAGKSTLLKLVTGTTNPDKGSVSL-GASVK-------------- 388
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGE---IFGLlgpNGAGKTTTIRIILGILAPDSGEVLWdGEPLDpedrrrigylpeer 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 389 -----------LGYFAQ-HSMDLLDGESTILQWLeERFpkagqaplralaGCFGFSGDDVEKrcrvLSGGEKARL-VMAA 455
Cdd:COG4152 81 glypkmkvgeqLVYLARlKGLSKAEAKRRADEWL-ERL------------GLGDRANKKVEE----LSKGNQQKVqLIAA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505055604 456 MLFDpPNFLVLDEPTNHLDLDTKEML---IKALSAyQG-TMLFVSHD 498
Cdd:COG4152 144 LLHD-PELLILDEPFSGLDPVNVELLkdvIRELAA-KGtTVIFSSHQ 188
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-225 |
9.11e-16 |
|
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: 76.84 E-value: 9.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS--NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE-KGMT------------- 65
Cdd:cd03256 1 IEVENLSKTypNGKKALK-DVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgTDINklkgkalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 66 IGYFDQD---VGEMagrSAVAEVMEGA-GPVSAVAAELR-----ELETAMsdpdrmdemdAIVERYGevqaryeeLDGYA 136
Cdd:cd03256 80 IGMIFQQfnlIERL---SVLENVLSGRlGRRSTWRSLFGlfpkeEKQRAL----------AALERVG--------LLDKA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 137 LegrARevlaglsfsqemmdgdVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLE-SLIWLENFL---KGYDGALL 212
Cdd:cd03256 139 Y---QR----------------ADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKrinREEGITVI 199
|
250
....*....|....*..
gi 505055604 213 MTSHD----REFMNRIV 225
Cdd:cd03256 200 VSLHQvdlaREYADRIV 216
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-234 |
9.19e-16 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.10 E-value: 9.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV-------------EKGMT- 65
Cdd:PRK11264 3 AIEVKNLVKKfHGQTVLH-GIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarslsqQKGLIr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 66 -----IGYFDQDVGEMAGRSAVAEVMEGagPVsAVAAELRELETAmsdpdrmdemdaiverygevqaryeeldgyalegR 140
Cdd:PRK11264 82 qlrqhVGFVFQNFNLFPHRTVLENIIEG--PV-IVKGEPKEEATA----------------------------------R 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 141 AREVLA--GLSFSQemmDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTS 215
Cdd:PRK11264 125 ARELLAkvGLAGKE---TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLaqeKRTMVIVT 201
|
250
....*....|....*....
gi 505055604 216 HDREFMNRIVTKIIEIDGG 234
Cdd:PRK11264 202 HEMSFARDVADRAIFMDQG 220
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
328-475 |
1.08e-15 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.08 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 328 KSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGA-----------SVKLGYFAQHS 396
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelARRRAVLPQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 -------------MDLldgestiLQWLEERfPKAGQAPLRALA--GCFGFSGddveKRCRVLSGGEKARL----VMA--- 454
Cdd:COG4559 85 slafpftveevvaLGR-------APHGSSA-AQDRQIVREALAlvGLAHLAG----RSYQTLSGGEQQRVqlarVLAqlw 152
|
170 180
....*....|....*....|.
gi 505055604 455 AMLFDPPNFLVLDEPTNHLDL 475
Cdd:COG4559 153 EPVDGGPRWLFLDEPTSALDL 173
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
23-217 |
1.32e-15 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 75.15 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 23 ALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYfdqdvgemaGRSAVAEVMegagpvsavaaelREL 102
Cdd:TIGR01166 14 AAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLID-GEPLDY---------SRKGLLERR-------------QRV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 103 ETAMSDPDrmDEM-DAIVERYGEVQARYEELDGYALEGRAREVLAGLSFSqEMMDGDVAKLSGGWKMRVALARILLMRPD 181
Cdd:TIGR01166 71 GLVFQDPD--DQLfAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGAS-GLRERPTHCLSGGEKKRVAIAGAVAMRPD 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 505055604 182 AMLLDEPSNHLDLESLIWLENFLKGYDGA---LLMTSHD 217
Cdd:TIGR01166 148 VLLLDEPTAGLDPAGREQMLAILRRLRAEgmtVVISTHD 186
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
27-236 |
1.63e-15 |
|
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: 75.41 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV--------EKGMT-------IGYFDQDVG---EMAGRSAVAEVMEG 88
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLngtvlfdsRKKINlppqqrkIGLVFQQYAlfpHLNVRENLAFGLKR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 89 AGPvsavaAELRELETAMSDpdRMDeMDAIVERYgevqaryeeldgyalegrarevlaglsfsqemmdgdVAKLSGGWKM 168
Cdd:cd03297 103 KRN-----REDRISVDELLD--LLG-LDHLLNRY------------------------------------PAQLSGGEKQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 169 RVALARILLMRPDAMLLDEPSNHLD----LESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:cd03297 139 RVALARALAAQPELLLLDEPFSALDralrLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-219 |
1.74e-15 |
|
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: 75.74 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqdvgemagrsa 81
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILL--------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 vaevmeGAGPVSAVAAELRELETAMSD---------------PDRMDEMDAiveryGEVQARYEE-LDGYALEGRAREvl 145
Cdd:cd03300 60 ------DGKDITNLPPHKRPVNTVFQNyalfphltvfeniafGLRLKKLPK-----AEIKERVAEaLDLVQLEGYANR-- 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 146 aglsfsqemmdgDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL----ESLIWLENFLKGYDGALLMTSHDRE 219
Cdd:cd03300 127 ------------KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLklrkDMQLELKRLQKELGITFVFVTHDQE 192
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
325-510 |
2.06e-15 |
|
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: 75.26 E-value: 2.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV------------KLGY 391
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIdGLKLtddkkninelrqKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 FAQH-----SMDLLDGESTILQWLEERFPKAGQAPLRALAGCFGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVL 466
Cdd:cd03262 81 VFQQfnlfpHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMNPKVMLF 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505055604 467 DEPTNHLDLDT-KEML--IKALSAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:cd03262 160 DEPTSALDPELvGEVLdvMKDLAEEGMTMVVVTHEMGFAREVADRVI 206
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
9-234 |
2.07e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 9 KSNSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVeKGMTIGYFDQDvGEMAGRSAVAEVMEG 88
Cdd:PRK10419 21 KHQHQTVLN-NVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKLNRA-QRKAFRRDIQMVFQD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 89 AgpVSAV----------AAELRELeTAMSDPDRmdemdaiverygevqaryeeldgyalEGRAREVLAGLSFSQEMMDGD 158
Cdd:PRK10419 98 S--ISAVnprktvreiiREPLRHL-LSLDKAER--------------------------LARASEMLRAVDLDDSVLDKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 159 VAKLSGGWKMRVALARILLMRPDAMLLDEP-SN---HLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:PRK10419 149 PPQLSGGQLQRVCLARALAVEPKLLILDEAvSNldlVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNG 228
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-216 |
2.50e-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: 74.70 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 5 ENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEmaGRSAVAE 84
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWN--------GTPLAE--QRDEPHE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 85 VMEGAGPVSAVAAELRELET-----AMSDPDRMDEMDAIvERYGevqaryeeLDGYAlegrarevlaglsfsqemmDGDV 159
Cdd:TIGR01189 74 NILYLGHLPGLKPELSALENlhfwaAIHGGAQRTIEDAL-AAVG--------LTGFE-------------------DLPA 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 160 AKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSH 216
Cdd:TIGR01189 126 AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
336-516 |
2.51e-15 |
|
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: 73.73 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 336 SRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHsmdlldgestilqwleerfP 415
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQR-------------------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 416 KAGQAPLRAlAGCFGFSgddvekrcRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQGTMLFV 495
Cdd:cd03223 74 YLPLGTLRE-QLIYPWD--------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISV 144
|
170 180
....*....|....*....|.
gi 505055604 496 SHdRRFLSALSNRVLELTPDG 516
Cdd:cd03223 145 GH-RPSLWKFHDRVLDLDGEG 164
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
21-236 |
2.89e-15 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 76.00 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVGEMAGRSAvaevmegagpvsavAAELR 100
Cdd:TIGR02769 31 SLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVS--------FRGQDLYQLDRKQR--------------RAFRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 ELETAMSD-PDRMDEMDAIVERYGEVQARYEELDGYALEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMR 179
Cdd:TIGR02769 89 DVQLVFQDsPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVK 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 180 PDAMLLDEPSNHLDL----ESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:TIGR02769 169 PKLIVLDEAVSNLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
335-512 |
2.96e-15 |
|
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: 78.48 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG------ASVK-----LGYFAQHSMdLLDGe 403
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNgvpladADADswrdqIAWVPQHPF-LFAG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 404 sTILQWLEERFPKAGQAPLRA---LAGCFGF-----SGDDVE--KRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHL 473
Cdd:TIGR02857 411 -TIAENIRLARPDASDAEIREaleRAGLDEFvaalpQGLDTPigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505055604 474 DLDTKEMLIKALSAY-QG-TMLFVSHdRRFLSALSNRVLEL 512
Cdd:TIGR02857 490 DAETEAEVLEALRALaQGrTVLLVTH-RLALAALADRIVVL 529
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
337-516 |
3.36e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 78.31 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 337 RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHSM----DLLD----------- 401
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYlplgTLREallypataeaf 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 402 GESTILQWLEerfpKAGqapLRALAGCFgfsgDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML 481
Cdd:COG4178 456 SDAELREALE----AVG---LGHLAERL----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAAL 524
|
170 180 190
....*....|....*....|....*....|....*..
gi 505055604 482 IKALSA--YQGTMLFVSHdRRFLSALSNRVLELTPDG 516
Cdd:COG4178 525 YQLLREelPGTTVISVGH-RSTLAAFHDRVLELTGDG 560
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
21-237 |
3.74e-15 |
|
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: 78.26 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDvgemAGRSAVAEVmeGAGPVsAVAAELR 100
Cdd:COG4988 357 SLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIN-GVDLSDLDPA----SWRRQIAWV--PQNPY-LFAGTIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 E-LetAMSDPDRMDEmdaiverygEVQAryeeldgyALEgrarevLAGL-SFSQEMMDG-------DVAKLSGGWKMRVA 171
Cdd:COG4988 429 EnL--RLGRPDASDE---------ELEA--------ALE------AAGLdEFVAALPDGldtplgeGGRGLSGGQAQRLA 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 172 LARILLMRPDAMLLDEPSNHLDLES--LIW--LENFLKGYdgALLMTSHDREFMNRiVTKIIEIDGGALT 237
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETeaEILqaLRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIV 550
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
24-234 |
5.83e-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: 74.74 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQvavekgmTIGYFDQDVgemaGRSAVAEVMEGAGPVS-AVAAELREL 102
Cdd:COG1119 26 VKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGN-------DVRLFGERR----GGEDVWELRKRIGLVSpALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 103 ETAmsdpdrmdeMDAIVE-RYGEVqARYEELDgYALEGRAREVLA--GLSfsqEMMDGDVAKLSGGWKMRVALARILLMR 179
Cdd:COG1119 95 ETV---------LDVVLSgFFDSI-GLYREPT-DEQRERARELLEllGLA---HLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 180 PDAMLLDEPSNHLDLES----LIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:COG1119 161 PELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDG 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-194 |
6.07e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 76.29 E-value: 6.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqdvgemAGR 79
Cdd:COG3842 5 ALELENVSKRyGDVTALD-DVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILL----------------DGR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 savaevmegagPVSAVAAELRELET-----A----MSdpdrmdemdaiVER---YGevqARYEELDGYALEGRAREVLA- 146
Cdd:COG3842 68 -----------DVTGLPPEKRNVGMvfqdyAlfphLT-----------VAEnvaFG---LRMRGVPKAEIRARVAELLEl 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505055604 147 -GLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL 194
Cdd:COG3842 123 vGLE---GLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDA 168
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
325-497 |
6.17e-15 |
|
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: 73.12 E-value: 6.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYG--SRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLDG 402
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI-----------------TLDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 E--STILQWLEERFPKAGQAPlralagcFGFSGDDVEKRCRVLSGGEKARLVMA-AMLFDPPnFLVLDEPTNHLDLDTKE 479
Cdd:cd03247 64 VpvSDLEKALSSLISVLNQRP-------YLFDTTLRNNLGRRFSGGERQRLALArILLQDAP-IVLLDEPTVGLDPITER 135
|
170 180
....*....|....*....|
gi 505055604 480 MLIKAL--SAYQGTMLFVSH 497
Cdd:cd03247 136 QLLSLIfeVLKDKTLIWITH 155
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-195 |
7.04e-15 |
|
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: 73.72 E-value: 7.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVGEMagRSA 81
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIID-GLKLTDDKKNINEL--RQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 VAEVMEGAgpvsAVAAELRELETAMSDPDRMDEMDAIverygEVQAR-YEELDGYALEGRArevlaglsfsqemmDGDVA 160
Cdd:cd03262 78 VGMVFQQF----NLFPHLTVLENITLAPIKVKGMSKA-----EAEERaLELLEKVGLADKA--------------DAYPA 134
|
170 180 190
....*....|....*....|....*....|....*
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLE 195
Cdd:cd03262 135 QLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-234 |
8.52e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 8.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILyiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAgrs 80
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN--------GQDLTALP--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 avaevmEGAGPVSAVAAE--------------------LReletaMSDPDRmDEMDAIVERYGevqaryeeldgyalegr 140
Cdd:COG3840 68 ------PAERPVSMLFQEnnlfphltvaqniglglrpgLK-----LTAEQR-AQVEQALERVG----------------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 141 arevLAGlsfsqeMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD----LESLIWLENFLKGYDGALLMTSH 216
Cdd:COG3840 119 ----LAG------LLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRERGLTVLMVTH 188
|
250
....*....|....*...
gi 505055604 217 DREFMNRIVTKIIEIDGG 234
Cdd:COG3840 189 DPEDAARIADRVLLVADG 206
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
341-512 |
9.14e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 73.96 E-value: 9.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVklgyfaqhsmdlldgestilqwleerfpkagqA 420
Cdd:COG1134 43 KDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRV--------------------------------S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 421 PLRALAGCF-----------------GFSGDDVEKRC-----------------RVLSGGEKARLVMAAMLFDPPNFLVL 466
Cdd:COG1134 91 ALLELGAGFhpeltgreniylngrllGLSRKEIDEKFdeivefaelgdfidqpvKTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505055604 467 DEPTNHLDLDTKE---MLIKALSAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:COG1134 171 DEVLAVGDAAFQKkclARIRELRESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-216 |
9.48e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 9.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVGemAGRS 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL--------WQGEPIR--RQRD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEGAGPVSAVAAELRELET-----AMSDPDRMDEMDAIVERYGevqaryeeldgyaLEGRarevlaglsfsqemM 155
Cdd:PRK13538 71 EYHQDLLYLGHQPGIKTELTALENlrfyqRLHGPGDDEALWEALAQVG-------------LAGF--------------E 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 156 DGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFL-----KGydGALLMTSH 216
Cdd:PRK13538 124 DVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALLaqhaeQG--GMVILTTH 187
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-233 |
1.07e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGqvAVEKGMTIGYFDQDVGEmagrsavaevmEGAGPVSAVaaeLREle 103
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG--EVDPELKISYKPQYIKP-----------DYDGTVEDL---LRS-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 104 tamsdpdrmdemdaIVERYGEVQARYEELDGYALEgrarevlaglsfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAM 183
Cdd:PRK13409 424 --------------ITDDLGSSYYKSEIIKPLQLE--------------RLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505055604 184 LLDEPSNHLDLESLI----WLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDG 233
Cdd:PRK13409 476 LLDEPSAHLDVEQRLavakAIRRIAEEREATALVVDHDIYMIDYISDRLMVFEG 529
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
323-512 |
1.36e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 323 DVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHSMdlLDg 402
Cdd:PRK09544 3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY--LD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 esTILQWLEERF----PKAGQAP-LRALAGCfgFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDT 477
Cdd:PRK09544 80 --TTLPLTVNRFlrlrPGTKKEDiLPALKRV--QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 505055604 478 KEMLIKALSAYQGTM----LFVSHDRRFLSALSNRVLEL 512
Cdd:PRK09544 156 QVALYDLIDQLRRELdcavLMVSHDLHLVMAKTDEVLCL 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
322-512 |
1.37e-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: 76.10 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTY--GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTnPDKGSVS----------LGASVKL 389
Cdd:COG1123 2 TPLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISgevlldgrdlLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 390 -----GYFAQHSMDLLDGeSTILQWLEErfpkagqaPLRALagcfGFSGDDVEKRCR-----------------VLSGGE 447
Cdd:COG1123 81 rgrriGMVFQDPMTQLNP-VTVGDQIAE--------ALENL----GLSRAEARARVLelleavglerrldryphQLSGGQ 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 448 KARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEM---LIKALSAYQG-TMLFVSHDRRFLSALSNRVLEL 512
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEildLLRELQRERGtTVLLITHDLGVVAEIADRVVVM 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
330-510 |
1.43e-14 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 73.24 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 330 VHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG----------ASVKLGY---FaQH- 395
Cdd:cd03219 6 LTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglpphEIARLGIgrtF-QIp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 ----SMDLLD----------GESTILQWLEERFPKAGQAPLRALAgcfgFSG--DDVEKRCRVLSGGEKARLVMAAMLFD 459
Cdd:cd03219 85 rlfpELTVLEnvmvaaqartGSGLLLARARREEREARERAEELLE----RVGlaDLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505055604 460 PPNFLVLDEPTNHLDLD-TKEM--LIKALSAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEeTEELaeLIRELRERGITVLLVEHDMDVVMSLADRVT 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-217 |
1.47e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGemagrs 80
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 avaevMEGAGPVSaVAAELReLETAMSDPDRMDEMDaiverygEVQAryeeldgyalegrarevlaglsfsQEMMDGDVA 160
Cdd:PRK09544 78 -----LDTTLPLT-VNRFLR-LRPGTKKEDILPALK-------RVQA------------------------GHLIDAPMQ 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWL----ENFLKGYDGALLMTSHD 217
Cdd:PRK09544 120 KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydliDQLRRELDCAVLMVSHD 180
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
325-512 |
1.48e-14 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 72.70 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSV-----SLGASVK----------- 388
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkPLDIAARnrigylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 389 ----------LGYFAQ-HSMDLLDGESTILQWLEErfpkagqaplralagcFGFSgDDVEKRCRVLSGGEKARLVMAAML 457
Cdd:cd03269 81 lypkmkvidqLVYLAQlKGLKKEEARRRIDEWLER----------------LELS-EYANKRVEELSKGNQQKVQFIAAV 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 458 FDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG---TMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARagkTVILSTHQMELVEELCDRVLLL 201
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
21-217 |
1.55e-14 |
|
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: 76.25 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtiGYFDQDVGEMAGRSAVAEVMEGAgpvSAVAAELR 100
Cdd:TIGR02868 355 SLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLD-----GVPVSSLDQDEVRRRVSVCAQDA---HLFDTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 ElETAMSDPDRMD-EMDAIVERYGevqaryeeldgyaLEGRAREVLAGLSFSqemMDGDVAKLSGGWKMRVALARILLMR 179
Cdd:TIGR02868 427 E-NLRLARPDATDeELWAALERVG-------------LADWLRALPDGLDTV---LGEGGARLSGGERQRLALARALLAD 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505055604 180 PDAMLLDEPSNHLDLE-SLIWLENFLKGYDG-ALLMTSHD 217
Cdd:TIGR02868 490 APILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
330-475 |
1.59e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 73.65 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 330 VHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVK----------LGYFAQHS-- 396
Cdd:PRK13548 8 LSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLnGRPLAdwspaelarrRAVLPQHSsl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 -----------MDLLDgestilqwLEERFPKAGQAPLRALA--GCFGFSGDDVekrcRVLSGGEKARLVMAAML------ 457
Cdd:PRK13548 88 sfpftveevvaMGRAP--------HGLSRAEDDALVAAALAqvDLAHLAGRDY----PQLSGGEQQRVQLARVLaqlwep 155
|
170
....*....|....*...
gi 505055604 458 FDPPNFLVLDEPTNHLDL 475
Cdd:PRK13548 156 DGPPRWLLLDEPTSALDL 173
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-510 |
1.65e-14 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.39 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGQELPDEGqvavekgmtigyfdqDVGEMAGRSAVAEVMEGagpvSAVAAELRELeta 105
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLG---------------DYEEEPSWDEVLKRFRG----TELQNYFKKL--- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 106 msdpdRMDEMDAIVE-RYGEVQARY------EELDGYALEGRAREVLAGLSFSqEMMDGDVAKLSGGWKMRVALARILLM 178
Cdd:PRK13409 156 -----YNGEIKVVHKpQYVDLIPKVfkgkvrELLKKVDERGKLDEVVERLGLE-NILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 179 RPDAMLLDEPSNHLDLESLIWLENFLKGY--DGALLMTSHDREFMNrIVTKIIEIdggaltTY--SGDYGF----YDEQR 250
Cdd:PRK13409 230 DADFYFFDEPTSYLDIRQRLNVARLIRELaeGKYVLVVEHDLAVLD-YLADNVHI------AYgePGAYGVvskpKGVRV 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 251 ALNArqqqaqferqqamlakeikFIERFKARashasqvqsrvkklEKIdRVepprRRQTVAFEFLPAPR--SGEDVVNLK 328
Cdd:PRK13409 303 GINE-------------------YLKGYLPE--------------ENM-RI----RPEPIEFEERPPRDesERETLVEYP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 329 SVHKTYGSRTiydgLDFM---VRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSlgASVKLGYFAQHSMDllDGEST 405
Cdd:PRK13409 345 DLTKKLGDFS----LEVEggeIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD--PELKISYKPQYIKP--DYDGT 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 406 ILQWLEERFPKAGQAPLRA-LAgcFGFSGDDV-EKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIK 483
Cdd:PRK13409 417 VEDLLRSITDDLGSSYYKSeII--KPLQLERLlDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAK 494
|
490 500 510
....*....|....*....|....*....|.
gi 505055604 484 ALSAY----QGTMLFVSHDRRFLSALSNRVL 510
Cdd:PRK13409 495 AIRRIaeerEATALVVDHDIYMIDYISDRLM 525
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-237 |
1.65e-14 |
|
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: 76.34 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS--NSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmTIGyfDQDVGEMAG- 78
Cdd:COG4987 334 LELEDVSFRypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI------TLG--GVDLRDLDEd 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 --RSAVAeVMEGAGPV--SAVAAELReletaMSDPDrmdemdaiverygevqaryeeldgyALEGRAREVL--AGLS-FS 151
Cdd:COG4987 406 dlRRRIA-VVPQRPHLfdTTLRENLR-----LARPD-------------------------ATDEELWAALerVGLGdWL 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 152 QEMMDG-------DVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES-LIWLENFLKGYDG-ALLMTSHDREFMN 222
Cdd:COG4987 455 AALPDGldtwlgeGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATeQALLADLLEALAGrTVLLITHRLAGLE 534
|
250
....*....|....*
gi 505055604 223 RiVTKIIEIDGGALT 237
Cdd:COG4987 535 R-MDRILVLEDGRIV 548
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-219 |
1.73e-14 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 73.14 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGRSa 81
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFG--------GEDATDVPVQE- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 82 vaevmEGAGPVSAVAAELREletamsdpdrMDEMDAIVerYG-EVQARYEELDGYALEGRAREVLAGLSFSQeMMDGDVA 160
Cdd:cd03296 74 -----RNVGFVFQHYALFRH----------MTVFDNVA--FGlRVKPRSERPPEAEIRAKVHELLKLVQLDW-LADRYPA 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTS----HDRE 219
Cdd:cd03296 136 QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTvfvtHDQE 198
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-223 |
1.82e-14 |
|
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: 75.79 E-value: 1.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDvgemAGRSAVAEVMEGAGPVSAVAAElr 100
Cdd:TIGR02857 342 SFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN-GVPLADADAD----SWRDQIAWVPQHPFLFAGTIAE-- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 elETAMSDPDRMD-EMDAIVERYGevqaryeeldgyalegrAREVLAGLSFSQEMMDGDV-AKLSGGWKMRVALARILLM 178
Cdd:TIGR02857 415 --NIRLARPDASDaEIREALERAG-----------------LDEFVAALPQGLDTPIGEGgAGLSGGQAQRLALARAFLR 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505055604 179 RPDAMLLDEPSNHLDLES-LIWLENFLKGYDGA-LLMTSHDREFMNR 223
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETeAEVLEALRALAQGRtVLLVTHRLALAAL 522
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-195 |
1.90e-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: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVG---EMAGRSAVAEVMEGAGPVSavaaelr 100
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-LDTVSYKPQYIKadyEGTVRDLLSSITKDFYTHP------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 ELETAMSDPDRMDemdaiverygevqaryeeldgyalegrarevlaglsfsqEMMDGDVAKLSGGWKMRVALARILLMRP 180
Cdd:cd03237 94 YFKTEIAKPLQIE---------------------------------------QILDREVPELSGGELQRVAIAACLSKDA 134
|
170
....*....|....*
gi 505055604 181 DAMLLDEPSNHLDLE 195
Cdd:cd03237 135 DIYLLDEPSAYLDVE 149
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
325-512 |
1.96e-14 |
|
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: 72.57 E-value: 1.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHSMDL-LDGE 403
Cdd:cd03220 23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGGGFNPeLTGR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 404 STI-----LQWLEERFPKAgqaplrALAGCFGFS--GDDVEKRCRVLSGGEKARLVMA-AMLFDpPNFLVLDEPTNHLDL 475
Cdd:cd03220 103 ENIylngrLLGLSRKEIDE------KIDEIIEFSelGDFIDLPVKTYSSGMKARLAFAiATALE-PDILLIDEVLAVGDA 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505055604 476 DTKE---MLIKALSAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd03220 176 AFQEkcqRRLRELLKQGKTVILVSHDPSSIKRLCDRALVL 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
324-512 |
2.09e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.39 E-value: 2.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTY-GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV-------------K 388
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVnGQDLsrlkrreipylrrR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 389 LGYFAQhsmD--LLDGEST----ILqwleerfpkagqaPLRALagcfGFSGDDVEKR-----------------CRVLSG 445
Cdd:COG2884 81 IGVVFQ---DfrLLPDRTVyenvAL-------------PLRVT----GKSRKEIRRRvrevldlvglsdkakalPHELSG 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 446 GEKARLVMA-AMLFDPPnFLVLDEPTNHLDLDTKE--M-LIKALSAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:COG2884 141 GEQQRVAIArALVNRPE-LLLADEPTGNLDPETSWeiMeLLEEINRRGTTVLIATHDLELVDRMPKRVLEL 210
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-219 |
2.21e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.50 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQdvgemagRSAVAEVMegagPVSAV-AAEL 99
Cdd:NF040873 12 DLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ-------RSEVPDSL----PLTVRdLVAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 100 -----RELETAMSDPDRMdEMDAIVERYGevqaryeeLDGyaLEGRArevlaglsfsqemmdgdVAKLSGGWKMRVALAR 174
Cdd:NF040873 81 grwarRGLWRRLTRDDRA-AVDDALERVG--------LAD--LAGRQ-----------------LGELSGGQRQRALLAQ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505055604 175 ILLMRPDAMLLDEPSNHLDLES---LIWLENFLKGYDGALLMTSHDRE 219
Cdd:NF040873 133 GLAQEADLLLLDEPTTGLDAESrerIIALLAEEHARGATVVVVTHDLE 180
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-216 |
3.44e-14 |
|
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: 71.37 E-value: 3.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 5 ENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGmtigyfdqdvGEMAGRSAVAE 84
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG----------PLDFQRDSIAR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 85 VMEGAGPVSAVAAELRELETAMSdpDRMDEMDAIVErygevqaryeeldgyalEGRAREVLAGLSfsqemmDGDVAKLSG 164
Cdd:cd03231 74 GLLYLGHAPGIKTTLSVLENLRF--WHADHSDEQVE-----------------EALARVGLNGFE------DRPVAQLSA 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 165 GWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSH 216
Cdd:cd03231 129 GQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHcarGGMVVLTTH 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-233 |
3.74e-14 |
|
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: 75.21 E-value: 3.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGqvAVEKGMTIGYFDQDVgemagrSAVAEvmegaGPVSAVaaeLRele 103
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEDLKISYKPQYI------SPDYD-----GTVEEF---LR--- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 104 tamsdpdrmdemDAIVERYGEVQARYEELDGYALEgrarevlaglsfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAM 183
Cdd:COG1245 424 ------------SANTDDFGSSYYKTEIIKPLGLE--------------KLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505055604 184 LLDEPSNHLDLESLI----WLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDG 233
Cdd:COG1245 478 LLDEPSAHLDVEQRLavakAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFEG 531
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
320-509 |
3.92e-14 |
|
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: 71.93 E-value: 3.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 320 SGEDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdL 399
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEI-----------------L 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 400 LDGestilqwleERFPKAGQAPLRALAGCFG--------FS----GDDV-------------EKRCRV------------ 442
Cdd:COG1127 64 VDG---------QDITGLSEKELYELRRRIGmlfqggalFDsltvFENVafplrehtdlseaEIRELVleklelvglpga 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 443 -------LSGGEKARLVMA-AMLFDPPnFLVLDEPTNHLDLDTKEM---LIKALS-AYQGTMLFVSHDRRFLSALSNRV 509
Cdd:COG1127 135 adkmpseLSGGMRKRVALArALALDPE-ILLYDEPTAGLDPITSAVideLIRELRdELGLTSVVVTHDLDSAFAIADRV 212
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
341-521 |
4.22e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 71.98 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV--------KLGYFAQH-----SMDLLDgesTI 406
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLnGKDItnlppekrDISYVPQNyalfpHMTVYK---NI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 LQWLEERFPKAGQAPLRAL--AGCFGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKA 484
Cdd:cd03299 93 AYGLKKRKVDKKEIERKVLeiAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505055604 485 LS----AYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:cd03299 172 LKkirkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
285-498 |
7.49e-14 |
|
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: 73.93 E-value: 7.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 285 ASQVQSRVKKLEKIDRVEPPRRRQTVAFEFLPAPrSGEDVVNLKSVHKTY---GSRTIYDGLDFMVRRRERWCIMGINGA 361
Cdd:TIGR02868 294 AQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGA-VGLGKPTLELRDLSAgypGAPPVLDGVSLDLPPGERVAILGPSGS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 362 GKSTLLKLVTGTTNPDKGSVSLG-----------ASVKLGYFAQ--HSMDlldgeSTILQWLEERFPKAGQAPLRA---- 424
Cdd:TIGR02868 373 GKSTLLATLAGLLDPLQGEVTLDgvpvssldqdeVRRRVSVCAQdaHLFD-----TTVRENLRLARPDATDEELWAaler 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 425 ------LAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDT-KEMLIKALSAYQG-TMLFVS 496
Cdd:TIGR02868 448 vgladwLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETaDELLEDLLAALSGrTVVLIT 527
|
..
gi 505055604 497 HD 498
Cdd:TIGR02868 528 HH 529
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
332-509 |
8.79e-14 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 70.48 E-value: 8.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 332 KTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV---------KLGYFAQHSMdlLD 401
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaGHDVvreprevrrRIGIVFQDLS--VD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 402 GESTilqwleerfpkaGQAPLRALAGCFGFSGDDVEKRCRVL-----------------SGGEKARLVMAAMLFDPPNFL 464
Cdd:cd03265 86 DELT------------GWENLYIHARLYGVPGAERRERIDELldfvglleaadrlvktySGGMRRRLEIARSLVHRPEVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505055604 465 VLDEPTNHLDLDTKEML---IKALSAYQG-TMLFVSHDRRFLSALSNRV 509
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVweyIEKLKEEFGmTILLTTHYMEEAEQLCDRV 202
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
29-252 |
9.63e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 74.13 E-value: 9.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 29 KIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQdvgemagrsavaevmegagpvsavaaelreletamsd 108
Cdd:PLN03073 537 RIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQ------------------------------------- 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 109 pDRMDEMDAIVERYGEVQARYEEldgyALEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:PLN03073 580 -HHVDGLDLSSNPLLYMMRCFPG----VPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 189 SNHLDLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTYSGDygFYDEQRAL 252
Cdd:PLN03073 655 SNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGT--FHDYKKTL 716
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
280-510 |
1.16e-13 |
|
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: 73.63 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 280 ARASHAsqvqsRVKKLEKIDRVEPPRRRqtvafefLPAPRSGEDVVNLkSVHKTYGSRTIYDGLDFMVRRRERWCIMGIN 359
Cdd:COG4618 301 ARQAYR-----RLNELLAAVPAEPERMP-------LPRPKGRLSVENL-TVVPPGSKRPILRGVSFSLEPGEVLGVIGPS 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 360 GAGKSTLLKLVTGTTNPDKGSVSL-GASVK----------LGYFAQhSMDLLDGesTIlqwlEE---RFPKA-GQAPLRA 424
Cdd:COG4618 368 GSGKSTLARLLVGVWPPTAGSVRLdGADLSqwdreelgrhIGYLPQ-DVELFDG--TI----AEniaRFGDAdPEKVVAA 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 425 --LAGC--------------FGFSGddvekrcRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML---IKAL 485
Cdd:COG4618 441 akLAGVhemilrlpdgydtrIGEGG-------ARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALaaaIRAL 513
|
250 260
....*....|....*....|....*
gi 505055604 486 SAYQGTMLFVSHDRRFLSAlSNRVL 510
Cdd:COG4618 514 KARGATVVVITHRPSLLAA-VDKLL 537
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
324-469 |
1.19e-13 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 70.65 E-value: 1.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKsvhKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG------------ASVKLGY 391
Cdd:cd03218 3 AENLS---KRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgqditklpmhkrARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 FAQHSMDL--LDGESTILQWLEER-FPKAGQAP-LRALAGCFGFSgdDVEKR-CRVLSGGEKARLVMAAMLFDPPNFLVL 466
Cdd:cd03218 80 LPQEASIFrkLTVEENILAVLEIRgLSKKEREEkLEELLEEFHIT--HLRKSkASSLSGGERRRVEIARALATNPKFLLL 157
|
...
gi 505055604 467 DEP 469
Cdd:cd03218 158 DEP 160
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
325-509 |
1.22e-13 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 70.09 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYG--SRTIY--DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG--ASVKLGYFAQHSMD 398
Cdd:cd03266 2 ITADALTKRFRdvKKTVQavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 399 LLDGESTILQWLEER-----F-------PKAGQAPLRALAGCFGFsGDDVEKRCRVLSGGEKARLVMA-AMLFDPPNfLV 465
Cdd:cd03266 82 FVSDSTGLYDRLTARenleyFaglyglkGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIArALVHDPPV-LL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505055604 466 LDEPTNHLDLDTKEML---IKALSAYQGTMLFVSHDRRFLSALSNRV 509
Cdd:cd03266 160 LDEPTTGLDVMATRALrefIRQLRALGKCILFSTHIMQEVERLCDRV 206
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
327-516 |
1.29e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 70.13 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV----------KLGYFAQH 395
Cdd:PRK10247 10 LQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFeGEDIstlkpeiyrqQVSYCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 SMdlLDGEST----ILQWLEERFPKAGQAPLRALAGcFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTN 471
Cdd:PRK10247 90 PT--LFGDTVydnlIFPWQIRNQQPDPAIFLDDLER-FALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505055604 472 HLDLDTK----EMLIKALSAYQGTMLFVSHDRRFLSALSNrVLELTPDG 516
Cdd:PRK10247 167 ALDESNKhnvnEIIHRYVREQNIAVLWVTHDKDEINHADK-VITLQPHA 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-194 |
1.61e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.57 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGRS 80
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVA--------GDDVEALSARA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 A---VAEVMEGAgpvsAVAAELReletamsdpdrmdeMDAIVE--------RYGevqaRYEELDGYALEgRAREVLAGLS 149
Cdd:PRK09536 75 AsrrVASVPQDT----SLSFEFD--------------VRQVVEmgrtphrsRFD----TWTETDRAAVE-RAMERTGVAQ 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505055604 150 FSqemmDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL 194
Cdd:PRK09536 132 FA----DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDI 172
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
24-193 |
1.90e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 70.88 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVeKGMTIGYfdqdvgemaGRSAVAEVMEGAGPVsavaaelrele 103
Cdd:PRK13639 25 AEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLI-KGEPIKY---------DKKSLLEVRKTVGIV----------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 104 taMSDPDrmDEMDA-IVER---YGEVQARYEELDgyaLEGRAREVLAGLSfsqemMDGDVAK----LSGGWKMRVALARI 175
Cdd:PRK13639 84 --FQNPD--DQLFApTVEEdvaFGPLNLGLSKEE---VEKRVKEALKAVG-----MEGFENKpphhLSGGQKKRVAIAGI 151
|
170
....*....|....*...
gi 505055604 176 LLMRPDAMLLDEPSNHLD 193
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLD 169
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-219 |
1.99e-13 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 71.79 E-value: 1.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGY---FDQDVGEMA 77
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD-GVDLSHvppYQRPINMMF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRSAVAEVMEGAgpvSAVAAELREletamsdpDRMDEmdaiveryGEVQARYEELdgyalegrarevlAGLSFSQEMMDG 157
Cdd:PRK11607 98 QSYALFPHMTVE---QNIAFGLKQ--------DKLPK--------AEIASRVNEM-------------LGLVHMQEFAKR 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 158 DVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD--LESLIWLE--NFLKGYDGALLMTSHDRE 219
Cdd:PRK11607 146 KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDkkLRDRMQLEvvDILERVGVTCVMVTHDQE 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-217 |
2.11e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.92 E-value: 2.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 5 ENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGRsavAE 84
Cdd:PRK10895 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID--------DEDISLLPLH---AR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 85 VMEGAGPVSAVAAELRELETamsdpdrMDEMDAIVErygevqaRYEELDGYALEGRAREVLAGLSFSQeMMDGDVAKLSG 164
Cdd:PRK10895 76 ARRGIGYLPQEASIFRRLSV-------YDNLMAVLQ-------IRDDLSAEQREDRANELMEEFHIEH-LRDSMGQSLSG 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 165 GWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENF---LKGYDGALLMTSHD 217
Cdd:PRK10895 141 GERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIiehLRDSGLGVLITDHN 196
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
324-510 |
2.37e-13 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 69.53 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTYGSR----TIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG--------------A 385
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllsgkelrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 386 SVKLGYFAQHsMDLLDGEsTILQ----WLE-ERFPKAGQA----PLRALAGCfgfsGDDVEKRCRVLSGGEKARLVMAAM 456
Cdd:cd03258 81 RRRIGMIFQH-FNLLSSR-TVFEnvalPLEiAGVPKAEIEervlELLELVGL----EDKADAYPAQLSGGQKQRVGIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 457 LFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG----TMLFVSHDRRFLSALSNRVL 510
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITHEMEVVKRICDRVA 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-239 |
2.53e-13 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 69.48 E-value: 2.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEK------GMTIGyFDqdvGEMAGRSAVaevmegagpvsavaa 97
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGrvssllGLGGG-FN---PELTGRENI--------------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 98 ELRELETAMSDPDRMDEMDAIVErygevqarYEELDGYalegrarevlaglsfsqemMDGDVAKLSGGWKMRVALARILL 177
Cdd:cd03220 106 YLNGRLLGLSRKEIDEKIDEIIE--------FSELGDF-------------------IDLPVKTYSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 178 MRPDAMLLDEP----SNHLDLESLIWLENFLKGyDGALLMTSHDREFMNRIVTKIIEIDGGALTTY 239
Cdd:cd03220 159 LEPDILLIDEVlavgDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-193 |
2.55e-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: 69.38 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS---NSHR--ILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE-------------- 61
Cdd:COG4181 8 IIELRGLTKTvgtGAGEltILK-GISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAgqdlfaldedarar 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 62 -KGMTIGYFDQDVGEMAGRSAVAEVMegagpvsaVAAELReletamsdpdrmdemdaiveryGEVQARyeeldgyaleGR 140
Cdd:COG4181 87 lRARHVGFVFQSFQLLPTLTALENVM--------LPLELA----------------------GRRDAR----------AR 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 141 AREVLA--GLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG4181 127 ARALLErvGLG---HRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-234 |
3.67e-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: 68.46 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE-KGMT------IGYFDQDV 73
Cdd:cd03269 1 LEVENVTKRfGRVTALD-DISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgKPLDiaarnrIGYLPEER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 74 GeMAGRSAVAEVMegagpvsAVAAELReletAMSDPDRMDEMDAIVERYGevqaryeeldgyaLEGRAREVlaglsfsqe 153
Cdd:cd03269 80 G-LYPKMKVIDQL-------VYLAQLK----GLKKEEARRRIDEWLERLE-------------LSEYANKR--------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 154 mmdgdVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD------LESLIwleNFLKGYDGALLMTSHDREFMNRIVTK 227
Cdd:cd03269 126 -----VEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDpvnvelLKDVI---RELARAGKTVILSTHQMELVEELCDR 197
|
....*..
gi 505055604 228 IIEIDGG 234
Cdd:cd03269 198 VLLLNKG 204
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-195 |
3.89e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.27 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQvavekgMTIG--YFD--QDVGEM 76
Cdd:COG4161 3 IQLKNINCFyGSHQALF-DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQ------LNIAghQFDfsQKPSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 AGRSAVAEVmegaGPVsavaAELRELETAMSDPDRMDEMDAIVERYGEVQARyeeldgyaleGRAREVLAGLSFsQEMMD 156
Cdd:COG4161 76 AIRLLRQKV----GMV----FQQYNLWPHLTVMENLIEAPCKVLGLSKEQAR----------EKAMKLLARLRL-TDKAD 136
|
170 180 190
....*....|....*....|....*....|....*....
gi 505055604 157 GDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLE 195
Cdd:COG4161 137 RFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-195 |
4.43e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 68.89 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGmtigYFD--QDVGEMAG 78
Cdd:PRK11124 3 IQLNGINCFyGAHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN----HFDfsKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 RSAVAEVmegaGPVSA---VAAELRELETAMSDPDRMDEMDaiverygEVQARyeeldgyaleGRAREVLAGLSFSqEMM 155
Cdd:PRK11124 78 RELRRNV----GMVFQqynLWPHLTVQQNLIEAPCRVLGLS-------KDQAL----------ARAEKLLERLRLK-PYA 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505055604 156 DGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLE 195
Cdd:PRK11124 136 DRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE 175
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-193 |
4.85e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEM 76
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTAlddvSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVD--------GVDLTAL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 AGRsavaevmegagpvsavaaELREL--ETAMsdpdrmdemdaIVERYGEVQAR--YE------ELDGY---ALEGRARE 143
Cdd:COG1135 73 SER------------------ELRAArrKIGM-----------IFQHFNLLSSRtvAEnvalplEIAGVpkaEIRKRVAE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 144 VLA--GLSfsqemmdgDVAK-----LSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG1135 124 LLElvGLS--------DKADaypsqLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
318-512 |
7.75e-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: 68.23 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 318 PRSGEDVVNLKSVHKTYGSR----TIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV----- 387
Cdd:COG4181 2 SSSSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLaGQDLfalde 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 388 ---------KLGyFAQHSMDLLDG----ESTILQwLEER-FPKAGQAPLRALA--GcfgfsgddVEKRC----RVLSGGE 447
Cdd:COG4181 82 dararlrarHVG-FVFQSFQLLPTltalENVMLP-LELAgRRDARARARALLErvG--------LGHRLdhypAQLSGGE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 448 KARlVMAAMLFDP-PNFLVLDEPTNHLDLDTKEMLIK---ALSAYQGTMLF-VSHDRRfLSALSNRVLEL 512
Cdd:COG4181 152 QQR-VALARAFATePAILFADEPTGNLDAATGEQIIDllfELNRERGTTLVlVTHDPA-LAARCDRVLRL 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
327-470 |
1.35e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 67.07 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG------------ASVKLGY--- 391
Cdd:cd03224 3 VENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgrditglppherARAGIGYvpe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 ----FAQHSMD--LLDGEST--------ILQWLEERFPKAGQApLRALAGcfgfsgddvekrcrVLSGGEKARLVMAAML 457
Cdd:cd03224 83 grriFPELTVEenLLLGAYArrrakrkaRLERVYELFPRLKER-RKQLAG--------------TLSGGEQQMLAIARAL 147
|
170
....*....|...
gi 505055604 458 FDPPNFLVLDEPT 470
Cdd:cd03224 148 MSRPKLLLLDEPS 160
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
31-237 |
1.39e-12 |
|
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: 68.99 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 31 GLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVGEMAGRSAVAEVMEGAG--PVSAVAAELRELETAMSD 108
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN-GRTLFDSRKGIFLPPEKRRIGYVFQEARlfPHLSVRGNLRYGMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 109 PDRMDEMDAIVErygevqaryeeldgyalegrarevLAGLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:TIGR02142 106 SERRISFERVIE------------------------LLGIG---HLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505055604 189 SNHLDL----ESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALT 237
Cdd:TIGR02142 159 LAALDDprkyEILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVA 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-219 |
1.40e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 66.74 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPD---EGQVavekgmtigYFDqdvgema 77
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEV---------LLN------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRSavaevmegagpVSAVAAELRELETAMSDPDRMDEMD-------AIVERYG--EVQARYEEldgyALEGrarevlAGL 148
Cdd:COG4136 65 GRR-----------LTALPAEQRRIGILFQDDLLFPHLSvgenlafALPPTIGraQRRARVEQ----ALEE------AGL 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 149 SfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENF----LKGYDGALLMTSHDRE 219
Cdd:COG4136 124 A---GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFREFvfeqIRQRGIPALLVTHDEE 195
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
335-512 |
1.50e-12 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 66.61 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGA---SVKLGYFAQHSM-----DLLDGESTI 406
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGtplAEQRDEPHENILylghlPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 ---LQWLEERFPKAGQAPLRALA--GCFGFSgddvEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML 481
Cdd:TIGR01189 91 lenLHFWAAIHGGAQRTIEDALAavGLTGFE----DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180 190
....*....|....*....|....*....|....
gi 505055604 482 IKALSAY---QGTMLFVSHDRRFLSALsnRVLEL 512
Cdd:TIGR01189 167 AGLLRAHlarGGIVLLTTHQDLGLVEA--RELRL 198
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-193 |
2.00e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 68.56 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtIGyfDQDVGEMAGR 79
Cdd:COG3839 3 SLELENVSKSyGGVEALK-DIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEIL------IG--GRDVTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 S----------A------VAEVMegagpvsAVAAELReletamsdpdRMDEmDAIVERYGEVqARYEELDGYaLEGRARE 143
Cdd:COG3839 74 DrniamvfqsyAlyphmtVYENI-------AFPLKLR----------KVPK-AEIDRRVREA-AELLGLEDL-LDRKPKQ 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 144 vlaglsfsqemmdgdvakLSGGWKMRVALARILLMRPDAMLLDEP-SNhLD 193
Cdd:COG3839 134 ------------------LSGGQRQRVALGRALVREPKVFLLDEPlSN-LD 165
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
327-502 |
2.17e-12 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 66.01 E-value: 2.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGttNPD----KGSVslgasvklgyfaqhsmdLLDG 402
Cdd:cd03217 3 IKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKyevtEGEI-----------------LFKG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 ESTILQWLEERFpKAG-----QAPLRalagcfgFSGDDVEKRCRVL----SGGEKARLVMAAMLFDPPNFLVLDEPTNHL 473
Cdd:cd03217 64 EDITDLPPEERA-RLGiflafQYPPE-------IPGVKNADFLRYVnegfSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 474 DLDTKEMLIKALSAYQG---TMLFVSHDRRFL 502
Cdd:cd03217 136 DIDALRLVAEVINKLREegkSVLIITHYQRLL 167
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
335-514 |
2.46e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 66.05 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL--GASVKLGYFAQ-----HSmDLLDGESTIL 407
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLdgGDIDDPDVAEAchylgHR-NAMKPALTVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 408 QWLE--ERFpkAGQAPLRALAG--CFGFSgdDVEKR-CRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLI 482
Cdd:PRK13539 92 ENLEfwAAF--LGGEELDIAAAleAVGLA--PLAHLpFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFA 167
|
170 180 190
....*....|....*....|....*....|....
gi 505055604 483 KALSAY--QGTMLFVShDRRFLSALSNRVLELTP 514
Cdd:PRK13539 168 ELIRAHlaQGGIVIAA-THIPLGLPGARELDLGP 200
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
332-510 |
2.48e-12 |
|
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: 67.05 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 332 KTYGSRTI-YDGLDFmvRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLgASVKLGYFAQHSMdlLDGESTILQWL 410
Cdd:cd03237 8 KTLGEFTLeVEGGSI--SESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQYIK--ADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 411 EERFPKAGQAPlralagcfgFSGDDV----------EKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEM 480
Cdd:cd03237 83 SSITKDFYTHP---------YFKTEIakplqieqilDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLM 153
|
170 180 190
....*....|....*....|....*....|....
gi 505055604 481 LIKALSAY----QGTMLFVSHDRRFLSALSNRVL 510
Cdd:cd03237 154 ASKVIRRFaennEKTAFVVEHDIIMIDYLADRLI 187
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-60 |
2.52e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 66.64 E-value: 2.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS------------------NSHRILYIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQV 58
Cdd:COG1134 4 MIEVENVSKSyrlyhepsrslkelllrrRRTRREEFWAlkdvSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
..
gi 505055604 59 AV 60
Cdd:COG1134 84 EV 85
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
339-512 |
2.64e-12 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.03 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 339 IYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKLGYFAQHSMDL--LDGESTILQWLEE--- 412
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIdGKTATRGDRSRFMAYLghLPGLKADLSTLENlhf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 413 ------RFPKagQAPLRALAgCFGFSGDDvEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALS 486
Cdd:PRK13543 106 lcglhgRRAK--QMPGSALA-IVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIS 181
|
170 180
....*....|....*....|....*....
gi 505055604 487 AY---QGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:PRK13543 182 AHlrgGGAALVTTHGAYAAPPVRTRMLTL 210
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-193 |
2.68e-12 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 67.07 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSnshrilYIEASA-ALN-------RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMtigyfdqdv 73
Cdd:TIGR04520 1 IEVENVSFS------YPESEKpALKnvslsieKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVD-GL--------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 74 gEMAGRSAVAEVMEGAGPV------SAVAAELRE-----LETAMSDPDrmdEMDAIVERygevqaryeeldgyALEgrar 142
Cdd:TIGR04520 65 -DTLDEENLWEIRKKVGMVfqnpdnQFVGATVEDdvafgLENLGVPRE---EMRKRVDE--------------ALK---- 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 143 evLAGLsfsQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:TIGR04520 123 --LVGM---EDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLD 168
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
327-474 |
3.14e-12 |
|
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: 66.44 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGS-RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV-------------KLGY 391
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdGTDInklkgkalrqlrrQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 FAQH-----SMDLLD-------GESTILQWLEERFPKAG-QAPLRALAGcFGFSgDDVEKRCRVLSGGEKARLVMAAMLF 458
Cdd:cd03256 83 IFQQfnlieRLSVLEnvlsgrlGRRSTWRSLFGLFPKEEkQRALAALER-VGLL-DKAYQRADQLSGGQQQRVAIARALM 160
|
170
....*....|....*.
gi 505055604 459 DPPNFLVLDEPTNHLD 474
Cdd:cd03256 161 QQPKLILADEPVASLD 176
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
21-189 |
3.41e-12 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 65.92 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVGEMAG----RSAVAEVMEGagpvsava 96
Cdd:cd03224 20 SLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIR--------FDGRDITGLPPheraRAGIGYVPEG-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 97 aelRELETAMSDPDRMdEMDAIVERYGEVQARYEELdgYAL-----EGRARevLAGLsfsqemmdgdvakLSGGWKMRVA 171
Cdd:cd03224 84 ---RRIFPELTVEENL-LLGAYARRRAKRKARLERV--YELfprlkERRKQ--LAGT-------------LSGGEQQMLA 142
|
170
....*....|....*...
gi 505055604 172 LARILLMRPDAMLLDEPS 189
Cdd:cd03224 143 IARALMSRPKLLLLDEPS 160
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
325-476 |
3.58e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 68.33 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG-----------ASVKLGYFA 393
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvealsaraASRRVASVP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 394 QHSMdlLDGESTILQWLE-------ERFPKAGQAPLRAL------AGCFGFSGDDVEKrcrvLSGGEKARLVMAAMLFDP 460
Cdd:PRK09536 84 QDTS--LSFEFDVRQVVEmgrtphrSRFDTWTETDRAAVeramerTGVAQFADRPVTS----LSGGERQRVLLARALAQA 157
|
170
....*....|....*.
gi 505055604 461 PNFLVLDEPTNHLDLD 476
Cdd:PRK09536 158 TPVLLLDEPTASLDIN 173
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
324-513 |
3.89e-12 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.05 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTY-GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgYFAQHSMDLLDG 402
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI---------WFSGHDITRLKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 EST---------ILQ---WLEERFPKAGQAPLRALAGCfgfSGDDVEKRCRV-----------------LSGGEKARLVM 453
Cdd:PRK10908 72 REVpflrrqigmIFQdhhLLMDRTVYDNVAIPLIIAGA---SGDDIRRRVSAaldkvglldkaknfpiqLSGGEQQRVGI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 454 AAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG---TMLFVSHDRRFLSALSNRVLELT 513
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvgvTVLMATHDIGLISRRSYRMLTLS 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
337-506 |
4.24e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 65.75 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 337 RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTG--TTNPDKGSVSLGAsvklgyfaqhsmDLLDGESTILqwleERF 414
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPD------------NQFGREASLI----DAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 415 PKAGQAP--LRALAGCfGFSgdDV---EKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDT----KEMLIKAL 485
Cdd:COG2401 107 GRKGDFKdaVELLNAV-GLS--DAvlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTakrvARNLQKLA 183
|
170 180
....*....|....*....|.
gi 505055604 486 SAYQGTMLFVSHDRRFLSALS 506
Cdd:COG2401 184 RRAGITLVVATHHYDVIDDLQ 204
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-193 |
4.91e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 66.67 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV------------------E 61
Cdd:COG4152 1 MLELKGLTKRfGDKTAVD-DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWdgepldpedrrrigylpeE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 62 KG----MTIG----YFdqdvgemagrsavaevmegagpvsavaAELReletAMSDPDRMDEMDAIVERYGevqaryeeld 133
Cdd:COG4152 80 RGlypkMKVGeqlvYL---------------------------ARLK----GLSKAEAKRRADEWLERLG---------- 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 134 gyaLEGRArevlaglsfsqemmDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG4152 119 ---LGDRA--------------NKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-233 |
5.05e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 67.66 E-value: 5.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDvgemagrs 80
Cdd:PRK09452 15 VELRGISKSfDGKEVIS-NLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLD--------GQD-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 avaevmegagpVSAVAAELRELETA---------MSDPD------RMDEMDAiveryGEVQARYEEldgyALegraREV- 144
Cdd:PRK09452 78 -----------ITHVPAENRHVNTVfqsyalfphMTVFEnvafglRMQKTPA-----AEITPRVME----AL----RMVq 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 145 LaglsfsQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMT----SHDRE- 219
Cdd:PRK09452 134 L------EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITfvfvTHDQEe 207
|
250 260
....*....|....*....|
gi 505055604 220 ---FMNRIV---TKIIEIDG 233
Cdd:PRK09452 208 altMSDRIVvmrDGRIEQDG 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-240 |
6.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.65 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmTIGYFDQDVGEM 76
Cdd:PRK13651 3 IKVKNIVKIfNKKLPTELKAldnvSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI------EWIFKDEKNKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 AGRSAVaevmegagpvsavaaELRELETAMSDPDRMDEMDAIVERYGEV-Q-ARYE------ELD------------GYA 136
Cdd:PRK13651 77 TKEKEK---------------VLEKLVIQKTRFKKIKKIKEIRRRVGVVfQfAEYQlfeqtiEKDiifgpvsmgvskEEA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 137 LEgRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLI-WLENFLKGYDGA--LLM 213
Cdd:PRK13651 142 KK-RAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKeILEIFDNLNKQGktIIL 220
|
250 260 270
....*....|....*....|....*....|....*
gi 505055604 214 TSHD----REFMNRIVT----KIIEiDGGaltTYS 240
Cdd:PRK13651 221 VTHDldnvLEWTKRTIFfkdgKIIK-DGD---TYD 251
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
315-497 |
6.36e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.88 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 315 LPAPRSGEDVVnLKSVHKTY-GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG----ASVKL 389
Cdd:COG1132 331 VPLPPVRGEIE-FENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdiRDLTL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 390 -------GYFAQHSMdLLDGesTILQWLeeRF--PKAGQAPLRA---LAGCFGF-----SGDD--VEKRCRVLSGGEKAR 450
Cdd:COG1132 410 eslrrqiGVVPQDTF-LFSG--TIRENI--RYgrPDATDEEVEEaakAAQAHEFiealpDGYDtvVGERGVNLSGGQRQR 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 451 LVMA-AMLFDPPnFLVLDEPTNHLDLDTKEMLIKALSAY-QG-TMLFVSH 497
Cdd:COG1132 485 IAIArALLKDPP-ILILDEATSALDTETEALIQEALERLmKGrTTIVIAH 533
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
325-474 |
6.82e-12 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 64.91 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDF-----MvrrrerWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVK---------L 389
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLtlgpgM------YGLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLkqpqklrrrI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 390 GYFAQH--------SMDLLDgestILQWLEE----RFPKAGQAPLRALAgcfgfSGDDVEKRCRVLSGGEKARLVMAAML 457
Cdd:cd03264 75 GYLPQEfgvypnftVREFLD----YIAWLKGipskEVKARVDEVLELVN-----LGDRAKKKIGSLSGGMRRRVGIAQAL 145
|
170
....*....|....*..
gi 505055604 458 FDPPNFLVLDEPTNHLD 474
Cdd:cd03264 146 VGDPSILIVDEPTAGLD 162
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
327-514 |
7.17e-12 |
|
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: 65.15 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTY-----GSRTI--YDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLgasvklgyfaQHSMDL 399
Cdd:COG4778 7 VENLSKTFtlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV----------RHDGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 400 LD----GESTIL-----------QWLEERfPKAG-----QAPLRALagcfGFSGDDVEKRCRVL---------------- 443
Cdd:COG4778 77 VDlaqaSPREILalrrrtigyvsQFLRVI-PRVSaldvvAEPLLER----GVDREEARARARELlarlnlperlwdlppa 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 444 --SGGEKARLVMA-AMLFDPPnFLVLDEPTNHLDLDTKEM---LIKALSAyQGT-MLFVSHDRRFLSALSNRVLELTP 514
Cdd:COG4778 152 tfSGGEQQRVNIArGFIADPP-LLLLDEPTASLDAANRAVvveLIEEAKA-RGTaIIGIFHDEEVREAVADRVVDVTP 227
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-193 |
8.00e-12 |
|
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: 65.40 E-value: 8.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSnshrilYIEASAALN-------RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQV-----------AVEKG 63
Cdd:cd03295 1 IEFENVTKR------YGGGKKAVNnlnleiaKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgedireqdPVELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 64 MTIGYFDQDVGEMAGRSavaeVMEGAGPVSAVAAELREletamsdpdrmdemdaiverygevqaRYEEldgyalegRARE 143
Cdd:cd03295 75 RKIGYVIQQIGLFPHMT----VEENIALVPKLLKWPKE--------------------------KIRE--------RADE 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 144 VLAGLSF-SQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:cd03295 117 LLALVGLdPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
26-239 |
9.88e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.59 E-value: 9.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfdqdvGEMAGRSAVAEVMEGAGPVsavaaelreleta 105
Cdd:PRK13652 29 RNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIR------------GEPITKENIREVRKFVGLV------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 106 MSDPDrmDEM-DAIVER---YGEVQAryeELDGYALEGRAREVLAGLSFSqEMMDGDVAKLSGGWKMRVALARILLMRPD 181
Cdd:PRK13652 84 FQNPD--DQIfSPTVEQdiaFGPINL---GLDEETVAHRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 182 AMLLDEPSNHLDLES----LIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTY 239
Cdd:PRK13652 158 VLVLDEPTAGLDPQGvkelIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAY 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
325-527 |
1.02e-11 |
|
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: 64.95 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLDGES 404
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEI-----------------LLDGKD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 ------------TILQ----------WLEERFP----KAGQAPLRA-------LAGCFGFSGDDVEKrcrvLSGGEKARL 451
Cdd:cd03300 64 itnlpphkrpvnTVFQnyalfphltvFENIAFGlrlkKLPKAEIKErvaealdLVQLEGYANRKPSQ----LSGGQQQRV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 452 VMAAMLFDPPNFLVLDEPTNHLDLD-TKEMLI--KALSAYQG-TMLFVSHDRRFLSALSNRVLELTPDGINQYGGGYSEY 527
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKlRKDMQLelKRLQKELGiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIY 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-510 |
1.20e-11 |
|
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: 67.12 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE----------KGMTIG-YFdqdvgemagrsavAEVMEGagpvsa 94
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEpswdevlkrfRGTELQdYF-------------KKLANG------ 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 95 vaaelrELETAMSdPDRMDemdAIVERY-GEVQaryEELDGYALEGRAREVLAGLSFSqEMMDGDVAKLSGGWKMRVALA 173
Cdd:COG1245 159 ------EIKVAHK-PQYVD---LIPKVFkGTVR---ELLEKVDERGKLDELAEKLGLE-NILDRDISELSGGELQRVAIA 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 174 RILLMRPDAMLLDEPSNHLDLE------SLIwleNFLKGYDGALLMTSHDREFMNrIVTKIIEIdggaltTY--SGDYGf 245
Cdd:COG1245 225 AALLRDADFYFFDEPSSYLDIYqrlnvaRLI---RELAEEGKYVLVVEHDLAILD-YLADYVHI------LYgePGVYG- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 246 ydeqralnarqqqaqferqqamlakeikfierfkaRASHASQVqsRVKKLEKID---RVEPPR-RRQTVAFEFLPAPR-- 319
Cdd:COG1245 294 -----------------------------------VVSKPKSV--RVGINQYLDgylPEENVRiRDEPIEFEVHAPRRek 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 320 SGEDVVNLKSVHKTYGsrtiydglDF-------MVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGasVKLGYF 392
Cdd:COG1245 337 EEETLVEYPDLTKSYG--------GFsleveggEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--LKISYK 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 393 AQH--------SMDLLDGEST-ILQ--WLEERFPKagqaPL---RALagcfgfsgddvEKRCRVLSGGEKARLVMAAMLF 458
Cdd:COG1245 407 PQYispdydgtVEEFLRSANTdDFGssYYKTEIIK----PLgleKLL-----------DKNVKDLSGGELQRVAIAACLS 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 459 DPPNFLVLDEPTNHLDLDTKEMLIKALSAY----QGTMLFVSHDRRFLSALSNRVL 510
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQRLAVAKAIRRFaenrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
26-234 |
1.35e-11 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 64.05 E-value: 1.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmTIGYFDQDVGEMAGRsavaevmegagPVSAVAAElRELETA 105
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRV------LINGVDVTAAPPADR-----------PVSMLFQE-NNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 106 MSDPDRMDEmdAIVERYgevqaRYEELDGYALEGRAREVlaGLsfsQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLL 185
Cdd:cd03298 85 LTVEQNVGL--GLSPGL-----KLTAEDRQAIEVALARV--GL---AGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505055604 186 DEPSNHLD---LESLIWLENFLKGYDG-ALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:cd03298 153 DEPFAALDpalRAEMLDLVLDLHAETKmTVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-228 |
1.51e-11 |
|
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: 64.06 E-value: 1.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYI--EASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEK----------GMTIGY- 68
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirtdrkaaRQSLGYc 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 69 --FDQDVGEMAGRsavaEVMEgagpvsaVAAELRELETamsdpdrmDEMDAIVERYgevqARYEELDGYALEgRAREvla 146
Cdd:cd03263 81 pqFDALFDELTVR----EHLR-------FYARLKGLPK--------SEIKEEVELL----LRVLGLTDKANK-RART--- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 147 glsfsqemmdgdvakLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES--LIWleNFLKGYDG--ALLMTSHDREFMN 222
Cdd:cd03263 134 ---------------LSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASrrAIW--DLILEVRKgrSIILTTHSMDEAE 196
|
....*.
gi 505055604 223 RIVTKI 228
Cdd:cd03263 197 ALCDRI 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-193 |
2.18e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 63.43 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV-EKGMT-IGYFDQDVGeMAGR 79
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIgGRDVTdLPPKDRDIA-MVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 S-------AVAEVMegagpvsAVAAELREletamSDPDRMDEmdaiverygevqaryeeldgyalegRAREVLAGLSFSq 152
Cdd:cd03301 80 NyalyphmTVYDNI-------AFGLKLRK-----VPKDEIDE-------------------------RVREVAELLQIE- 121
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505055604 153 EMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:cd03301 122 HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLD 162
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-236 |
2.26e-11 |
|
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: 62.62 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENIS---KSNSHRILyIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV-----------EKGMTIG 67
Cdd:cd03246 1 LEVENVSfryPGAEPPVL-RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLdgadisqwdpnELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 68 YFDQDVgemagrsavaevmegagpvsavaaelreletamsdpdrmdemdaiverygevqaryeeldgyalegrarevlag 147
Cdd:cd03246 80 YLPQDD-------------------------------------------------------------------------- 85
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 148 lsfsqEMMDGDVAK--LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENF---LKGYDGALLMTSHDREFMN 222
Cdd:cd03246 86 -----ELFSGSIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAiaaLKAAGATRIVIAHRPETLA 160
|
250
....*....|....
gi 505055604 223 RiVTKIIEIDGGAL 236
Cdd:cd03246 161 S-ADRILVLEDGRV 173
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
332-469 |
3.01e-11 |
|
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: 63.45 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 332 KTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG------------ASVKLGYFAQHS--- 396
Cdd:TIGR04406 9 KSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgqdithlpmherARLGIGYLPQEAsif 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 397 --MDLLDGESTILQWLEERFPKAGQAPLRALAGCFGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEP 469
Cdd:TIGR04406 89 rkLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQIS-HLRDNKAMSLSGGERRRVEIARALATNPKFILLDEP 162
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-193 |
3.03e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.97 E-value: 3.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfdqdvGEMAGRS 80
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLD------------GGDIDDP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEGAGPVSAVAAELRELET-----AMSDPDRMDEMDAIvERYGevqaryeeLDGyalegrarevLAGLSFsqemm 155
Cdd:PRK13539 70 DVAEACHYLGHRNAMKPALTVAENlefwaAFLGGEELDIAAAL-EAVG--------LAP----------LAHLPF----- 125
|
170 180 190
....*....|....*....|....*....|....*...
gi 505055604 156 dgdvAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK13539 126 ----GYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-219 |
3.89e-11 |
|
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: 63.12 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEaSAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE-KGMT--------IGYFDQD 72
Cdd:cd03299 1 LKVENLSKDWKEFKLKNV-SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgKDITnlppekrdISYVPQN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 73 vgemagrsavaevmegagpvsavaaelRELETAMSdpdrmdemdaiVERYGEVQARYEELDGYALEGRAREVLAGLSFSq 152
Cdd:cd03299 80 ---------------------------YALFPHMT-----------VYKNIAYGLKKRKVDKKEIERKVLEIAEMLGID- 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 153 EMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL---ESLIWLENFL-KGYDGALLMTSHDRE 219
Cdd:cd03299 121 HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVrtkEKLREELKKIrKEFGVTVLHVTHDFE 191
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
335-510 |
4.31e-11 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 63.67 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL---------GASVK-----LGYFAQHSMDLL 400
Cdd:TIGR02769 22 QRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFrgqdlyqldRKQRRafrrdVQLVFQDSPSAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 401 DGESTILQWLEE------RFPKAGQ-APLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHL 473
Cdd:TIGR02769 102 NPRMTVRQIIGEplrhltSLDESEQkARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505055604 474 DLDTKEMLIKALSAYQ---GT-MLFVSHDRRFLSALSNRVL 510
Cdd:TIGR02769 182 DMVLQAVILELLRKLQqafGTaYLFITHDLRLVQSFCQRVA 222
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
24-193 |
4.32e-11 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 64.37 E-value: 4.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigYFD-QDVGEMAGRsavaevmegagpvsavaaELREL 102
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEI---------LFDgQDITGLSGR------------------ELRPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 103 ETAM----SDP-----DRMDEMDAIveryGEVQARYEELDGYALEGRAREVLA--GLSfsQEMMDGDVAKLSGGWKMRVA 171
Cdd:COG4608 94 RRRMqmvfQDPyaslnPRMTVGDII----AEPLRIHGLASKAERRERVAELLElvGLR--PEHADRYPHEFSGGQRQRIG 167
|
170 180
....*....|....*....|..
gi 505055604 172 LARILLMRPDAMLLDEPSNHLD 193
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALD 189
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-217 |
4.40e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.54 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 4 IENISKSNSHRI------LYIEAsaalnrGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigyfdqdvgeMA 77
Cdd:PRK11247 15 LNAVSKRYGERTvlnqldLHIPA------GQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-----------------LA 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRSAVAEVMEgagpvsavaaelrelETamsdpdRMDEMDAIVERYGEVqaryeeLD--GYALEG----RAREVLAGLSFS 151
Cdd:PRK11247 72 GTAPLAEARE---------------DT------RLMFQDARLLPWKKV------IDnvGLGLKGqwrdAALQALAAVGLA 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 152 QEMMDGDVAkLSGGWKMRVALARILLMRPDAMLLDEPSNHLD------LESLIwlENFLKGYDGALLMTSHD 217
Cdd:PRK11247 125 DRANEWPAA-LSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrieMQDLI--ESLWQQHGFTVLLVTHD 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-216 |
5.69e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.17 E-value: 5.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfdqdvGEMAGRSAVAEVMEGAGPVSAVAAELRELE 103
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQID------------GKTATRGDRSRFMAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 104 TamsdpdrMDEMDAIVERygevqaRYEELDGYALegrareVLAGLSFSQEMMdgdVAKLSGGWKMRVALARILLMRPDAM 183
Cdd:PRK13543 102 N-------LHFLCGLHGR------RAKQMPGSAL------AIVGLAGYEDTL---VRQLSAGQKKRLALARLWLSPAPLW 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 505055604 184 LLDEPSNHLDLESLIWLENFLKGY---DGALLMTSH 216
Cdd:PRK13543 160 LLDEPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
335-513 |
5.70e-11 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 62.13 E-value: 5.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL---GASVKLGYFAQ--HSMDLLDGESTILQW 409
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLnggPLDFQRDSIARglLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 410 LEE-RFpkagQAPLRALAGCF------GFSGddVEKR-CRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML 481
Cdd:cd03231 91 LENlRF----WHADHSDEQVEealarvGLNG--FEDRpVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180 190
....*....|....*....|....*....|....*
gi 505055604 482 IKALSAY---QGTMLFVSHDRRFLSALSNRVLELT 513
Cdd:cd03231 165 AEAMAGHcarGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
21-234 |
6.47e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 63.22 E-value: 6.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqdVGEMAGRSAVAEVMEGAGPVsavaaelr 100
Cdd:PRK13647 25 SLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKV------------MGREVNAENEKWVRSKVGLV-------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 eletaMSDPDrmDEM-DAIVERYGEVQARYEELDGYALEGRAREVLAGLSFsQEMMDGDVAKLSGGWKMRVALARILLMR 179
Cdd:PRK13647 85 -----FQDPD--DQVfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 180 PDAMLLDEPSNHLD---LESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGG 234
Cdd:PRK13647 157 PDVIVLDEPMAYLDprgQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
325-521 |
7.44e-11 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 61.89 E-value: 7.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG--------------ASVKLG 390
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdlppkdrdiAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 391 YFAQHSMDLLDgesTILQWLEER-FPKAG-QAPLRALAGCFGFSGdDVEKRCRVLSGGEKARLVMA-AMLFDPPNFLvLD 467
Cdd:cd03301 81 YALYPHMTVYD---NIAFGLKLRkVPKDEiDERVREVAELLQIEH-LLDRKPKQLSGGQRQRVALGrAIVREPKVFL-MD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 468 EPTNHLD----LDTKEMLIKALSAYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:cd03301 156 EPLSNLDaklrVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
341-513 |
7.76e-11 |
|
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: 62.10 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV------KLGYFAQHSMdlldgestiLQWLEER 413
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGKQItepgpdRMVVFQNYSL---------LPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 414 -------------FPKAGQAPLR----ALAGCfgfsGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLD 476
Cdd:TIGR01184 73 enialavdrvlpdLSKSERRAIVeehiALVGL----TEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505055604 477 TK----EMLIKALSAYQGTMLFVSHDRRFLSALSNRVLELT 513
Cdd:TIGR01184 149 TRgnlqEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLT 189
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
343-512 |
8.31e-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: 63.59 E-value: 8.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 343 LDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV---------------KLGYFAQ------------- 394
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQearlfphlsvrgn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 395 --HSMDLLDGESTILQWlEERFPKAGQAPLralagcfgfsgddVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNH 472
Cdd:TIGR02142 96 lrYGMKRARPSERRISF-ERVIELLGIGHL-------------LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505055604 473 LDLDTKEMLIKAL----SAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:TIGR02142 162 LDDPRKYEILPYLerlhAEFGIPILYVSHSLQEVLRLADRVVVL 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
21-189 |
8.65e-11 |
|
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: 61.92 E-value: 8.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDVGEMA----GRSAVAEVMEGAGpvsaVA 96
Cdd:COG0410 23 SLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR--------FDGEDITGLPphriARLGIGYVPEGRR----IF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 97 AEL--RE-LETAMSDPDRMDEMDAIVERygeVQARYEELdgyaleGRAREVLAGLsfsqemmdgdvakLSGGWKMRVALA 173
Cdd:COG0410 91 PSLtvEEnLLLGAYARRDRAEVRADLER---VYELFPRL------KERRRQRAGT-------------LSGGEQQMLAIG 148
|
170
....*....|....*.
gi 505055604 174 RILLMRPDAMLLDEPS 189
Cdd:COG0410 149 RALMSRPKLLLLDEPS 164
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-497 |
9.43e-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: 61.03 E-value: 9.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNP--DKGSVSL-GASVKL-------GYFAQHsmDLLDGES 404
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLInGRPLDKrsfrkiiGYVPQD--DILHPTL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 TILQWLEerfpkagqaplralagcfgFSGddvekRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKA 484
Cdd:cd03213 98 TVRETLM-------------------FAA-----KLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170
....*....|....*.
gi 505055604 485 LS--AYQG-TMLFVSH 497
Cdd:cd03213 154 LRrlADTGrTIICSIH 169
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-234 |
1.38e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 63.65 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmTIGyfDQDVGEMAgrsavaevmegagpvsavAAELR 100
Cdd:COG1132 360 SLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI------LID--GVDIRDLT------------------LESLR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 EletAMS----DPDRMDE--MDAIveRYGEVQARYEELDGYALEGRAREVLAGLSfsqemmDG---DV----AKLSGGWK 167
Cdd:COG1132 414 R---QIGvvpqDTFLFSGtiRENI--RYGRPDATDEEVEEAAKAAQAHEFIEALP------DGydtVVgergVNLSGGQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 168 MRVALARILLMRPDAMLLDEPSNHLDLES--LIW--LENFLKGYdgALLMTSHdrefmnRIVT-----KIIEIDGG 234
Cdd:COG1132 483 QRIAIARALLKDPPILILDEATSALDTETeaLIQeaLERLMKGR--TTIVIAH------RLSTirnadRILVLDDG 550
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
329-510 |
1.47e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.01 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 329 SVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVS-----LGASVKLGYFA---------Q 394
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgepLAKLNRAQRKAfrrdiqmvfQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 395 HSMDLLDGESTILQWLEE------RFPKAGQ-APLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLD 467
Cdd:PRK10419 97 DSISAVNPRKTVREIIREplrhllSLDKAERlARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505055604 468 EPTNHLDLDTKEMLIKALSAYQ---GT-MLFVSHDRRFLSALSNRVL 510
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQqqfGTaCLFITHDLRLVERFCQRVM 223
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
321-521 |
1.47e-10 |
|
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: 63.99 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 321 GEDVVNLKSVHKTYGSRTIYDgLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGAsvklgyfaqHSMDLL 400
Cdd:TIGR01193 472 GDIVINDVSYSYGYGSNILSD-ISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNG---------FSLKDI 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 401 DgeSTILQWLEERFPkagQAPlralagcFGFSG----------------DDVEKRCRV---------------------- 442
Cdd:TIGR01193 542 D--RHTLRQFINYLP---QEP-------YIFSGsilenlllgakenvsqDEIWAACEIaeikddienmplgyqtelseeg 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 443 --LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQ-GTMLFVSHdRRFLSALSNRVLELTPDGINQ 519
Cdd:TIGR01193 610 ssISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQdKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE 688
|
..
gi 505055604 520 YG 521
Cdd:TIGR01193 689 QG 690
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
325-510 |
1.57e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.64 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGS-----RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdL 399
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI-----------------L 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 400 LDGEStILQWLEER--------F--PKAGQAP-------LrALA----GCFGFS------------------GDDVEKR- 439
Cdd:COG1101 65 IDGKD-VTKLPEYKrakyigrvFqdPMMGTAPsmtieenL-ALAyrrgKRRGLRrgltkkrrelfrellatlGLGLENRl 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 440 -CRV--LSGGEkaR----LVMAAMlfDPPNFLVLDEPTNHLDLDTKEMLI----KALSAYQGTMLFVSHDRRFLSALSNR 508
Cdd:COG1101 143 dTKVglLSGGQ--RqalsLLMATL--TKPKLLLLDEHTAALDPKTAALVLelteKIVEENNLTTLMVTHNMEQALDYGNR 218
|
..
gi 505055604 509 VL 510
Cdd:COG1101 219 LI 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-193 |
1.63e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 62.51 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV---------EKGMT-- 65
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHAlnnvSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVdgqdltalsEKELRka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 66 ---IGYFDQDVGEMAGRSAVAEVmegagpvsAVAAELreletamsdpDRMDEmdaiveryGEVQARYEELdgyaLEgrar 142
Cdd:PRK11153 81 rrqIGMIFQHFNLLSSRTVFDNV--------ALPLEL----------AGTPK--------AEIKARVTEL----LE---- 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 143 evLAGLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK11153 127 --LVGLS---DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-193 |
1.75e-10 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 62.43 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 4 IENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQV------------------------A 59
Cdd:PRK11432 9 LKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIfidgedvthrsiqqrdicmvfqsyA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 60 VEKGMTIGyfdQDVG---EMAGRSAvaevmegagpvsavaAELREletamsdpdRMDEMDAIVErygevqaryeeLDGYA 136
Cdd:PRK11432 89 LFPHMSLG---ENVGyglKMLGVPK---------------EERKQ---------RVKEALELVD-----------LAGFE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 137 legrarevlaglsfsqemmDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK11432 131 -------------------DRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
325-512 |
1.88e-10 |
|
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: 60.88 E-value: 1.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTI-YDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV------KLGYFAQHs 396
Cdd:cd03292 1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVnGQDVsdlrgrAIPYLRRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 MDLLDGESTILqwleerfPKAGQAPLRALA-GCFGFSGDDVEKRCRV-----------------LSGGEKARLVMAAMLF 458
Cdd:cd03292 80 IGVVFQDFRLL-------PDRNVYENVAFAlEVTGVPPREIRKRVPAalelvglshkhralpaeLSGGEQQRVAIARAIV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 459 DPPNFLVLDEPTNHLDLDTKEM---LIKALSAYQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd03292 153 NSPTILIADEPTGNLDPDTTWEimnLLKKINKAGTTVVVATHAKELVDTTRHRVIAL 209
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-234 |
2.20e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.03 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-----------NSHRIL------YIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVA 59
Cdd:COG4586 1 IIEVENLSKTyrvyekepglkGALKGLfrreyrEVEAvddiSFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 60 VekgmtigyfdqdvgemAGRSAVAEVMEGAGPVSAV------------AAELRELETAMSD-PDRmdemdaiverygEVQ 126
Cdd:COG4586 81 V----------------LGYVPFKRRKEFARRIGVVfgqrsqlwwdlpAIDSFRLLKAIYRiPDA------------EYK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 127 ARYEELDgyalegrarEVLaGLSfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKG 206
Cdd:COG4586 133 KRLDELV---------ELL-DLG---ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKE 199
|
250 260 270
....*....|....*....|....*....|....*
gi 505055604 207 Y---DGA-LLMTSHDrefMN---RIVTKIIEIDGG 234
Cdd:COG4586 200 YnreRGTtILLTSHD---MDdieALCDRVIVIDHG 231
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
325-521 |
2.26e-10 |
|
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: 60.82 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG---ASVK------LGYFAQH 395
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgedATDVpvqernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 -----SMDLLDGESTIL--QWLEERFPKAG-QAPLRALAGCFGFSGddVEKRC-RVLSGGEKARLVMAAMLFDPPNFLVL 466
Cdd:cd03296 83 yalfrHMTVFDNVAFGLrvKPRSERPPEAEiRAKVHELLKLVQLDW--LADRYpAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 467 DEPTNHLDLDTKEMLIKALSAYQG----TMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
31-188 |
2.31e-10 |
|
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: 62.43 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 31 GLVGPNGAGKTTLFRMITGQELPDEGQVAV--------EKGMT-------IGYFDQDvgemagrsavaevmegagpvsav 95
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsARGIFlpphrrrIGYVFQE----------------------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 96 aAEL-------RELETAMSD---PDRMDEMDAIVERYGevqaryeeldgyalegrarevLAGLsfsqemMDGDVAKLSGG 165
Cdd:COG4148 86 -ARLfphlsvrGNLLYGRKRaprAERRISFDEVVELLG---------------------IGHL------LDRRPATLSGG 137
|
170 180
....*....|....*....|...
gi 505055604 166 WKMRVALARILLMRPDAMLLDEP 188
Cdd:COG4148 138 ERQRVAIGRALLSSPRLLLMDEP 160
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-193 |
2.68e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 61.18 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENIS---KSNSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGyfDQDVGEMag 78
Cdd:PRK13635 6 IRVEHISfryPDAATYALK-DVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG-GMVLS--EETVWDV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 RSAVAEVMEGagPVSA-VAAELRElETAMSDPDRMDEMDAIVERygeVQAryeeldgyALEgrarevLAGLsfsQEMMDG 157
Cdd:PRK13635 80 RRQVGMVFQN--PDNQfVGATVQD-DVAFGLENIGVPREEMVER---VDQ--------ALR------QVGM---EDFLNR 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 505055604 158 DVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK13635 137 EPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
345-512 |
2.81e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 60.60 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 345 FMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSV--------SLGASVK-------LGYFAQH-------------S 396
Cdd:PRK11629 30 FSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqpmsKLSSAAKaelrnqkLGFIYQFhhllpdftalenvA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 MDLLDGESTilqwleerfPKAGQAPLRALAGCFGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDL- 475
Cdd:PRK11629 110 MPLLIGKKK---------PAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDAr 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505055604 476 --DTKEMLIKALSAYQGT-MLFVSHDRRFLSALSnRVLEL 512
Cdd:PRK11629 180 naDSIFQLLGELNRLQGTaFLVVTHDLQLAKRMS-RQLEM 218
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
317-521 |
3.09e-10 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 61.89 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 317 APRSGEDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHS 396
Cdd:PRK09452 7 QPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 --------------MDLLDGESTILQWleERFPKAGQAP----------LRALAgcfgfsgddvEKRCRVLSGGEKARLV 452
Cdd:PRK09452 87 hvntvfqsyalfphMTVFENVAFGLRM--QKTPAAEITPrvmealrmvqLEEFA----------QRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 453 MAAMLFDPPNFLVLDEPTNHLDLD-TKEML--IKALSAYQG-TMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKlRKQMQneLKALQRKLGiTFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
325-499 |
3.23e-10 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 61.65 E-value: 3.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG----ASVK-----LGYFAQ- 394
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrdvTGLPpekrnVGMVFQd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 395 -----HsMDLLD----GestilqwLEER-FPKAGQAPL--RALA--GCFGFSgddvEKRCRVLSGGEKARLVMA-AMLFD 459
Cdd:COG3842 86 yalfpH-LTVAEnvafG-------LRMRgVPKAEIRARvaELLElvGLEGLA----DRYPHQLSGGQQQRVALArALAPE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505055604 460 PPnFLVLDEPTNHLDLDTKEMLIKALSAYQ----GTMLFVSHDR 499
Cdd:COG3842 154 PR-VLLLDEPLSALDAKLREEMREELRRLQrelgITFIYVTHDQ 196
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-194 |
3.29e-10 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 60.48 E-value: 3.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGR 79
Cdd:COG4604 1 MIEIKNVSKRyGGKVVLD-DVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD--------GLDVATTPSR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 sAVAEVMEGAGPVSAVAAEL--REL---------ETAMSDPDRmdemdAIVERY------GEVQARYeeLDgyalegrar 142
Cdd:COG4604 72 -ELAKRLAILRQENHINSRLtvRELvafgrfpysKGRLTAEDR-----EIIDEAiayldlEDLADRY--LD--------- 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505055604 143 evlaglsfsqemmdgdvaKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL 194
Cdd:COG4604 135 ------------------ELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
342-498 |
4.08e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 60.24 E-value: 4.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 342 GLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTnPDKGSVSLG-----------ASVKLGYFAQHSMDLLDgeSTILQWL 410
Cdd:COG4138 14 PISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNgrplsdwsaaeLARHRAYLSQQQSPPFA--MPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 411 EERFPKAGQAP-----LRALAGCFGFSgDDVEKRCRVLSGGEKARLVMAAMLF------DP-PNFLVLDEPTNHLD---- 474
Cdd:COG4138 91 ALHQPAGASSEaveqlLAQLAEALGLE-DKLSRPLTQLSGGEWQRVRLAAVLLqvwptiNPeGQLLLLDEPMNSLDvaqq 169
|
170 180
....*....|....*....|....*.
gi 505055604 475 --LDTkemLIKALSAYQGTMLFVSHD 498
Cdd:COG4138 170 aaLDR---LLRELCQQGITVVMSSHD 192
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-234 |
4.51e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.83 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKsnshriLYIE----ASAALNR-------GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGyfD 70
Cdd:PRK13637 3 IKIENLTH------IYMEgtpfEKKALDNvnieiedGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIID-GVDIT--D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 71 QDVGEMAGRSAVAEVMEGAgpvsavAAELRElETAMSD----PDRMDEMDaiveryGEVQARYEEldgyALEgrarevLA 146
Cdd:PRK13637 74 KKVKLSDIRKKVGLVFQYP------EYQLFE-ETIEKDiafgPINLGLSE------EEIENRVKR----AMN------IV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 147 GLSFsQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL----ESLIWLENFLKGYDGALLMTSHDREFMN 222
Cdd:PRK13637 131 GLDY-EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPkgrdEILNKIKELHKEYNMTIILVSHSMEDVA 209
|
250
....*....|..
gi 505055604 223 RIVTKIIEIDGG 234
Cdd:PRK13637 210 KLADRIIVMNKG 221
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
327-502 |
5.20e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 60.08 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGttNPD----KGSVslgasvklgyfaqhsmdLLDG 402
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG--HPKyevtSGSI-----------------LLDG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 EStILQWL-EERFpKAG-----QAP-----------LRALAGCFG---FSGDDVEKRCRV-------------------L 443
Cdd:COG0396 64 ED-ILELSpDERA-RAGiflafQYPveipgvsvsnfLRTALNARRgeeLSAREFLKLLKEkmkelgldedfldryvnegF 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 444 SGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG---TMLFVSHDRRFL 502
Cdd:COG0396 142 SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpdrGILIITHYQRIL 203
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
343-498 |
5.20e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.95 E-value: 5.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 343 LDFMVRRRERWCIMGINGAGKSTLLKLVTGTTnPDKGSVSLGAS-------VKL----GYFAQHS-----MDlldgestI 406
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQpleawsaAELarhrAYLSQQQtppfaMP-------V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 LQWLEERFP-----KAGQAPLRALAGCFGFsGDDVEKRCRVLSGGEKARLVMAAMLF--DP---PN--FLVLDEPTNHLD 474
Cdd:PRK03695 87 FQYLTLHQPdktrtEAVASALNEVAEALGL-DDKLGRSVNQLSGGEWQRVRLAAVVLqvWPdinPAgqLLLLDEPMNSLD 165
|
170 180 190
....*....|....*....|....*....|
gi 505055604 475 ------LDTkemLIKALSAYQGTMLFVSHD 498
Cdd:PRK03695 166 vaqqaaLDR---LLSELCQQGIAVVMSSHD 192
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-250 |
5.36e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFR----MITGQELPdEGQVAVekgmtIGYFDQDVGE 75
Cdd:PRK09984 4 IIRVEKLAKTfNQHQALH-AVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSA-GSHIEL-----LGRTVQREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 76 MAG-----RSAVAEVMEGAGPVSAVAAELRELETAM-SDPdrmdEMDAIVERYGEVQARYeeldgyALEGRAREVLAGLS 149
Cdd:PRK09984 77 LARdirksRANTGYIFQQFNLVNRLSVLENVLIGALgSTP----FWRTCFSWFTREQKQR------ALQALTRVGMVHFA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 150 FSQemmdgdVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESL-IWLENF--LKGYDG-ALLMTSHDREFMNRIV 225
Cdd:PRK09984 147 HQR------VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESArIVMDTLrdINQNDGiTVVVTLHQVDYALRYC 220
|
250 260
....*....|....*....|....*
gi 505055604 226 TKIIEIDGGALtTYSGDYGFYDEQR 250
Cdd:PRK09984 221 ERIVALRQGHV-FYDGSSQQFDNER 244
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
21-236 |
5.38e-10 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 59.98 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV---------EKGMTIGYFDQDVGEMAgRSAVAEVMEGAGP 91
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVngqtinlvrDKDGQLKVADKNQLRLL-RTRLTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 92 VSAVAAelreLETAMSDPdrmdemdaiVERYGEVQARYEEldgyalegRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVA 171
Cdd:PRK10619 104 WSHMTV----LENVMEAP---------IQVLGLSKQEARE--------RAVKYLAKVGIDERAQGKYPVHLSGGQQQRVS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 172 LARILLMRPDAMLLDEPSNHLDLE---SLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
343-512 |
5.65e-10 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 59.43 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 343 LDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKLGYFAQHSMDLLDGESTILQWLEE--------- 412
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLInGVDVTAAPPADRPVSMLFQENNLFAHLTVeqnvglgls 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 413 ---RFPKAGQAPLRALAGCFGFSGDDvEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK-EM--LIKALS 486
Cdd:cd03298 97 pglKLTAEDRQAIEVALARVGLAGLE-KRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRaEMldLVLDLH 175
|
170 180
....*....|....*....|....*..
gi 505055604 487 AYQG-TMLFVSHDRRFLSALSNRVLEL 512
Cdd:cd03298 176 AETKmTVLMVTHQPEDAKRLAQRVVFL 202
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
24-237 |
7.38e-10 |
|
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: 58.09 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigYFDQDvgemagrsavaevmegagPVSAVAAELRELE 103
Cdd:cd03247 25 LKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGV------------------PVSDLEKALSSLI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 104 TAMSdpdrmdemdaiverygevQARYeeldgyalegrarevlaglSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAM 183
Cdd:cd03247 78 SVLN------------------QRPY-------------------LFDTTLRNNLGRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 184 LLDEPSNHLD----LESLIWLENFLKgyDGALLMTSHDREFMNRiVTKIIEIDGGALT 237
Cdd:cd03247 121 LLDEPTVGLDpiteRQLLSLIFEVLK--DKTLIWITHHLTGIEH-MDKILFLENGKII 175
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
13-372 |
7.42e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 13 HRILYIEaSAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQ----------VAVEKgmtigyFDQDVGEMAGRSAV 82
Cdd:PRK10938 16 TKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrLSFEQ------LQKLVSDEWQRNNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 83 AEVMEGAGPVSAVAAELRELETamSDPDRMDEMDAiverygevQARYEELdgyaLEGRarevlaglsFSQemmdgdvakL 162
Cdd:PRK10938 89 DMLSPGEDDTGRTTAEIIQDEV--KDPARCEQLAQ--------QFGITAL----LDRR---------FKY---------L 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 163 SGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFL-----KGYDGALLMTSHDR--EFMNRIvtkiieidgGA 235
Cdd:PRK10938 137 STGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLaslhqSGITLVLVLNRFDEipDFVQFA---------GV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 236 LT----TYSGDYGfYDEQRALNArqqqaqferqqaMLAkeikfierfkarasHAsqvqsrvkklEKIDRVEPPRRRQTVA 311
Cdd:PRK10938 208 LAdctlAETGERE-EILQQALVA------------QLA--------------HS----------EQLEGVQLPEPDEPSA 250
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 312 FEFLPAprsGEDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTG 372
Cdd:PRK10938 251 RHALPA---NEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
24-217 |
8.36e-10 |
|
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: 59.02 E-value: 8.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPD------EGQVAVEKGMTIGYFDQDVGEMAGRSAVAEVmegAGPVSAVAA 97
Cdd:TIGR01184 8 IQQGEFISLIGHSGCGKSTLLNLISGLAQPTsggvilEGKQITEPGPDRMVVFQNYSLLPWLTVRENI---ALAVDRVLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 98 ELREletamsdpdrmDEMDAIVErygevqaryEELDgyalegrarevLAGLsfsQEMMDGDVAKLSGGWKMRVALARILL 177
Cdd:TIGR01184 85 DLSK-----------SERRAIVE---------EHIA-----------LVGL---TEAADKRPGQLSGGMKQRVAIARALS 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505055604 178 MRPDAMLLDEPSNHLDL---ESL------IWLENFLkgydgALLMTSHD 217
Cdd:TIGR01184 131 IRPKVLLLDEPFGALDAltrGNLqeelmqIWEEHRV-----TVLMVTHD 174
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
322-539 |
1.04e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 59.36 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTY--GSRTIyDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV-----------K 388
Cdd:PRK13647 2 DNIIEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREvnaenekwvrsK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 389 LGYFAQHSMDLLdGESTIlqWLEERFpkagqAPLRalagcFGFSGDDVEKRCRV-----------------LSGGEKARL 451
Cdd:PRK13647 81 VGLVFQDPDDQV-FSSTV--WDDVAF-----GPVN-----MGLDKDEVERRVEEalkavrmwdfrdkppyhLSYGQKKRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 452 VMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAY--QGTMLFVS-HDRRFLSALSNRVLELTpDGINQYGGGYSEYV 528
Cdd:PRK13647 148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhnQGKTVIVAtHDVDLAAEWADQVIVLK-EGRVLAEGDKSLLT 226
|
250
....*....|.
gi 505055604 529 ERTGQEAPGLR 539
Cdd:PRK13647 227 DEDIVEQAGLR 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
325-510 |
1.05e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 58.99 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG-----ASVKLGY-------- 391
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidTARSLSQqkglirql 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 -----FAQHSMDLLDGESTILQWLE-----ERFPKAGQAPL-RALAGCFGFSGDDvEKRCRVLSGGEKARLVMAAMLFDP 460
Cdd:PRK11264 84 rqhvgFVFQNFNLFPHRTVLENIIEgpvivKGEPKEEATARaRELLAKVGLAGKE-TSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505055604 461 PNFLVLDEPTNHLDLD-TKEML--IKALSAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:PRK11264 163 PEVILFDEPTSALDPElVGEVLntIRQLAQEKRTMVIVTHEMSFARDVADRAI 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
25-196 |
1.11e-09 |
|
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: 58.78 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 25 NRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtiGYFDQDVGEMAGRSAVAEVMEgagpvsavaaelrelET 104
Cdd:cd03251 26 PAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILID-----GHDVRDYTLASLRRQIGLVSQ---------------DV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 105 AMSDpdrmdemDAIVE--RYGEVQARYEELdgyalEGRAREVLAgLSFSQEMMDG-DV------AKLSGGWKMRVALARI 175
Cdd:cd03251 86 FLFN-------DTVAEniAYGRPGATREEV-----EEAARAANA-HEFIMELPEGyDTvigergVKLSGGQRQRIAIARA 152
|
170 180
....*....|....*....|.
gi 505055604 176 LLMRPDAMLLDEPSNHLDLES 196
Cdd:cd03251 153 LLKDPPILILDEATSALDTES 173
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-196 |
1.22e-09 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 60.59 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENIS-KSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGqeLPDEGQvavekgmtigyfdqdvGEMAgR 79
Cdd:COG4178 362 ALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG--LWPYGS----------------GRIA-R 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 SAVAEVM---------EGAgpvsavaaeLREletAMSDPDRMDEMDaiverygevqaryeeldgyalEGRAREVL--AGL 148
Cdd:COG4178 423 PAGARVLflpqrpylpLGT---------LRE---ALLYPATAEAFS---------------------DAELREALeaVGL 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 149 SFSQEMMDGDVA---KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES 196
Cdd:COG4178 470 GHLAERLDEEADwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
344-498 |
1.37e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 59.19 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 344 DFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGA---------------SVKLGYFAQH-----SMDLLD-- 401
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamsrkelrelrRKKISMVFQSfallpHRTVLEnv 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 402 -------GEStilqwLEERFPKAGQAplRALAGCFGFSgddvEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLD 474
Cdd:cd03294 124 afglevqGVP-----RAEREERAAEA--LELVGLEGWE----HKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180
....*....|....*....|....*...
gi 505055604 475 -LDTKEM---LIKALSAYQGTMLFVSHD 498
Cdd:cd03294 193 pLIRREMqdeLLRLQAELQKTIVFITHD 220
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
322-521 |
1.39e-09 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 58.83 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKLGYFAQHSMDLL 400
Cdd:PRK10619 3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVnGQTINLVRDKDGQLKVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 401 DGEStiLQWLEERFPKAGQ----------------APLRALagcfGFSGDDVEKRC-----RV-------------LSGG 446
Cdd:PRK10619 83 DKNQ--LRLLRTRLTMVFQhfnlwshmtvlenvmeAPIQVL----GLSKQEARERAvkylaKVgideraqgkypvhLSGG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 447 EKARLVMAAMLFDPPNFLVLDEPTNHLDLD-TKEML--IKALSAYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPElVGEVLriMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
322-497 |
1.40e-09 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.42 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKlgyFA--QHSMD 398
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEPVR---FRspRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 399 LldGESTILQ--------------WLeERFPKAG----------QApLRALAGcFGFSgDDVEKRCRVLSGGEK-----A 449
Cdd:COG1129 79 A--GIAIIHQelnlvpnlsvaeniFL-GREPRRGglidwramrrRA-RELLAR-LGLD-IDPDTPVGDLSVAQQqlveiA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505055604 450 RlvmaAMLFDpPNFLVLDEPTNHLDLDTKEML---IKALSAyQG-TMLFVSH 497
Cdd:COG1129 153 R----ALSRD-ARVLILDEPTASLTEREVERLfriIRRLKA-QGvAIIYISH 198
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-193 |
1.70e-09 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 58.81 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 5 ENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAgrsavae 84
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLID--------GQDIAAMS------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 85 vmegagpvsavAAELRELetamsdpdRMDEMDAIVERYG---------------EVQARYEEldgyALEGRAREVLA--G 147
Cdd:cd03294 93 -----------RKELREL--------RRKKISMVFQSFAllphrtvlenvafglEVQGVPRA----EREERAAEALElvG 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505055604 148 LS-FSQEMMDgdvaKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:cd03294 150 LEgWEHKYPD----ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-61 |
1.81e-09 |
|
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: 56.67 E-value: 1.81e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 2 IRIENISKS-NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE 61
Cdd:cd03216 1 LELRGITKRfGGVKALD-GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD 60
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
21-236 |
2.23e-09 |
|
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: 57.87 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVGemagRSAVAEVmeGAGPVsAVAAELR 100
Cdd:cd03248 34 SFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLD-GKPISQYEHKYL----HSKVSLV--GQEPV-LFARSLQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 eletamsdpdrmdemDAIVerYGEVQARYEELDGYALEGRARevlaglSFSQEMMDG---DV----AKLSGGWKMRVALA 173
Cdd:cd03248 106 ---------------DNIA--YGLQSCSFECVKEAAQKAHAH------SFISELASGydtEVgekgSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 174 RILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY--DGALLMTSHDREFMNRiVTKIIEIDGGAL 236
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
355-518 |
2.93e-09 |
|
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: 56.85 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLV----TGTTNPDK----------GSVSLGASVKLG--------YFAQHSMDLLD-------GESt 405
Cdd:cd03240 27 IVGQNGAGKTTIIEALkyalTGELPPNSkggahdpkliREGEVRAQVKLAfenangkkYTITRSLAILEnvifchqGES- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 406 ilQWLEERFPKAgqaplralagcfgfsgddvekrcrvLSGGEKA------RLVMAAMLFDPPNFLVLDEPTNHLDLDTKE 479
Cdd:cd03240 106 --NWPLLDMRGR-------------------------CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505055604 480 M-LIKALSAYQGTMLF----VSHDRRFLSALSNrVLELTPDGIN 518
Cdd:cd03240 159 EsLAEIIEERKSQKNFqlivITHDEELVDAADH-IYRVEKDGRQ 201
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
27-193 |
3.22e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.22 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyFDQDVGEMAGRSAVAEVMEGAGPVSAVAAELRELETAM 106
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRV--------DDTLITSTSKNKDIKQIRKKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 107 SD----PdrmdemdaivERYGEVQARYEELdgyalegrAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDA 182
Cdd:PRK13649 105 KDvafgP----------QNFGVSQEEAEAL--------AREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKI 166
|
170
....*....|.
gi 505055604 183 MLLDEPSNHLD 193
Cdd:PRK13649 167 LVLDEPTAGLD 177
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-234 |
3.55e-09 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 57.28 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHriLYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfdqdvGEMAGRS 80
Cdd:PRK10771 1 MLKLTDITWLYHH--LPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLN------------GQDHTTT 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEvmegaGPVSAVAAE---LRELETAMS-----------DPDRMDEMDAIVERYGevqaryeeldgyaLEgrarevla 146
Cdd:PRK10771 67 PPSR-----RPVSMLFQEnnlFSHLTVAQNiglglnpglklNAAQREKLHAIARQMG-------------IE-------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 147 glsfsqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD----LESLIWLENFLKGYDGALLMTSHDREFMN 222
Cdd:PRK10771 121 ------DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQLTLLMVSHSLEDAA 194
|
250
....*....|..
gi 505055604 223 RIVTKIIEIDGG 234
Cdd:PRK10771 195 RIAPRSLVVADG 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
341-510 |
3.88e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.17 E-value: 3.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLgasvkLGY--------FAQHsMDLLDGESTILQW--- 409
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV-----LGYvpfkrrkeFARR-IGVVFGQRSQLWWdlp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 410 LEERF----------PKAGQAPLRALAGCFGFsGDDVEKRCRVLSGGEKARL-VMAAMLFDPPnFLVLDEPTNHLDLDTK 478
Cdd:COG4586 113 AIDSFrllkaiyripDAEYKKRLDELVELLDL-GELLDTPVRQLSLGQRMRCeLAAALLHRPK-ILFLDEPTIGLDVVSK 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 505055604 479 EMLIKALSAY----QGTMLFVSHDRRFLSALSNRVL 510
Cdd:COG4586 191 EAIREFLKEYnrerGTTILLTSHDMDDIEALCDRVI 226
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-193 |
3.92e-09 |
|
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: 57.24 E-value: 3.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEM---A 77
Cdd:cd03253 1 IEFENVTFAyDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILID--------GQDIREVtldS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRSAVAEVMEgagpvsavaaelrelETAMSDPDRMDEMdaiveRYGEVQARYEELDGYALEGRAREVLAGLSFSQEMMDG 157
Cdd:cd03253 73 LRRAIGVVPQ---------------DTVLFNDTIGYNI-----RYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVG 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 505055604 158 DVA-KLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:cd03253 133 ERGlKLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
355-497 |
4.40e-09 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.35 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVklgyfaqhsmdLLDGESTIlqWL--EER-----FPKAGQAPLRALAG 427
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRV-----------LFDAEKGI--CLppEKRrigyvFQDARLFPHYKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 428 --CFGFSGDDVEKRCRV----------------LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQ 489
Cdd:PRK11144 96 nlRYGMAKSMVAQFDKIvallgieplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLA 175
|
170
....*....|..
gi 505055604 490 GT----MLFVSH 497
Cdd:PRK11144 176 REinipILYVSH 187
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-244 |
4.74e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.32 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 31 GLVGPNGAGKTTLFRMITGQELPDEGQVaVEKGMTIGYFDQdvGEMAGRSAVAEVMEgagpvsavaaelreletamsDPD 110
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAV-LWQGKPLDYSKR--GLLALRQQVATVFQ--------------------DPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 111 RmdemdaiverygevQARYEELD----------GYALEGRAREVLAGLSF--SQEMMDGDVAKLSGGWKMRVALARILLM 178
Cdd:PRK13638 88 Q--------------QIFYTDIDsdiafslrnlGVPEAEITRRVDEALTLvdAQHFRHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 179 RPDAMLLDEPSNHLD---LESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTYsGDYG 244
Cdd:PRK13638 154 QARYLLLDEPTAGLDpagRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTH-GAPG 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
333-498 |
4.88e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 56.34 E-value: 4.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 333 TYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPD---KGSVSL-GASV--------KLGYFAQhsMDLL 400
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLnGRRLtalpaeqrRIGILFQ--DDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 401 DGESTILQWLEERFPKAGQAPLR------AL--AGCFGFSGDDVEKrcrvLSGGEKARLVMAAMLFDPPNFLVLDEPTNH 472
Cdd:COG4136 88 FPHLSVGENLAFALPPTIGRAQRrarveqALeeAGLAGFADRDPAT----LSGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190
....*....|....*....|....*....|
gi 505055604 473 LD----LDTKEMLIKALSAYQGTMLFVSHD 498
Cdd:COG4136 164 LDaalrAQFREFVFEQIRQRGIPALLVTHD 193
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-188 |
4.94e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.47 E-value: 4.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigYFDQDVGEMAGRS 80
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI---------LFDGENIPAMSRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEV--------MEGA-----GPVSAVAAELRElETAMSDP----DRMDEMDAIverygevqaryeeldgyalegrare 143
Cdd:PRK11831 78 RLYTVrkrmsmlfQSGAlftdmNVFDNVAYPLRE-HTQLPAPllhsTVMMKLEAV------------------------- 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505055604 144 vlaGLSFSQEMMDgdvAKLSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:PRK11831 132 ---GLRGAAKLMP---SELSGGMARRAALARAIALEPDLIMFDEP 170
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
331-521 |
5.56e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 57.51 E-value: 5.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 331 HKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL------GASVK-----LGYFAQHSMDL 399
Cdd:PRK13652 11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrgepitKENIRevrkfVGLVFQNPDDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 400 ------------------LDgESTILQWLEERFPKAGQAPLRalagcfgfsgddvEKRCRVLSGGEKARLVMAAMLFDPP 461
Cdd:PRK13652 91 ifsptveqdiafgpinlgLD-EETVAHRVSSALHMLGLEELR-------------DRVPHHLSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 462 NFLVLDEPTNHLDLDTKEMLIKALSA----YQGTMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDlpetYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYG 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
24-230 |
5.62e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 58.68 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIgyfdQDVGEMAGRSAVAEVMEgagPVSAVAAELRElE 103
Cdd:PRK11160 363 IKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN-GQPI----ADYSEAALRQAISVVSQ---RVHLFSATLRD-N 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 104 TAMSDPDRMDE-MDAIVERYGevqaryeeLdGYALEGRArevlaGLSfsQEMMDGDvAKLSGGWKMRVALARILLMRPDA 182
Cdd:PRK11160 434 LLLAAPNASDEaLIEVLQQVG--------L-EKLLEDDK-----GLN--AWLGEGG-RQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 183 MLLDEPSNHLD--LESLIwLENFLK-GYDGALLMTSHdR----EFMNRIV----TKIIE 230
Cdd:PRK11160 497 LLLDEPTEGLDaeTERQI-LELLAEhAQNKTVLMITH-RltglEQFDRICvmdnGQIIE 553
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-216 |
6.47e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 56.84 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 32 LVGPNGAGKTTLFRMITGQ-ELPDEGQVAVE---KGMTIgyFDQDVGEMagRSAVAEVMEGAGPVsavaAELRELETAMS 107
Cdd:PRK14247 34 LMGPSGSGKSTLLRVFNRLiELYPEARVSGEvylDGQDI--FKMDVIEL--RRRVQMVFQIPNPI----PNLSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 108 DPdrmdEMDAIVERYGEVQARYEEldgyALEgRAR---EVlaglsfsQEMMDGDVAKLSGGWKMRVALARILLMRPDAML 184
Cdd:PRK14247 106 GL----KLNRLVKSKKELQERVRW----ALE-KAQlwdEV-------KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLL 169
|
170 180 190
....*....|....*....|....*....|....
gi 505055604 185 LDEPSNHLDLESLIWLEN-FLK-GYDGALLMTSH 216
Cdd:PRK14247 170 ADEPTANLDPENTAKIESlFLElKKDMTIVLVTH 203
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
334-497 |
6.54e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 6.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 334 YGSRTIYDgLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV---------------KLGYFAQHSMD 398
Cdd:PRK13643 17 FASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPES 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 399 LLdGESTILQWL----------EERFPKAGQAPLRALagcfGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDE 468
Cdd:PRK13643 96 QL-FEETVLKDVafgpqnfgipKEKAEKIAAEKLEMV----GLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 469 PTNHLDLDTK-EM--LIKALSAYQGTMLFVSH 497
Cdd:PRK13643 171 PTAGLDPKARiEMmqLFESIHQSGQTVVLVTH 202
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-234 |
6.64e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 57.02 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENIS------KSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVG 74
Cdd:PRK13633 4 MIKCKNVSykyesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVD--------GLDTS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 75 EMagrSAVAEVMEGAGPVsavaaelreletaMSDPDRmDEMDAIVERygEVQARYEELDGYALEGRAR--EVLAGLSFSq 152
Cdd:PRK13633 76 DE---ENLWDIRNKAGMV-------------FQNPDN-QIVATIVEE--DVAFGPENLGIPPEEIRERvdESLKKVGMY- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 153 EMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD----LESLIWLENFLKGYDGALLMTSHdreFMNRIVT-- 226
Cdd:PRK13633 136 EYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDpsgrREVVNTIKELNKKYGITIILITH---YMEEAVEad 212
|
....*...
gi 505055604 227 KIIEIDGG 234
Cdd:PRK13633 213 RIIVMDSG 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
341-509 |
6.64e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 57.01 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKlgYFAQHSMDLLDGESTILQWLEERF--PKA 417
Cdd:PRK13639 19 KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIK--YDKKSLLEVRKTVGIVFQNPDDQLfaPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 418 GQ----APLRalagcFGFSGDDVEKRCRV-----------------LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLD 476
Cdd:PRK13639 97 EEdvafGPLN-----LGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 505055604 477 TKEMLIKALSAY--QG-TMLFVSHDRRFLSALSNRV 509
Cdd:PRK13639 172 GASQIMKLLYDLnkEGiTIIISTHDVDLVPVYADKV 207
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
293-497 |
6.75e-09 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 58.58 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 293 KKLEKIDRvePPRRRQTVAFeflpAPRSGEDVVNLKSVHKTYGSRT---IYDGLDFMVRRRERWCIMGINGAGKSTLLKL 369
Cdd:TIGR00958 453 KVFEYLDR--KPNIPLTGTL----APLNLEGLIEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAAL 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 370 VTGTTNPDKGSVSLGAS--VKLGYFAQHSMDLLDGESTIL---------QWLEERFPKAGQAPLRALAGCFGFSGD---- 434
Cdd:TIGR00958 527 LQNLYQPTGGQVLLDGVplVQYDHHYLHRQVALVGQEPVLfsgsvreniAYGLTDTPDEEIMAAAKAANAHDFIMEfpng 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 435 ---DVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQGTMLFVSH 497
Cdd:TIGR00958 607 ydtEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-193 |
1.21e-08 |
|
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: 57.39 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 20 ASAALNRGEKIGLVGPNGAGKTTLFRMITGQeLPDEGQVAVEkgmtigyfDQDVGEMAGRsavaevmegagpvsavaaEL 99
Cdd:COG4172 305 VSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFD--------GQDLDGLSRR------------------AL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 100 RELETAMS----DP-----DRMDEMDAIVEryG-EVQARyeELDGYALEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMR 169
Cdd:COG4172 358 RPLRRRMQvvfqDPfgslsPRMTVGQIIAE--GlRVHGP--GLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQRQR 433
|
170 180
....*....|....*....|....
gi 505055604 170 VALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALD 457
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
320-497 |
1.71e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.96 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 320 SGEDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKLGYFA----- 393
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIdGKPVRIRSPRdaial 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 394 ------QHSMD----------LLDGESTILQWLEerfPKAGQAPLRALAGCFGFsgdDVEKRCRV--LSGGEKARLVMAA 455
Cdd:COG3845 81 gigmvhQHFMLvpnltvaeniVLGLEPTKGGRLD---RKAARARIRELSERYGL---DVDPDAKVedLSVGEQQRVEILK 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505055604 456 MLFDPPNFLVLDEPTNHL-DLDTKEML--IKALSAYQGTMLFVSH 497
Cdd:COG3845 155 ALYRGARILILDEPTAVLtPQEADELFeiLRRLAAEGKSIIFITH 199
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
327-470 |
1.79e-08 |
|
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: 55.37 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVK-----------LGY--- 391
Cdd:COG0410 6 VENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFdGEDITglpphriarlgIGYvpe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 ----FAQ-----------HSMDLLDGESTILQWLEERFPKAGQApLRALAGcfgfsgddvekrcrVLSGGEKARLVMA-A 455
Cdd:COG0410 86 grriFPSltveenlllgaYARRDRAEVRADLERVYELFPRLKER-RRQRAG--------------TLSGGEQQMLAIGrA 150
|
170
....*....|....*
gi 505055604 456 MLFDpPNFLVLDEPT 470
Cdd:COG0410 151 LMSR-PKLLLLDEPS 164
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-193 |
1.90e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.58 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDE---GQVAVEkGMTIGyfdqdvgemagRSAVAEVMEGAGPVsavaa 97
Cdd:PRK13640 27 SFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVD-GITLT-----------AKTVWDIREKVGIV----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 98 elreletaMSDPDRMdemdaiverygEVQARYEELDGYALEGRA----------REVLAGLSFSqEMMDGDVAKLSGGWK 167
Cdd:PRK13640 90 --------FQNPDNQ-----------FVGATVGDDVAFGLENRAvprpemikivRDVLADVGML-DYIDSEPANLSGGQK 149
|
170 180
....*....|....*....|....*.
gi 505055604 168 MRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLD 175
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-234 |
1.93e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 55.76 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSnshrilYIEASAALN-------RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVeKGMTIGYFDQDV 73
Cdd:PRK13644 1 MIRLENVSYS------YPDGTPALEninlvikKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV-SGIDTGDFSKLQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 74 G--------------EMAGRSAVAEVMEGAGPVSAVAAELRELetamsdpdrmdeMDAIVERYGEVQARYEEldgyaleg 139
Cdd:PRK13644 74 GirklvgivfqnpetQFVGRTVEEDLAFGPENLCLPPIEIRKR------------VDRALAEIGLEKYRHRS-------- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 140 rarevlaglsfsqemmdgdVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIW-LENFLKGYDGA--LLMTSH 216
Cdd:PRK13644 134 -------------------PKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAvLERIKKLHEKGktIVYITH 194
|
250
....*....|....*...
gi 505055604 217 DREFMNrIVTKIIEIDGG 234
Cdd:PRK13644 195 NLEELH-DADRIIVMDRG 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
19-238 |
1.96e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 55.21 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 19 EASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVaVEKGmtigyfdQDVGEMAgrsavaevmegagpvSAVAAE 98
Cdd:PRK11629 27 NVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDV-IFNG-------QPMSKLS---------------SAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 99 LRELETAMsdpdrmdemdaiVERYGEVQARYEELDGYAL------------EGRAREVLAGLSFSQEMMDGDvAKLSGGW 166
Cdd:PRK11629 84 LRNQKLGF------------IYQFHHLLPDFTALENVAMplligkkkpaeiNSRALEMLAAVGLEHRANHRP-SELSGGE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 167 KMRVALARILLMRPDAMLLDEPSNHLDL---ESLIWLENFLKGYDG-ALLMTSHDREFMNRIvTKIIEIDGGALTT 238
Cdd:PRK11629 151 RQRVAIARALVNNPRLVLADEPTGNLDArnaDSIFQLLGELNRLQGtAFLVVTHDLQLAKRM-SRQLEMRDGRLTA 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-193 |
2.02e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.38 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKS--NSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGY---------- 68
Cdd:PRK13632 7 MIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKID-GITISKenlkeirkki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 69 ---FDQDVGEMAGRSAVAEVMEGagpvsavaaelreLETAMSDPdrmDEMDAIVERYGEVQARYEELDgyalegraREVL 145
Cdd:PRK13632 86 giiFQNPDNQFIGATVEDDIAFG-------------LENKKVPP---KKMKDIIDDLAKKVGMEDYLD--------KEPQ 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505055604 146 aglsfsqemmdgdvaKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK13632 142 ---------------NLSGGQKQRVAIASVLALNPEIIIFDESTSMLD 174
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
335-513 |
2.22e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.42 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKLGYFAQHSmDLL--------DGEST 405
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWqGEPIRRQRDEYHQ-DLLylghqpgiKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 406 ILQWLeeRFPKAGQAPLR------ALAGcFGFSG-DDVEkrCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK 478
Cdd:PRK13538 91 ALENL--RFYQRLHGPGDdealweALAQ-VGLAGfEDVP--VRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 505055604 479 EMLIKALSAY--QGTM-LFVSHDRrfLSALSNRVLELT 513
Cdd:PRK13538 166 ARLEALLAQHaeQGGMvILTTHQD--LPVASDKVRKLR 201
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
324-498 |
2.30e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.62 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTYGSRT-IYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASvKLGYFAQHSMDLLDG 402
Cdd:PRK13636 5 ILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGK-PIDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 ESTILQWLEER-FPKAGQAPLRALAGCFGFSGDDVEKRCR-----------------VLSGGEKARLVMAAMLFDPPNFL 464
Cdd:PRK13636 84 VGMVFQDPDNQlFSASVYQDVSFGAVNLKLPEDEVRKRVDnalkrtgiehlkdkpthCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 505055604 465 VLDEPTNHLD-LDTKEMLIKALSAYQG---TMLFVSHD 498
Cdd:PRK13636 164 VLDEPTAGLDpMGVSEIMKLLVEMQKElglTIIIATHD 201
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
27-196 |
2.44e-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: 54.80 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDvgemAGRSAVAEVMEGAGPVSAVAAElrelETAM 106
Cdd:cd03252 28 GEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVD-GHDLALADPA----WLRRQVGVVLQENVLFNRSIRD----NIAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 107 SDPDrMDeMDAIVErygevQARyeeldgyaLEGrAREVLAGLSFSQEMMDGDV-AKLSGGWKMRVALARILLMRPDAMLL 185
Cdd:cd03252 99 ADPG-MS-MERVIE-----AAK--------LAG-AHDFISELPEGYDTIVGEQgAGLSGGQRQRIAIARALIHNPRILIF 162
|
170
....*....|.
gi 505055604 186 DEPSNHLDLES 196
Cdd:cd03252 163 DEATSALDYES 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2-196 |
2.59e-08 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 54.54 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKS-NSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIgyfdQDVGEMAGRS 80
Cdd:cd03254 3 IEFENVNFSyDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILID-GIDI----RDISRKSLRS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEGAGPVSavaaelreletamsdpdrmdemDAIVE--RYGEVQARYEELDGYALEGRAREVLAGLSFSQEMMDGD 158
Cdd:cd03254 78 MIGVVLQDTFLFS----------------------GTIMEniRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGE 135
|
170 180 190
....*....|....*....|....*....|....*....
gi 505055604 159 VAK-LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES 196
Cdd:cd03254 136 NGGnLSQGERQLLAIARAMLRDPKILILDEATSNIDTET 174
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
24-225 |
2.77e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 54.69 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQEL--PDEGQVavekgmtigYFD-QDVGEMagrsavaEVME--GAG-------P 91
Cdd:COG0396 23 IKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSI---------LLDgEDILEL-------SPDEraRAGiflafqyP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 92 VS----AVAAELRELETAMsdpdrmdemdaiverygevqaRYEELDGYALEGRAREVLAGLSFSQEMMDGDV-AKLSGGW 166
Cdd:COG0396 87 VEipgvSVSNFLRTALNAR---------------------RGEELSAREFLKLLKEKMKELGLDEDFLDRYVnEGFSGGE 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 167 KMRVALARILLMRPDAMLLDEPSNHLDLESL------IwleNFLKGYDGALLMTSHDREFMNRIV 225
Cdd:COG0396 146 KKRNEILQMLLLEPKLAILDETDSGLDIDALrivaegV---NKLRSPDRGILIITHYQRILDYIK 207
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
17-217 |
2.79e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 55.24 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 17 YIEASAALN-------RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVaVEKGMTIGYFDQdvGEMAGRSAVAEVMEga 89
Cdd:PRK13636 15 YSDGTHALKgininikKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGKPIDYSRK--GLMKLRESVGMVFQ-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 90 gpvsavaaelreletamsDPDRMDEMDAIVE--RYGEVQARYEELDgyaLEGRAREVLAGLSFSQeMMDGDVAKLSGGWK 167
Cdd:PRK13636 90 ------------------DPDNQLFSASVYQdvSFGAVNLKLPEDE---VRKRVDNALKRTGIEH-LKDKPTHCLSFGQK 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505055604 168 MRVALARILLMRPDAMLLDEPSNHLD----LESLIWLENFLKGYDGALLMTSHD 217
Cdd:PRK13636 148 KRVAIAGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKELGLTIIIATHD 201
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
325-530 |
3.11e-08 |
|
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: 54.47 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSR---TIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLD 401
Cdd:cd03249 1 IEFKNVSFRYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEI-----------------LLD 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 402 GEST---ILQWLEERFPKAGQAPL--------RALAGCFGFSGDDVEKRCRV------------------------LSGG 446
Cdd:cd03249 64 GVDIrdlNLRWLRSQIGLVSQEPVlfdgtiaeNIRYGKPDATDEEVEEAAKKanihdfimslpdgydtlvgergsqLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 447 EKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALS-AYQG-TMLFVSHdRrfLSALSN----------RVLEL-T 513
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDrAMKGrTTIVIAH-R--LSTIRNadliavlqngQVVEQgT 220
|
250
....*....|....*..
gi 505055604 514 PDGINQYGGGYSEYVER 530
Cdd:cd03249 221 HDELMAQKGVYAKLVKA 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
323-510 |
3.15e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 3.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 323 DVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV-----------KLGY 391
Cdd:PRK13650 6 EVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLlteenvwdirhKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 FAQHSMDL-------------LDGESTILQWLEERFPKAGQaplraLAGCFGFSgddvEKRCRVLSGGEKARLVMAAMLF 458
Cdd:PRK13650 86 VFQNPDNQfvgatveddvafgLENKGIPHEEMKERVNEALE-----LVGMQDFK----EREPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 459 DPPNFLVLDEPTNHLDLDTKEMLIKALSA----YQGTMLFVSHDRRFLsALSNRVL 510
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHDLDEV-ALSDRVL 211
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
325-539 |
3.42e-08 |
|
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: 55.96 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTN--PDKGSV--SLGASVKLGY--------- 391
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyHVALCEKCGYverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 --------FAQHSMDLLDGESTILQWLEERFPKAGQAP-------------LRALAGcFGFSGDDVEKRC---------- 440
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTfalygddtvldnvLEALEE-IGYEGKEAVGRAvdliemvqls 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 441 -------RVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDT----KEMLIKALSAYQGTMLFVSHDRRFLSALSNRV 509
Cdd:TIGR03269 160 hrithiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTaklvHNALEEAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250 260 270
....*....|....*....|....*....|
gi 505055604 510 LELTPDGINQYGGGySEYVERTGQEAPGLR 539
Cdd:TIGR03269 240 IWLENGEIKEEGTP-DEVVAVFMEGVSEVE 268
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-217 |
3.42e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENIS---KSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfdqdvGEMA 77
Cdd:PRK13650 4 IIEVKNLTfkyKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIID------------GDLL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRSAVAEVMEGAGPVsavaaelreletaMSDPDRmDEMDAIVE------------RYGEVQARYEEldgyALEgrarevL 145
Cdd:PRK13650 72 TEENVWDIRHKIGMV-------------FQNPDN-QFVGATVEddvafglenkgiPHEEMKERVNE----ALE------L 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 146 AGLsfsQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKG----YDGALLMTSHD 217
Cdd:PRK13650 128 VGM---QDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirddYQMTVISITHD 200
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
323-509 |
3.90e-08 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 56.56 E-value: 3.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 323 DVVNLKSVHKTYG--SRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV---------KLG 390
Cdd:TIGR01257 1936 DILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVaGKSIltnisdvhqNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 391 YFAQHSM--DLLDGESTILQWLE------ERFPKAGQAPLRALagcfGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPN 462
Cdd:TIGR01257 2016 YCPQFDAidDLLTGREHLYLYARlrgvpaEEIEKVANWSIQSL----GLS-LYADRLAGTYSGGNKRKLSTAIALIGCPP 2090
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 463 FLVLDEPTNHLDLDTKEML---IKALSAYQGTMLFVSHDRRFLSALSNRV 509
Cdd:TIGR01257 2091 LVLLDEPTTGMDPQARRMLwntIVSIIREGRAVVLTSHSMEECEALCTRL 2140
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-236 |
4.00e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 54.61 E-value: 4.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDVGEMAGRSAVAEVMEGAGPVSAVAAELRELETAM 106
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 107 SDPDRMDEMDAIVErygevqaryeeldgyALEGRAREVLAGLSfsqemmdgdVAKLSGGWKMRVALARILLMRPDAMLLD 186
Cdd:PRK10253 113 FTRWRKEDEEAVTK---------------AMQATGITHLADQS---------VDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 187 EPSNHLDLESLIWLENFL------KGYDGALLMtsHDREFMNRIVTKIIEIDGGAL 236
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLselnreKGYTLAAVL--HDLNQACRYASHLIALREGKI 222
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
328-512 |
4.03e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.01 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 328 KSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV--------------KLGYF 392
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLhqmdeearaklrakHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 393 AQHSM--------------DLLDGEStilqwleERFPKAGQAPLRALAGCfgfsGDDVEKRCRVLSGGEKARLVMAAMLF 458
Cdd:PRK10584 94 FQSFMliptlnalenvelpALLRGES-------SRQSRNGAKALLEQLGL----GKRLDHLPAQLSGGEQQRVALARAFN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 459 DPPNFLVLDEPTNHLDLDTKEMLIKALSA----YQGTMLFVSHDRRfLSALSNRVLEL 512
Cdd:PRK10584 163 GRPDVLFADEPTGNLDRQTGDKIADLLFSlnreHGTTLILVTHDLQ-LAARCDRRLRL 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
315-497 |
4.12e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 55.24 E-value: 4.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 315 LPAPRSGEDVV---NLKSV--HKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKL 389
Cdd:PRK13631 12 VPNPLSDDIILrvkNLYCVfdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 390 GYFAQHSMDLLDGESTILQWLEER--------FPK------------------AGQAPLRA--LAGCF----GFSGDDVE 437
Cdd:PRK13631 92 DKKNNHELITNPYSKKIKNFKELRrrvsmvfqFPEyqlfkdtiekdimfgpvaLGVKKSEAkkLAKFYlnkmGLDDSYLE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 438 KRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLD-TKEM--LIKALSAYQGTMLFVSH 497
Cdd:PRK13631 172 RSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKgEHEMmqLILDAKANNKTVFVITH 234
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
334-498 |
4.94e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 54.25 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 334 YGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGA-----------SVKLGYFAQHsmdLLDG 402
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismlssrqlARRLALLPQH---HLTP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 ESTILQWLEERfpkaGQAPLRALAGcfGFSGDD----------------VEKRCRVLSGGEKARLVMAAMLFDPPNFLVL 466
Cdd:PRK11231 89 EGITVRELVAY----GRSPWLSLWG--RLSAEDnarvnqameqtrinhlADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 505055604 467 DEPTNHLDLDTK-EM--LIKALSAYQGTMLFVSHD 498
Cdd:PRK11231 163 DEPTTYLDINHQvELmrLMRELNTQGKTVVTVLHD 197
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
327-505 |
5.66e-08 |
|
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: 53.80 E-value: 5.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGttNPD----KGSVSLGASV----------KLGYF 392
Cdd:TIGR01978 3 IKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFKGQDllelepderaRAGLF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 393 A--QHSMDL--LDGESTILQWLEERFPKAGQAPLRALA---------GCFGFSGDDVEKRCRV-LSGGEKARLVMAAMLF 458
Cdd:TIGR01978 81 LafQYPEEIpgVSNLEFLRSALNARRSARGEEPLDLLDfekllkeklALLDMDEEFLNRSVNEgFSGGEKKRNEILQMAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 459 DPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG---TMLFVSHDRRFLSAL 505
Cdd:TIGR01978 161 LEPKLAILDEIDSGLDIDALKIVAEGINRLREpdrSFLIITHYQRLLNYI 210
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-193 |
5.81e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 55.52 E-value: 5.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV-----------EKGMTIGYFDQDVGEMAGrsAVAEVmega 89
Cdd:COG4618 352 SFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLdgadlsqwdreELGRHIGYLPQDVELFDG--TIAEN---- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 90 gpvsaVAaelReletaMSDPDrmdeMDAIVErygevqaryeeldgyAlegrARevLAG-----LSFSQ---EMMDGDVAK 161
Cdd:COG4618 426 -----IA---R-----FGDAD----PEKVVA---------------A----AK--LAGvhemiLRLPDgydTRIGEGGAR 467
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG4618 468 LSGGQRQRIGLARALYGDPRLVVLDEPNSNLD 499
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
325-498 |
6.34e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 54.69 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfaqhsmdLLDGEs 404
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI-----------------LIGGR- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 tILQWLE--ER----------------------FpkagqaPLRALagcfGFSGDDVEKRCRV-----------------L 443
Cdd:COG3839 66 -DVTDLPpkDRniamvfqsyalyphmtvyeniaF------PLKLR----KVPKAEIDRRVREaaellgledlldrkpkqL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 444 SGGEKARLVMA-AMLFDPPNFLvLDEPTNHLDLDTKEML---IKALSAYQG-TMLFVSHD 498
Cdd:COG3839 135 SGGQRQRVALGrALVREPKVFL-LDEPLSNLDAKLRVEMraeIKRLHRRLGtTTIYVTHD 193
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
326-498 |
7.38e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 53.55 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 326 NLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL------GASVKLGYFAQHS--- 396
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLdgkpveGPGAERGVVFQNEgll 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 --MDLLDGESTILQWL----EERFPKAGQapLRALAGCFGFSgddvEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPT 470
Cdd:PRK11248 83 pwRNVQDNVAFGLQLAgvekMQRLEIAHQ--MLKKVGLEGAE----KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPF 156
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 471 NHLDLDTKE-MLIKALSAYQGT---MLFVSHD 498
Cdd:PRK11248 157 GALDAFTREqMQTLLLKLWQETgkqVLLITHD 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-217 |
9.71e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 54.71 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTT----LFRMITGQelpdeGQVavekgmtigYFDQDVGEMAGRSAVAevmegagPVSava 96
Cdd:PRK15134 306 SFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEI---------WFDGQPLHNLNRRQLL-------PVR--- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 97 aelRELETAMSDPD-----RMDEMDAIVErygEVQARYEELDGYALEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVA 171
Cdd:PRK15134 362 ---HRIQVVFQDPNsslnpRLNVLQIIEE---GLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIA 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 172 LARILLMRPDAMLLDEPSNHLD----LESLIWLENFLKGYDGALLMTSHD 217
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDktvqAQILALLKSLQQKHQLAYLFISHD 485
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-198 |
1.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 53.58 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENIS---KSNS---HRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVG 74
Cdd:PRK13643 1 MIKFEKVNytyQPNSpfaSRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--------DIVVS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 75 EMAGRSAVAEVMEGAGPVSAVAAELRELETAMSDpdrmdeMDAIVERYGEVQARYEELdgyalegrAREVLAGLSFSQEM 154
Cdd:PRK13643 72 STSKQKEIKPVRKKVGVVFQFPESQLFEETVLKD------VAFGPQNFGIPKEKAEKI--------AAEKLEMVGLADEF 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505055604 155 MDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLI 198
Cdd:PRK13643 138 WEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
325-498 |
1.20e-07 |
|
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: 52.57 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLK-------LVTGTtnPDKGSVSLGASvklgyfaqhsm 397
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRllnrlndLIPGA--PDEGEVLLDGK----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 398 DLLDGESTILqWLEER----------FPK---------------AGQAPLRAL-------AGCFgfsgDDVEKR--CRVL 443
Cdd:cd03260 68 DIYDLDVDVL-ELRRRvgmvfqkpnpFPGsiydnvayglrlhgiKLKEELDERveealrkAALW----DEVKDRlhALGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 444 SGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK---EMLIKALSAyQGTMLFVSHD 498
Cdd:cd03260 143 SGGQQQRLCLARALANEPEVLLLDEPTSALDPISTakiEELIAELKK-EYTIVIVTHN 199
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-217 |
1.28e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 52.92 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGqELPDEGQVAVEkGMTIGyfDQDVGEMAGRSA-------------VAEVME 87
Cdd:COG4138 16 SAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLN-GRPLS--DWSAAELARHRAylsqqqsppfampVFQYLA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 88 GAGPVSAVAAELRELetamsdpdrmdeMDAIVERYGevqaryeeLDgyALEGRarevlaglSFSQemmdgdvakLSGG-W 166
Cdd:COG4138 92 LHQPAGASSEAVEQL------------LAQLAEALG--------LE--DKLSR--------PLTQ---------LSGGeW 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 167 KmRVALARILL-----MRPDA--MLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHD 217
Cdd:COG4138 133 Q-RVRLAAVLLqvwptINPEGqlLLLDEPMNSLDVAQQAALDRLLRELcqqGITVVMSSHD 192
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
341-510 |
1.39e-07 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 51.66 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKL---GYFAQHSMDLLdgestilqwLEERFpK 416
Cdd:cd03215 17 RDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRrspRDAIRAGIAYV---------PEDRK-R 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 417 AGQAPLRALAGCFGFSgddvekrcRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEM---LIKALSAYQGTML 493
Cdd:cd03215 87 EGLVLDLSVAENIALS--------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEiyrLIRELADAGKAVL 158
|
170
....*....|....*..
gi 505055604 494 FVSHDRRFLSALSNRVL 510
Cdd:cd03215 159 LISSELDELLGLCDRIL 175
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-235 |
1.39e-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: 51.39 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENIS-KSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGqeLPDEGQvavekGmTIGyfdqdvgeMAGRS 80
Cdd:cd03223 1 IELENLSlATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG--LWPWGS-----G-RIG--------MPEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVmegagpvsavaaelreletamsdPDRmdemdaiverygevqaryeeldGYALEGRAREVLAgLSFSQEmmdgdva 160
Cdd:cd03223 65 DLLFL-----------------------PQR----------------------PYLPLGTLREQLI-YPWDDV------- 91
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 161 kLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGYDGALLMTSHdREFMNRIVTKIIEIDGGA 235
Cdd:cd03223 92 -LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGITVISVGH-RPSLWKFHDRVLDLDGEG 164
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
335-499 |
1.48e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 54.20 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVK----------LGYFAQHSMdLLDge 403
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIdGTDIRtvtraslrrnIAVVFQDAG-LFN-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 404 STILQWLEERFPKAGQAPLRALA-------------GCFGFsgdDVEKRCRVLSGGEKARLVMA-AMLFDPPnFLVLDEP 469
Cdd:PRK13657 423 RSIEDNIRVGRPDATDEEMRAAAeraqahdfierkpDGYDT---VVGERGRQLSGGERQRLAIArALLKDPP-ILILDEA 498
|
170 180 190
....*....|....*....|....*....|
gi 505055604 470 TNHLDLDTKEMLIKALSAyqgtmlfVSHDR 499
Cdd:PRK13657 499 TSALDVETEAKVKAALDE-------LMKGR 521
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
334-498 |
1.54e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 334 YGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV----------KLGYFAQHSMDllDG 402
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdGEHIqhyaskevarRIGLLAQNATT--PG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 ESTILQWLEE-RFPkagQAPL---------RALAGCFGFSG--DDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPT 470
Cdd:PRK10253 95 DITVQELVARgRYP---HQPLftrwrkedeEAVTKAMQATGitHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 471 NHLDLDTKEMLIKALSAY---QG-TMLFVSHD 498
Cdd:PRK10253 172 TWLDISHQIDLLELLSELnreKGyTLAAVLHD 203
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
6-194 |
1.67e-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: 52.75 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 6 NISKSNSHRilYIEASAALNR------GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtiGYFDQDVGEMAGr 79
Cdd:cd03236 1 ELEDEPVHR--YGPNSFKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDP-----PDWDEILDEFRG- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 savaevmegagpvsavaAELRELETAMSDpdrmDEMDAIverygeVQARYEELDGYALEGRAREVLAG------------ 147
Cdd:cd03236 73 -----------------SELQNYFTKLLE----GDVKVI------VKPQYVDLIPKAVKGKVGELLKKkdergkldelvd 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505055604 148 -LSFSQeMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL 194
Cdd:cd03236 126 qLELRH-VLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
325-497 |
1.78e-07 |
|
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: 52.23 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYG-SRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGA----SVKLGYFAQH---- 395
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirEVTLDSLRRAigvv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 --SMDLLDgeSTILQWLEERFPKAGQAPLR--ALAGC---------FGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPN 462
Cdd:cd03253 81 pqDTVLFN--DTIGYNIRYGRPDATDEEVIeaAKAAQihdkimrfpDGYD-TIVGERGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 505055604 463 FLVLDEPTNHLDLDTKEMLIKALSAYQG--TMLFVSH 497
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKgrTTIVIAH 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
355-510 |
1.85e-07 |
|
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: 53.18 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVklgyfaqhsmdLLDGESTIlqWL--EER-----------FP------ 415
Cdd:COG4148 30 LFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEV-----------LQDSARGI--FLppHRRrigyvfqearlFPhlsvrg 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 416 --KAGQAPLRALAGCFGFsgDDV----------EKRCRVLSGGEKARLVMA-AMLFDpPNFLVLDEPTNHLDLDTK-EML 481
Cdd:COG4148 97 nlLYGRKRAPRAERRISF--DEVvellgighllDRRPATLSGGERQRVAIGrALLSS-PRLLLMDEPLAALDLARKaEIL 173
|
170 180 190
....*....|....*....|....*....|..
gi 505055604 482 --IKALSAYQGT-MLFVSHDRRFLSALSNRVL 510
Cdd:COG4148 174 pyLERLRDELDIpILYVSHSLDEVARLADHVV 205
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-193 |
2.20e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.88 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 6 NISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQEL--PDEGQVAVEKGMtigyFDQD------VGEMA 77
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQ----FGREaslidaIGRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRSAVAEVMEGAGPVSAVAaeLReletamsdpdrmdemdaiverygevqARYEEldgyalegrarevlaglsfsqemmdg 157
Cdd:COG2401 111 DFKDAVELLNAVGLSDAVL--WL--------------------------RRFKE-------------------------- 136
|
170 180 190
....*....|....*....|....*....|....*.
gi 505055604 158 dvakLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG2401 137 ----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
340-497 |
2.54e-07 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 51.89 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 340 YDGL----DFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKLGYFAQHSMDLLDGES------TILQ 408
Cdd:PRK10771 11 YHHLpmrfDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPVSMLFQENnlfshlTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 409 WLE------ERFPKAGQAPLRALAGCFGFSgDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK-EML 481
Cdd:PRK10771 91 NIGlglnpgLKLNAAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRqEML 169
|
170
....*....|....*....
gi 505055604 482 I---KALSAYQGTMLFVSH 497
Cdd:PRK10771 170 TlvsQVCQERQLTLLMVSH 188
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
19-248 |
2.78e-07 |
|
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: 53.20 E-value: 2.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 19 EASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmTIGYFD-QDVGEMAGRSAVAEVMEGagPVSAVAA 97
Cdd:TIGR01193 492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEI------LLNGFSlKDIDRHTLRQFINYLPQE--PYIFSGS 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 98 ELRELETAMSDPDRMDEMDAIVErYGEVQARYEELD-GYALEgrarevLAGLSFSqemmdgdvakLSGGWKMRVALARIL 176
Cdd:TIGR01193 564 ILENLLLGAKENVSQDEIWAACE-IAEIKDDIENMPlGYQTE------LSEEGSS----------ISGGQKQRIALARAL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 177 LMRPDAMLLDEPSNHLDL--ESLIwLENFLKGYDGALLMTSHdREFMNRIVTKIIEIDGGALTTySGDY-------GFYD 247
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTitEKKI-VNNLLNLQDKTIIFVAH-RLSVAKQSDKIIVLDHGKIIE-QGSHdelldrnGFYA 703
|
.
gi 505055604 248 E 248
Cdd:TIGR01193 704 S 704
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
32-253 |
3.17e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 51.93 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 32 LVGPNGAGKTTLFRMITGQELPDEGQvavekgmTIgyfdqdVGEMAGRSAVAEVMEgagpvsaVAAELRELETAMSDPDR 111
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQ-------TI------VGDYAIPANLKKIKE-------VKRLRKEIGLVFQFPEY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 112 MDEMDAIVE--RYGEVQARYEELDGYAlegRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPS 189
Cdd:PRK13645 102 QLFQETIEKdiAFGPVNLGENKQEAYK---KVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 190 NHLD---LESLIWL-ENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGALTTYSGDYGFYDEQRALN 253
Cdd:PRK13645 179 GGLDpkgEEDFINLfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLT 246
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-194 |
3.20e-07 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 51.75 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGqELPDEGQ---VAVEKGMTIG---YFDQDVG 74
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG-DLTGGGAprgARVTGDVTLNgepLAAIDAP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 75 EMAGRSAV-AEVMEGAGPVSAvaaelRELETAMSDPDrmdemdaiVERYGEVQARYEELDGYALEGRAREVLAGLsfsqe 153
Cdd:PRK13547 80 RLARLRAVlPQAAQPAFAFSA-----REIVLLGRYPH--------ARRAGALTHRDGEIAWQALALAGATALVGR----- 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 154 mmdgDVAKLSGGWKMRVALARIL---------LMRPDAMLLDEPSNHLDL 194
Cdd:PRK13547 142 ----DVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDL 187
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-196 |
3.35e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 52.92 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQeLPDEGQVAVEkgmtiGYFDQDVGEMAGRSAVAEVmeGAGPvSAVAAELR 100
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKIN-----GIELRELDPESWRKHLSWV--GQNP-QLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 ElETAMSDPDRMDEmdaiverygEVQAryeeldgyALE-GRAREVLAGLSFSQEMMDGD-VAKLSGGWKMRVALARILLM 178
Cdd:PRK11174 441 D-NVLLGNPDASDE---------QLQQ--------ALEnAWVSEFLPLLPQGLDTPIGDqAAGLSVGQAQRLALARALLQ 502
|
170
....*....|....*...
gi 505055604 179 RPDAMLLDEPSNHLDLES 196
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHS 520
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
332-512 |
4.07e-07 |
|
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: 50.72 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 332 KTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPD---KGSVSLGASVKLGYFAQHSMDLL-DGES--- 404
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIyVSEEdvh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 ----TILQWLEerfpkagqaplralagcfgFS----GDDVekrCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLD 476
Cdd:cd03233 95 fptlTVRETLD-------------------FAlrckGNEF---VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 505055604 477 TK-EML--IKALSAYQGTMLFVShdrrfLSALSNRVLEL 512
Cdd:cd03233 153 TAlEILkcIRTMADVLKTTTFVS-----LYQASDEIYDL 186
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
317-497 |
4.31e-07 |
|
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: 50.93 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 317 APRSGEDVVNLKSVHKTYGSRT---IYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgyfa 393
Cdd:cd03248 4 APDHLKGIVKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQV------------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 394 qhsmdLLDGESTIL---QWLEERFPKAGQAPL---------------------------RALAGCF------GFSgDDVE 437
Cdd:cd03248 72 -----LLDGKPISQyehKYLHSKVSLVGQEPVlfarslqdniayglqscsfecvkeaaqKAHAHSFiselasGYD-TEVG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 438 KRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALsaYQG----TMLFVSH 497
Cdd:cd03248 146 EKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL--YDWperrTVLVIAH 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-231 |
4.45e-07 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 51.98 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEA----SAALNRGEKIGLVGPNGAGKTTLFRMITGQeLPDEGQVAvekGmTIGYFDQDVGEM 76
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAvdgvSFDVRRGETLGLVGESGSGKSTLARAILGL-LPPPGITS---G-EILFDGEDLLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 77 AGRsavaevmegagpvsavaaELREL---ETAM--SDPdrmdeMDAIVERY------GEVQARYEELDGYALEGRAREVL 145
Cdd:COG0444 76 SEK------------------ELRKIrgrEIQMifQDP-----MTSLNPVMtvgdqiAEPLRIHGGLSKAEARERAIELL 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 146 A--GLSFSQEMMDgdvaK----LSGGWKMRVALARILLMRPDAMLLDEPSNHLD----------LESLIwlenflKGYDG 209
Cdd:COG0444 133 ErvGLPDPERRLD----RypheLSGGMRQRVMIARALALEPKLLIADEPTTALDvtiqaqilnlLKDLQ------RELGL 202
|
250 260 270
....*....|....*....|....*....|
gi 505055604 210 ALLMTSHD----REFMNRIVT----KIIEI 231
Cdd:COG0444 203 AILFITHDlgvvAEIADRVAVmyagRIVEE 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
27-193 |
4.93e-07 |
|
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: 50.24 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQ--ELPDEGQVAVEkGMT---------IGYFDQDvgEMA-GRSAVAEVMEgagpvsa 94
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLIN-GRPldkrsfrkiIGYVPQD--DILhPTLTVRETLM------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 95 VAAELReletamsdpdrmdemdaiverygevqaryeeldgyalegrarevlaglsfsqemmdgdvaKLSGGWKMRVALAR 174
Cdd:cd03213 105 FAAKLR------------------------------------------------------------GLSGGERKRVSIAL 124
|
170
....*....|....*....
gi 505055604 175 ILLMRPDAMLLDEPSNHLD 193
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLD 143
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
21-236 |
5.32e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.32 E-value: 5.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVGEMAGRSAVAEVMEgagpvsavAAELR 100
Cdd:PRK13646 27 NTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-DITITHKTKDKYIRPVRKRIGMVFQ--------FPESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 ELETAmsdpdrmdemdaiVERYGEVQARYEELDGYALEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRP 180
Cdd:PRK13646 98 LFEDT-------------VEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 181 DAMLLDEPSNHLDLESLIWLENFLKGY----DGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLqtdeNKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
26-233 |
5.45e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 50.55 E-value: 5.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgMTIGyfdQDVGEMAGRSAVAEVMEGAGPVSA---VAAELREL 102
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGLDDGSSGEV-----SLVG---QPLHQMDEEARAKLRAKHVGFVFQsfmLIPTLNAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 103 ETAmsdpdrmdEMDAIVERYGEVQARyeeldgyaleGRAREVLAGLSFSQEMmDGDVAKLSGGWKMRVALARILLMRPDA 182
Cdd:PRK10584 107 ENV--------ELPALLRGESSRQSR----------NGAKALLEQLGLGKRL-DHLPAQLSGGEQQRVALARAFNGRPDV 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 183 MLLDEPSNHLDLESLIWLENFL----KGYDGALLMTSHDREFMNRIVTKIIEIDG 233
Cdd:PRK10584 168 LFADEPTGNLDRQTGDKIADLLfslnREHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
332-510 |
5.78e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 5.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 332 KTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL----GASVKL----------------GY 391
Cdd:PRK11701 14 KLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdGQLRDLyalseaerrrllrtewGF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 FAQHSMDLLDGESTILQWLEERFPKAGQ---APLRALAgcfGFSGDDVE-------KRCRVLSGGEKARLVMAAMLFDPP 461
Cdd:PRK11701 94 VHQHPRDGLRMQVSAGGNIGERLMAVGArhyGDIRATA---GDWLERVEidaaridDLPTTFSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 462 NFLVLDEPTNHLD-------LDtkemLIKALSAYQG-TMLFVSHDRRFLSALSNRVL 510
Cdd:PRK11701 171 RLVFMDEPTGGLDvsvqarlLD----LLRGLVRELGlAVVIVTHDLAVARLLAHRLL 223
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
325-484 |
5.80e-07 |
|
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: 50.69 E-value: 5.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGS--RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV----------KLGY 391
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIdGHDVrdytlaslrrQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 FAQHSMdLLDGesTILQWLEERFPKAGQAPLRA---LAGCFGF-----SGDD--VEKRCRVLSGGEKARLVMA-AMLFDP 460
Cdd:cd03251 81 VSQDVF-LFND--TVAENIAYGRPGATREEVEEaarAANAHEFimelpEGYDtvIGERGVKLSGGQRQRIAIArALLKDP 157
|
170 180
....*....|....*....|....
gi 505055604 461 PnFLVLDEPTNHLDLDTkEMLIKA 484
Cdd:cd03251 158 P-ILILDEATSALDTES-ERLVQA 179
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-225 |
5.92e-07 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 50.22 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQE--LPDEGQVAVEkgmtigyfDQDVGEMagrsavaEVMEGAgpvsavaae 98
Cdd:cd03217 20 NLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFK--------GEDITDL-------PPEERA--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 99 LRELETAMSDPdrmdemdaiverygevqaryEELDGYALEGRAREVLAGLSfsqemmdgdvaklsGGWKMRVALARILLM 178
Cdd:cd03217 76 RLGIFLAFQYP--------------------PEIPGVKNADFLRYVNEGFS--------------GGEKKRNEILQLLLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 179 RPDAMLLDEPSNHLDLESLIWLE---NFLKGYDGALLMTSHDREFMNRIV 225
Cdd:cd03217 122 EPDLAILDEPDSGLDIDALRLVAeviNKLREEGKSVLIITHYQRLLDYIK 171
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
327-521 |
6.11e-07 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 50.78 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLgasvklgyfAQHSMDLLDGES-- 404
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNI---------AGHQFDFSQKPSek 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 ----------------------TILQWLEErfpkagqAPLRALagcfGFSGDDVEKRCRV-----------------LSG 445
Cdd:COG4161 76 airllrqkvgmvfqqynlwphlTVMENLIE-------APCKVL----GLSKEQAREKAMKllarlrltdkadrfplhLSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 446 GEKARLVMAAMLFDPPNFLVLDEPTNHLDLD-TKEM--LIKALSAYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:COG4161 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVveIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
326-498 |
6.41e-07 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 51.02 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 326 NLKSVHKTYG----SRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL------GASVKLGYFAQH 395
Cdd:COG4525 5 TVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLdgvpvtGPGADRGVVFQK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 SmdlldgesTILQWL-----------------EERFPKAGQapLRALAGCFGFSGDDVEKrcrvLSGGEKARLVMAAMLF 458
Cdd:COG4525 85 D--------ALLPWLnvldnvafglrlrgvpkAERRARAEE--LLALVGLADFARRRIWQ----LSGGMRQRVGIARALA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505055604 459 DPPNFLVLDEPTNHLDLDTKE----MLIKALSAYQGTMLFVSHD 498
Cdd:COG4525 151 ADPRFLLMDEPFGALDALTREqmqeLLLDVWQRTGKGVFLITHS 194
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-194 |
6.51e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 6.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigYFDQDV------GEMAGRSAVAEVMEGagP--- 91
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELY--------YQGQDLlkadpeAQKLLRQKIQIVFQN--Pygs 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 92 ------VSAVAAELRELETAMSDPDRMDEMDAIVERYGevqARYEELDGYAlegrarevlaglsfsqEMmdgdvakLSGG 165
Cdd:PRK11308 105 lnprkkVGQILEEPLLINTSLSAAERREKALAMMAKVG---LRPEHYDRYP----------------HM-------FSGG 158
|
170 180
....*....|....*....|....*....
gi 505055604 166 WKMRVALARILLMRPDAMLLDEPSNHLDL 194
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDV 187
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
339-521 |
6.60e-07 |
|
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: 50.10 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 339 IYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLgasvklgyfaqhsmDLLDGESTILQWLEERFPKAG 418
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI--------------DGIDISTIPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 419 QAP------LRALAGCFG-FSGDDVEKRCRV------LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKAL 485
Cdd:cd03369 89 QDPtlfsgtIRSNLDPFDeYSDEEIYGALRVsegglnLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*...
gi 505055604 486 -SAYQG-TMLFVSHDRRFLsALSNRVLELTPDGINQYG 521
Cdd:cd03369 169 rEEFTNsTILTIAHRLRTI-IDYDKILVMDAGEVKEYD 205
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
26-188 |
6.62e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 50.16 E-value: 6.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGqELP-DEGQVAVEKgmTIGYFDQdvgemagrsaVAEVMEGAgpvsavaaeLRE--L 102
Cdd:cd03250 30 KGELVAIVGPVGSGKSSLLSALLG-ELEkLSGSVSVPG--SIAYVSQ----------EPWIQNGT---------IREniL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 103 etaMSDPdrMDEmdaivERYGEVqaryeeLDGYALEgraREVlaglsfsQEMMDGDV-------AKLSGGWKMRVALARI 175
Cdd:cd03250 88 ---FGKP--FDE-----ERYEKV------IKACALE---PDL-------EILPDGDLteigekgINLSGGQKQRISLARA 141
|
170
....*....|...
gi 505055604 176 LLMRPDAMLLDEP 188
Cdd:cd03250 142 VYSDADIYLLDDP 154
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-188 |
6.83e-07 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 50.50 E-value: 6.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 10 SNSHRILYIEA--------------SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigYFDQDvgE 75
Cdd:COG4674 5 TMHGPILYVEDltvsfdgfkalndlSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSV---------LFGGT--D 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 76 MAGRSAVAEVMEGAG-----PvsAVAAEL--RE-LETAMS-------------DPDRMDEMDAIVERYGevqaryeeldg 134
Cdd:COG4674 74 LTGLDEHEIARLGIGrkfqkP--TVFEELtvFEnLELALKgdrgvfaslfarlTAEERDRIEEVLETIG----------- 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505055604 135 yaLEGRaREVLAGLsfsqemmdgdvakLSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:COG4674 141 --LTDK-ADRLAGL-------------LSHGQKQWLEIGMLLAQDPKLLLLDEP 178
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
341-510 |
7.28e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGA------SVKL-------GYFAQHSMdlldgestiL 407
Cdd:PRK13637 24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGvditdkKVKLsdirkkvGLVFQYPE---------Y 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 408 QWLEERFPKAGQAPLRALagcfGFSGDDVEKRCRV-------------------LSGGEKARLVMAAMLFDPPNFLVLDE 468
Cdd:PRK13637 95 QLFEETIEKDIAFGPINL----GLSEEEIENRVKRamnivgldyedykdkspfeLSGGQKRRVAIAGVVAMEPKILILDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505055604 469 PTNHLDLDTKE---MLIKAL-SAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:PRK13637 171 PTAGLDPKGRDeilNKIKELhKEYNMTIILVSHSMEDVAKLADRII 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
443-510 |
7.43e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 51.24 E-value: 7.43e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 443 LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLD-LDTKEML--IKALSAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:PRK13651 166 LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILeiFDNLNKQGKTIILVTHDLDNVLEWTKRTI 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
27-196 |
7.54e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 52.03 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIgyfdQDVGEMAGRSAVAEVMEgagpvsavaaelreletam 106
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLD-GHDL----ADYTLASLRRQVALVSQ------------------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 107 sdpDRMDEMDAIVErygevQARYEELDGYALEgRAREVLAG---LSFSQEMMDG-------DVAKLSGGWKMRVALARIL 176
Cdd:TIGR02203 414 ---DVVLFNDTIAN-----NIAYGRTEQADRA-EIERALAAayaQDFVDKLPLGldtpigeNGVLLSGGQRQRLAIARAL 484
|
170 180
....*....|....*....|
gi 505055604 177 LMRPDAMLLDEPSNHLDLES 196
Cdd:TIGR02203 485 LKDAPILILDEATSALDNES 504
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
284-497 |
8.55e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 51.75 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 284 HASQVQSRVKKLEKIDRVEPprrrqTVAFEFLPAPRSGEDVVNLKSVHKTY--GSRTIYDGLDFMVRRRERWCIMGINGA 361
Cdd:PRK11160 303 HLGQVIASARRINEITEQKP-----EVTFPTTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGC 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 362 GKSTLLKLVTGTTNPDKGSVSLGAsVKLGYFAQHSM-----------DLLDGE-----------------STILQWLEER 413
Cdd:PRK11160 378 GKSTLLQLLTRAWDPQQGEILLNG-QPIADYSEAALrqaisvvsqrvHLFSATlrdnlllaapnasdealIEVLQQVGLE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 414 FPKAGQAPLRALAGCFGfsgddvekrcRVLSGGEKARLVMA-AMLFDPPnFLVLDEPTNHLDLDTkEMLIKAL---SAYQ 489
Cdd:PRK11160 457 KLLEDDKGLNAWLGEGG----------RQLSGGEQRRLGIArALLHDAP-LLLLDEPTEGLDAET-ERQILELlaeHAQN 524
|
....*...
gi 505055604 490 GTMLFVSH 497
Cdd:PRK11160 525 KTVLMITH 532
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-193 |
9.39e-07 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.47 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE------KGMTIGYFDQDVG 74
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDgkpvegPGAERGVVFQNEG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 75 EMAGRSAVAEVmegagpvsAVAAELRELETAmsdpdrmdemdaivERygevqaryeeldgyalEGRAREVLA--GLSFSQ 152
Cdd:PRK11248 81 LLPWRNVQDNV--------AFGLQLAGVEKM--------------QR----------------LEIAHQMLKkvGLEGAE 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 505055604 153 EMMdgdVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK11248 123 KRY---IWQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
357-499 |
1.00e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 357 GINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKLGYFA-QHSMDLLDGESTILQWLEER-------FPKAGQAPLRALAG 427
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFeRQSIKKDLCTyQKQLCFVGHRSGINPYLTLRenclydiHFSPGAVGITELCR 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 428 CFGFsGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQ---GTMLFVSHDR 499
Cdd:PRK13540 114 LFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRakgGAVLLTSHQD 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
324-384 |
1.03e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.21 E-value: 1.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 324 VVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG 384
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-237 |
1.09e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.87 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSnshrilYIEASAALN-------RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQvavekgmtIGYFDQDV 73
Cdd:PRK10908 1 MIRFEHVSKA------YLGGRQALQgvtfhmrPGEMAFLTGHSGAGKSTLLKLICGIERPSAGK--------IWFSGHDI 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 74 GEMAGRsavaEVmegagPVsavaaeLRElETAMSDPDRMDEMDAIVerYGEVqARYEELDGYALEGRAREVLAGLSFSQE 153
Cdd:PRK10908 67 TRLKNR----EV-----PF------LRR-QIGMIFQDHHLLMDRTV--YDNV-AIPLIIAGASGDDIRRRVSAALDKVGL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 154 MmdgDVAK-----LSGGWKMRVALARILLMRPDAMLLDEPSNHLD---LESLIWLENFLKGYDGALLMTSHDREFMNRIV 225
Cdd:PRK10908 128 L---DKAKnfpiqLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGILRLFEEFNRVGVTVLMATHDIGLISRRS 204
|
250
....*....|..
gi 505055604 226 TKIIEIDGGALT 237
Cdd:PRK10908 205 YRMLTLSDGHLH 216
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-61 |
1.14e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.18 E-value: 1.14e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 1 MIRIENISKS------NSHrilyieASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE 61
Cdd:COG3845 5 ALELRGITKRfggvvaNDD------VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILID 65
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
324-510 |
1.18e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 49.71 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGAsvklgyfaqhsMDLLDGE 403
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-----------LKVNDPK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 404 STILQWLEER---------FPKagqapLRALAGCF-------GFSGDDVEKRCRV-----------------LSGGEKAR 450
Cdd:PRK09493 70 VDERLIRQEAgmvfqqfylFPH-----LTALENVMfgplrvrGASKEEAEKQAREllakvglaerahhypseLSGGQQQR 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 451 LVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALS--AYQG-TMLFVSHDRRFLSALSNRVL 510
Cdd:PRK09493 145 VAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQdlAEEGmTMVIVTHEIGFAEKVASRLI 207
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
27-196 |
1.28e-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: 49.85 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMT-----------IGYFDQDvgemagrsavaevmegagPVsAV 95
Cdd:cd03249 29 GKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIrdlnlrwlrsqIGLVSQE------------------PV-LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 96 AAELRElETAMSDPDRMDEMDAIVERYGEVQARYEEL-DGYalegrarEVLAGLSFSQemmdgdvakLSGGWKMRVALAR 174
Cdd:cd03249 90 DGTIAE-NIRYGKPDATDEEVEEAAKKANIHDFIMSLpDGY-------DTLVGERGSQ---------LSGGQKQRIAIAR 152
|
170 180
....*....|....*....|..
gi 505055604 175 ILLMRPDAMLLDEPSNHLDLES 196
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAES 174
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
27-236 |
1.29e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqdvgemAGRSavaevmegagpvsaVAAELRELETAM 106
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATV----------------AGKS--------------ILTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 107 SDPDRMDEMDAIV--ERYGEVQARYEELDGYALEGRAREVLA--GLSFSQEMMDGdvaKLSGGWKMRVALARILLMRPDA 182
Cdd:TIGR01257 2015 GYCPQFDAIDDLLtgREHLYLYARLRGVPAEEIEKVANWSIQslGLSLYADRLAG---TYSGGNKRKLSTAIALIGCPPL 2091
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 183 MLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLWNTIVSIireGRAVVLTSHSMEECEALCTRLAIMVKGAF 2148
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
296-509 |
1.43e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 51.55 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 296 EKIDRVEPPRRRQTVAFEF-LPAPRSGEDVVNLKSVHKTYGsRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTT 374
Cdd:TIGR01257 902 EEMEDPEHPEGINDSFFEReLPGLVPGVCVKNLVKIFEPSG-RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 375 NPDKGSVSLGAS----------VKLGYFAQHSM---DLLDGESTIL-QWLEERFPKAGQAPLRALAGCFGFSGDDVEKrC 440
Cdd:TIGR01257 981 PPTSGTVLVGGKdietnldavrQSLGMCPQHNIlfhHLTVAEHILFyAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEE-A 1059
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 441 RVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG--TMLFVSHDRRFLSALSNRV 509
Cdd:TIGR01257 1060 QDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrTIIMSTHHMDEADLLGDRI 1130
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
337-510 |
1.59e-06 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 49.37 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 337 RTIYDGL----DFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVkLGY----------FAQH------ 395
Cdd:COG3840 8 TYRYGDFplrfDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWnGQDL-TALppaerpvsmlFQENnlfphl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 ------------SMDLLDGESTILQWLEERFpkagqaplrALAGCfgfsgddVEKRCRVLSGGEKARLVMAAMLFDPPNF 463
Cdd:COG3840 87 tvaqniglglrpGLKLTAEQRAQVEQALERV---------GLAGL-------LDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 464 LVLDEPTNHLDLDTK-EM--LIKALSA-YQGTMLFVSHDRRFLSALSNRVL 510
Cdd:COG3840 151 LLLDEPFSALDPALRqEMldLVDELCReRGLTVLMVTHDPEDAARIADRVL 201
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
328-485 |
1.63e-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: 49.15 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 328 KSVHKTYGS-RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSlgasvklgyfaqhsMDLLDGESTI 406
Cdd:cd03254 6 ENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQIL--------------IDGIDIRDIS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 LQWLEERFPKAGQAPlralagcFGFSG---------------DDVEKRCRV------------------------LSGGE 447
Cdd:cd03254 72 RKSLRSMIGVVLQDT-------FLFSGtimenirlgrpnatdEEVIEAAKEagahdfimklpngydtvlgenggnLSQGE 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 505055604 448 KARLVMA-AMLFDPPnFLVLDEPTNHLDLDTKEMLIKAL 485
Cdd:cd03254 145 RQLLAIArAMLRDPK-ILILDEATSNIDTETEKLIQEAL 182
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-203 |
1.65e-06 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 49.49 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGqvavekgmTIGYFDQDVGEMAG-- 78
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSG--------RIVFDGKDITDWQTak 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 --RSAVAEVMEGAGPVSAVAAElreletamsDPDRMDEMDAIVERYGEVQARYEELDGYALEGRAREvlAGlsfsqemmd 156
Cdd:PRK11614 77 imREAVAIVPEGRRVFSRMTVE---------ENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQR--AG--------- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 505055604 157 gdvaKLSGGWKMRVALARILLMRPDAMLLDEPSnhLDLESLIWLENF 203
Cdd:PRK11614 137 ----TMSGGEQQMLAIGRALMSQPRLLLLDEPS--LGLAPIIIQQIF 177
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
442-497 |
1.69e-06 |
|
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: 50.90 E-value: 1.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 442 VLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQGTMLFVSH 497
Cdd:TIGR00954 582 VLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
327-384 |
1.84e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 49.31 E-value: 1.84e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG 384
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVD 61
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
443-522 |
1.91e-06 |
|
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: 48.09 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 443 LSGGEKARLVMAAMLF--DPPNFLVLDEPTNHLDLDTKEML---IKALSAYQGTMLFVSHDRRFLSaLSNRVLELTPdGI 517
Cdd:cd03238 88 LSGGELQRVKLASELFsePPGTLFILDEPSTGLHQQDINQLlevIKGLIDLGNTVILIEHNLDVLS-SADWIIDFGP-GS 165
|
....*
gi 505055604 518 NQYGG 522
Cdd:cd03238 166 GKSGG 170
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
355-485 |
1.91e-06 |
|
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: 48.39 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTG--TTNPDKGSVSLGASVKLGYFAQHS-----MDLLDGESTILQWLEerfpkagqaplralag 427
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRSTgyveqQDVHSPNLTVREALR---------------- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 428 cfgFSGDdvekrCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKAL 485
Cdd:cd03232 102 ---FSAL-----LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFL 151
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
162-216 |
2.39e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.87 E-value: 2.39e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLDL----ESLIWLENFLKGYDGALLMTSH 216
Cdd:PRK11144 129 LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLprkrELLPYLERLAREINIPILYVSH 187
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
341-512 |
2.79e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 49.06 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV--------------KLGYFAQHSMDLLdGEST 405
Cdd:PRK13641 24 DNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIaGYHItpetgnknlkklrkKVSLVFQFPEAQL-FENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 406 ILQWLE---ERF----PKAGQAPLRALAGCfGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK 478
Cdd:PRK13641 103 VLKDVEfgpKNFgfseDEAKEKALKWLKKV-GLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 505055604 479 EMLIKALSAYQG---TMLFVSHDRRFLSALSNRVLEL 512
Cdd:PRK13641 182 KEMMQLFKDYQKaghTVILVTHNMDDVAEYADDVLVL 218
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
27-216 |
2.82e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.11 E-value: 2.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQdvgeMAGRSAVAEVmeGAGPVsAVAAELRELETAM 106
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD-GVPLVQYDH----HYLHRQVALV--GQEPV-LFSGSVRENIAYG 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 107 SDPDRMDEMDAIVERYGEVQARYEELDGYALEgrarevlAGLSFSQemmdgdvakLSGGWKMRVALARILLMRPDAMLLD 186
Cdd:TIGR00958 579 LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTE-------VGEKGSQ---------LSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190
....*....|....*....|....*....|
gi 505055604 187 EPSNHLDLESLIWLENFLKGYDGALLMTSH 216
Cdd:TIGR00958 643 EATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-217 |
2.90e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.78 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQeLPDEGQVAVEkgmtigyfDQDVGEMAGRS-AV--AEVMEGAGPVSAVAA 97
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFA--------GQPLEAWSAAElARhrAYLSQQQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 98 eLRELetAMSDPDRMDEmdaiverygevqaryeeldgYALEGRAREVLAGLSFsQEMMDGDVAKLSGG-WKmRVALARIL 176
Cdd:PRK03695 87 -FQYL--TLHQPDKTRT--------------------EAVASALNEVAEALGL-DDKLGRSVNQLSGGeWQ-RVRLAAVV 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 177 L-----MRPDA--MLLDEPSNHLDLESLIWLENFLK---GYDGALLMTSHD 217
Cdd:PRK03695 142 LqvwpdINPAGqlLLLDEPMNSLDVAQQAALDRLLSelcQQGIAVVMSSHD 192
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-206 |
3.00e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 16 LYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMT------------IGYFDQD----------- 72
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlkdinlkwwrskIGVVSQDpllfsnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 73 ----VGEMAGRSAVAEVMEGAGPVSAVAAELRELETAMSDPDrMDEMDAIVERYGEVQAR--YEELDGYALEGRAREVL- 145
Cdd:PTZ00265 480 ikysLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGD-LNDMSNTTDSNELIEMRknYQTIKDSEVVDVSKKVLi 558
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 146 ----AGLSFSQEMMDG-DVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLE---NFLKG 206
Cdd:PTZ00265 559 hdfvSALPDKYETLVGsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQktiNNLKG 627
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-223 |
3.07e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.02 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQvavekgmtIGYFDQDVGEmaGRS 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGE--------ILFERQSIKK--DLC 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEVMEGAGPVSAVAAELRELETAMSDPDRMDEMDAIVErygevqaryeeldgyalegrarevLAGLSFSQEMMDGDVA 160
Cdd:PRK13540 71 TYQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITE------------------------LCRLFSLEHLIDYPCG 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHDREFMNR 223
Cdd:PRK13540 127 LLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHrakGGAVLLTSHQDLPLNK 192
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-194 |
3.57e-06 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 48.47 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGRS 80
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLG--------DKPISMLSSRQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 ---AVAEVmegagPVSAVAAE---LRELETAMSDP-----DRMDEMD-AIVERygevqaryeeldgyALEGRAREVLAgl 148
Cdd:PRK11231 74 larRLALL-----PQHHLTPEgitVRELVAYGRSPwlslwGRLSAEDnARVNQ--------------AMEQTRINHLA-- 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505055604 149 sfsqemmDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL 194
Cdd:PRK11231 133 -------DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
320-381 |
4.37e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 48.61 E-value: 4.37e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 320 SGEDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSV 381
Cdd:PRK11831 3 SVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
349-517 |
5.14e-06 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 46.60 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 349 RRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSlgasvklgyfaqhsmdLLDGESTILQWLEERfpkagqaplralagc 428
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI----------------YIDGEDILEEVLDQL--------------- 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 429 fgfSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQGTMLFVSHDRRFLsALSNR 508
Cdd:smart00382 50 ---LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVI-LTTND 125
|
....*....
gi 505055604 509 VLELTPDGI 517
Cdd:smart00382 126 EKDLGPALL 134
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-83 |
5.37e-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: 46.80 E-value: 5.37e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDV----GEMAgRSAVA 83
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-GITPVYKPQYIdlsgGELQ-RVAIA 83
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
341-510 |
5.64e-06 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 48.91 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTL----LKLVtgttnPDKGSVslgasvklgYFAQHSMDLLDGES------------ 404
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEI---------RFDGQDLDGLSRRAlrplrrrmqvvf 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 -----------TILQWLEErfpkagqaPLRALAGcfGFSGDDVEKR-CRVL-----------------SGGEKARLVMA- 454
Cdd:COG4172 369 qdpfgslsprmTVGQIIAE--------GLRVHGP--GLSAAERRARvAEALeevgldpaarhryphefSGGQRQRIAIAr 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505055604 455 AMLFDPpNFLVLDEPTNHLD-------LDtkemLIKALSA-YQGTMLFVSHDRRFLSALSNRVL 510
Cdd:COG4172 439 ALILEP-KLLVLDEPTSALDvsvqaqiLD----LLRDLQReHGLAYLFISHDLAVVRALAHRVM 497
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
322-383 |
5.76e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 49.01 E-value: 5.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 322 EDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL 383
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI 64
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
341-498 |
6.03e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.06 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV----------KLGYFAQHSMDLLDG---ESTI 406
Cdd:PRK13632 26 KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITIskenlkeirkKIGIIFQNPDNQFIGatvEDDI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 LQWLEERF--PKAGQAPLRALAGCFGFsGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKA 484
Cdd:PRK13632 106 AFGLENKKvpPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKI 184
|
170
....*....|....*...
gi 505055604 485 LSAYQG----TMLFVSHD 498
Cdd:PRK13632 185 MVDLRKtrkkTLISITHD 202
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-193 |
6.16e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 48.00 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtigyFDQDVGEMAGRS 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH---------YRMRDGQLRDLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AVAEvmegagpvsavaAELREL--------ETAMSDPDRMdEMDA---IVERYGEVQARYeeldgYaleGRAREV----L 145
Cdd:PRK11701 77 ALSE------------AERRRLlrtewgfvHQHPRDGLRM-QVSAggnIGERLMAVGARH-----Y---GDIRATagdwL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505055604 146 AGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK11701 136 ERVEIDAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
161-512 |
6.38e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.93 E-value: 6.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 161 KLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL----ESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRC 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 237 TtysgdygfydEQRALNARQQQAQFERQQAMLAKEikfierfkaRASHASQVQSRVKKLEKIDRVEpprrrqtVAFEFlp 316
Cdd:PRK15134 236 V----------EQNRAATLFSAPTHPYTQKLLNSE---------PSGDPVPLPEPASPLLDVEQLQ-------VAFPI-- 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 317 apRSGedvvnlkSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKST----LLKLVtgttnPDKGSVSLGASvKLGYF 392
Cdd:PRK15134 288 --RKG-------ILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQ-PLHNL 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 393 AQHSM---------------DLLDGESTILQWLEE------RFPKAGQAPLRALAgCFGFSGDDVEKRCRV---LSGGEK 448
Cdd:PRK15134 353 NRRQLlpvrhriqvvfqdpnSSLNPRLNVLQIIEEglrvhqPTLSAAQREQQVIA-VMEEVGLDPETRHRYpaeFSGGQR 431
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 449 ARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEM---LIKALSA-YQGTMLFVSHDRRFLSALSNRVLEL 512
Cdd:PRK15134 432 QRIAIARALILKPSLIILDEPTSSLDKTVQAQilaLLKSLQQkHQLAYLFISHDLHVVRALCHQVIVL 499
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
324-510 |
6.40e-06 |
|
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: 48.13 E-value: 6.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 324 VVNLKSVHKTYGSRTIY----DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNP---DKGSVS------LGASVK-- 388
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILfdgedlLKLSEKel 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 389 -------LGYFAQHSMDLLDGESTILQWLEErfpkagqaPLRALagcFGFSGDDVEKRC-----RV-------------- 442
Cdd:COG0444 81 rkirgreIQMIFQDPMTSLNPVMTVGDQIAE--------PLRIH---GGLSKAEARERAielleRVglpdperrldryph 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505055604 443 -LSGGEKARLVMA-AMLFDPpNFLVLDEPTNHLD-------LDtkemLIKALSAYQG-TMLFVSHDRRFLSALSNRVL 510
Cdd:COG0444 150 eLSGGMRQRVMIArALALEP-KLLIADEPTTALDvtiqaqiLN----LLKDLQRELGlAILFITHDLGVVAEIADRVA 222
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
325-497 |
6.45e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.82 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDG-----LDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV------------ 387
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLitstsknkdikq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 388 ---KLGYFAQHSMDLLdGESTILQ---WLEERF---PKAGQAPLRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLF 458
Cdd:PRK13649 83 irkKVGLVFQFPESQL-FEETVLKdvaFGPQNFgvsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505055604 459 DPPNFLVLDEPTNHLD-LDTKEM--LIKALSAYQGTMLFVSH 497
Cdd:PRK13649 162 MEPKILVLDEPTAGLDpKGRKELmtLFKKLHQSGMTIVLVTH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
24-193 |
7.89e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 48.10 E-value: 7.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAV-EKGMtigyfdQDVgEMAGRsavaevmeGAGPVSAVAAELREL 102
Cdd:PRK11000 26 IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgEKRM------NDV-PPAER--------GVGMVFQSYALYPHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 103 ETAmsdpdrmDEMD-----AIVERyGEVQARYEEldgyalegrAREVLAgLSfsqEMMDGDVAKLSGGWKMRVALARILL 177
Cdd:PRK11000 91 SVA-------ENMSfglklAGAKK-EEINQRVNQ---------VAEVLQ-LA---HLLDRKPKALSGGQRQRVAIGRTLV 149
|
170
....*....|....*.
gi 505055604 178 MRPDAMLLDEPSNHLD 193
Cdd:PRK11000 150 AEPSVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
320-498 |
8.14e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 47.87 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 320 SGEDVVNLKSVHKTY--GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVS----LGASVklgyfa 393
Cdd:PRK13640 1 MKDNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitvDGITL------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 394 qhsmdlldGESTIlqW-LEERFPKAGQAPLRALAGcfGFSGDDV----EKRC-----------RV--------------- 442
Cdd:PRK13640 75 --------TAKTV--WdIREKVGIVFQNPDNQFVG--ATVGDDVafglENRAvprpemikivrDVladvgmldyidsepa 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 443 -LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG----TMLFVSHD 498
Cdd:PRK13640 143 nLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknnlTVISITHD 203
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
355-498 |
9.05e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.47 E-value: 9.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDKGSVSLG----ASVKLGYFAQHsmdlldgestiLQWLEERFPKA-----------GQ 419
Cdd:PRK10575 42 LIGHNGSGKSTLLKMLGRHQPPSEGEILLDaqplESWSSKAFARK-----------VAYLPQQLPAAegmtvrelvaiGR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 420 APLRALAGCFGfsgddVEKRCRV-------------------LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKE- 479
Cdd:PRK10575 111 YPWHGALGRFG-----AADREKVeeaislvglkplahrlvdsLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVd 185
|
170 180
....*....|....*....|..
gi 505055604 480 --MLIKALSAYQG-TMLFVSHD 498
Cdd:PRK10575 186 vlALVHRLSQERGlTVIAVLHD 207
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
443-524 |
9.15e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.67 E-value: 9.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 443 LSGGEKARLVMAAMLFDP---PNFLVLDEPTNHLDLDTKEMLIKALSA--YQG-TMLFVSHDRRFLSaLSNRVLELTPDG 516
Cdd:PRK00635 810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSltHQGhTVVIIEHNMHVVK-VADYVLELGPEG 888
|
....*...
gi 505055604 517 INQygGGY 524
Cdd:PRK00635 889 GNL--GGY 894
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-193 |
1.01e-05 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 47.16 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENIS----KSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQV-----AVEK-GMTIGYFD 70
Cdd:COG4525 3 MLTVRHVSvrypGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEItldgvPVTGpGADRGVVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 71 QDVGEMAGRSAVAEVmegagpvsAVAAELRELETAmsdpdrmdemdaivERygevqaryeeldgyalEGRAREVLA--GL 148
Cdd:COG4525 83 QKDALLPWLNVLDNV--------AFGLRLRGVPKA--------------ER----------------RARAEELLAlvGL 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505055604 149 sfsQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG4525 125 ---ADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-193 |
1.02e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.14 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 32 LVGPNGAGKTTLFRMIT-----GQELPDEGQVAVeKGMTIgyFDQDVGEMAGRSAVAEVMEGAGPVS--------AVAAE 98
Cdd:PRK14267 35 LMGPSGCGKSTLLRTFNrllelNEEARVEGEVRL-FGRNI--YSPDVDPIEVRREVGMVFQYPNPFPhltiydnvAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 99 LRELETAMsdpdrmDEMDAIVERYGEVQARYEELdgyalegrarevlaglsfsQEMMDGDVAKLSGGWKMRVALARILLM 178
Cdd:PRK14267 112 LNGLVKSK------KELDERVEWALKKAALWDEV-------------------KDRLNDYPSNLSGGQRQRLVIARALAM 166
|
170
....*....|....*
gi 505055604 179 RPDAMLLDEPSNHLD 193
Cdd:PRK14267 167 KPKILLMDEPTANID 181
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
336-498 |
1.06e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 336 SRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTG--TTNPDKGSVSLGASVKLGYFAQHSMD---LLDGESTILQWL 410
Cdd:PRK13547 13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTGDVTLNGEPLAAIDaprLARLRAVLPQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 411 EERFP----------------KAGQAPLR---------ALAGCFGFSGDDVEkrcrVLSGGEKARLVMAAMLFD------ 459
Cdd:PRK13547 93 QPAFAfsareivllgrypharRAGALTHRdgeiawqalALAGATALVGRDVT----TLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505055604 460 ---PPNFLVLDEPTNHLDLDTKEMLIKALSA----YQGTMLFVSHD 498
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRlardWNLGVLAIVHD 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
138-193 |
1.16e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.32 E-value: 1.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 138 EGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK13634 122 KQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
336-488 |
1.19e-05 |
|
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: 46.50 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 336 SRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDK---GSVSL-GASVKLGYFAQH------SMDLLDG--- 402
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFnGQPRKPDQFQKCvayvrqDDILLPGltv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 -ES---TILQWLEERFPKAGQAPLRAlagcfgfsgDDVEKRC----------RVLSGGEKARLVMAAMLFDPPNFLVLDE 468
Cdd:cd03234 99 rETltyTAILRLPRKSSDAIRKKRVE---------DVLLRDLaltriggnlvKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180
....*....|....*....|
gi 505055604 469 PTNHLDLDTKEMLIKALSAY 488
Cdd:cd03234 170 PTSGLDSFTALNLVSTLSQL 189
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
355-485 |
1.20e-05 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 48.12 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDkgsVSLGASVKL--------------GYFAQHsmDLLDGESTILQWL--------EE 412
Cdd:TIGR00955 56 VMGSSGAGKTTLMNALAFRSPKG---VKGSGSVLLngmpidakemraisAYVQQD--DLFIPTLTVREHLmfqahlrmPR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 413 RFPKAG-----QAPLRA--LAGC----FGfsgddVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML 481
Cdd:TIGR00955 131 RVTKKEkrervDEVLQAlgLRKCantrIG-----VPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
....
gi 505055604 482 IKAL 485
Cdd:TIGR00955 206 VQVL 209
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
325-498 |
1.20e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.08 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIY-----DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG--------------- 384
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYehqaiHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithktkdkyirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 385 ASVKLGYFAQHSmdlldgESTILQWLEER---F-PKAGQAPL-----RA--LAGCFGFSGDDVEKRCRVLSGGEKARLVM 453
Cdd:PRK13646 83 VRKRIGMVFQFP------ESQLFEDTVEReiiFgPKNFKMNLdevknYAhrLLMDLGFSRDVMSQSPFQMSGGQMRKIAI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 505055604 454 AAMLFDPPNFLVLDEPTNHLDLDTKEM---LIKALSAYQG-TMLFVSHD 498
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQvmrLLKSLQTDENkTIILVSHD 205
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
3-194 |
1.20e-05 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 47.09 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 3 RIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGRSAV 82
Cdd:PRK10575 13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLD--------AQPLESWSSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 83 AEVmeGAGPVSAVAAE---LRELETAMSDPdrmdeMDAIVERYG-EVQARYEEldgyALEgrarevLAGLS-FSQEMMDg 157
Cdd:PRK10575 85 RKV--AYLPQQLPAAEgmtVRELVAIGRYP-----WHGALGRFGaADREKVEE----AIS------LVGLKpLAHRLVD- 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 505055604 158 dvaKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL 194
Cdd:PRK10575 147 ---SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDI 180
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-194 |
1.29e-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: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVavekgmtigyfdQDVGEMAGRSAVAEVMEGAgpvsavaaeLR 100
Cdd:TIGR01271 446 SFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------------KHSGRISFSPQTSWIMPGT---------IK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 E-LETAMSdpdrMDEMdaiveRYGEV-QARYEELDGYALEGRAREVLaglsfsqemMDGDVAkLSGGWKMRVALARILLM 178
Cdd:TIGR01271 505 DnIIFGLS----YDEY-----RYTSViKACQLEEDIALFPEKDKTVL---------GEGGIT-LSGGQRARISLARAVYK 565
|
170
....*....|....*.
gi 505055604 179 RPDAMLLDEPSNHLDL 194
Cdd:TIGR01271 566 DADLYLLDSPFTHLDV 581
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
27-193 |
1.44e-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: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAvekgmtIGyfDQDVGEM--AGRS--------------AVAEVMegag 90
Cdd:PRK11650 30 GEFIVLVGPSGCGKSTLLRMVAGLERITSGEIW------IG--GRVVNELepADRDiamvfqnyalyphmSVRENM---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 91 pvsAVAAELReletamsdpdRMDEmDAIVERYGEVqARYEELDGYaLEGRAREvlaglsfsqemmdgdvakLSGGWKMRV 170
Cdd:PRK11650 98 ---AYGLKIR----------GMPK-AEIEERVAEA-ARILELEPL-LDRKPRE------------------LSGGQRQRV 143
|
170 180
....*....|....*....|...
gi 505055604 171 ALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK11650 144 AMGRAIVREPAVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-205 |
1.48e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 46.67 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIgyfDQDVGEMagRSAVAEVMEGagPVSAVAAELRELETA 105
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKL--RKHIGIVFQN--PDNQFVGSIVKYDVA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 106 MSDPDRMDEMDAIVERYGEVQARYEELDgYAlegrarevlaglsfsqemmDGDVAKLSGGWKMRVALARILLMRPDAMLL 185
Cdd:PRK13648 107 FGLENHAVPYDEMHRRVSEALKQVDMLE-RA-------------------DYEPNALSGGQKQRVAIAGVLALNPSVIIL 166
|
170 180
....*....|....*....|...
gi 505055604 186 DEPSNHLD---LESLIWLENFLK 205
Cdd:PRK13648 167 DEATSMLDpdaRQNLLDLVRKVK 189
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-61 |
1.54e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 47.71 E-value: 1.54e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 1 MIRIENISKS--------NshrilyieASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE 61
Cdd:COG1129 4 LLEMRGISKSfggvkaldG--------VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLD 64
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
341-384 |
1.88e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.21 E-value: 1.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG 384
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILID 64
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-194 |
2.15e-05 |
|
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: 47.13 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENIS---KSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQElpdEGQVAVEKGMTIGYFDQDVGEMA 77
Cdd:TIGR02633 257 ILEARNLTcwdVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY---PGKFEGNVFINGKPVDIRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 78 GRSAVAEVME-----GAGPVSAVAAELREletamsdpdrmdemdAIVERYgevqARYEELDGYALEGRAREVLAGLSFSQ 152
Cdd:TIGR02633 334 IRAGIAMVPEdrkrhGIVPILGVGKNITL---------------SVLKSF----CFKMRIDAAAELQIIGSAIQRLKVKT 394
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 505055604 153 EMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDL 194
Cdd:TIGR02633 395 ASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-193 |
2.16e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.92 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 4 IENISKSNSHRIlyieaSAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQDvGEMAGRSAVA 83
Cdd:PRK10762 260 VDNLSGPGVNDV-----SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQD-GLANGIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 84 EVMEGAGpvsavaaelreLETAMSDPDRMD--EMDAIVERYGEVQaryeeldgyalegRAREVLAGLSFSQEM------M 155
Cdd:PRK10762 334 EDRKRDG-----------LVLGMSVKENMSltALRYFSRAGGSLK-------------HADEQQAVSDFIRLFniktpsM 389
|
170 180 190
....*....|....*....|....*....|....*...
gi 505055604 156 DGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:PRK10762 390 EQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
355-524 |
2.23e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.11 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVK--LGYFAQHSM-----DLLDGESTILQWLE--ERFPKAGQAPLRAL 425
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDevLKRFRGTELqnyfkKLYNGEIKVVHKPQyvDLIPKVFKGKVREL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 426 ------AGCFgfsgDDV----------EKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLD---TKEMLIKALS 486
Cdd:PRK13409 184 lkkvdeRGKL----DEVverlglenilDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRqrlNVARLIRELA 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 505055604 487 AYQgTMLFVSHDRRFLSALSNRVLEL---------------TPDGINQYGGGY 524
Cdd:PRK13409 260 EGK-YVLVVEHDLAVLDYLADNVHIAygepgaygvvskpkgVRVGINEYLKGY 311
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
355-524 |
2.29e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.21 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVK--LGYFAQHSM-----DLLDGESTIL---QWLEeRFPKAGQAPLRA 424
Cdd:cd03236 31 LVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDeiLDEFRGSELqnyftKLLEGDVKVIvkpQYVD-LIPKAVKGKVGE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 425 LAGCFGFSG--DDVEKRCRV----------LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLD---TKEMLIKALSAYQ 489
Cdd:cd03236 110 LLKKKDERGklDELVDQLELrhvldrnidqLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKqrlNAARLIRELAEDD 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 490 GTMLFVSHDRRFLSALSNRVLEL---------------TPDGINQYGGGY 524
Cdd:cd03236 190 NYVLVVEHDLAVLDYLSDYIHCLygepgaygvvtlpksVREGINEFLDGY 239
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
343-521 |
2.47e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.81 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 343 LDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVKLGYFAQHSMDLLDG-ESTILQWLEERFPKAGQAP 421
Cdd:PRK13545 43 ISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGiENIELKGLMMGLTKEKIKE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 422 LRALAGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAY--QG-TMLFVSHD 498
Cdd:PRK13545 123 IIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFkeQGkTIFFISHS 202
|
170 180
....*....|....*....|...
gi 505055604 499 RRFLSALSNRVLELTPDGINQYG 521
Cdd:PRK13545 203 LSQVKSFCTKALWLHYGQVKEYG 225
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
21-193 |
2.75e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfdqdvgemaGRSAVAEvmegagpvsAVAAELR 100
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKID----------------GELLTAE---------NVWNLRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 ELETAMSDPDRmDEMDAIVERYGEVQARYEELDGYALEGRAREVLAGLSfsqeMMD---GDVAKLSGGWKMRVALARILL 177
Cdd:PRK13642 82 KIGMVFQNPDN-QFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVN----MLDfktREPARLSGGQKQRVAVAGIIA 156
|
170
....*....|....*.
gi 505055604 178 MRPDAMLLDEPSNHLD 193
Cdd:PRK13642 157 LRPEIIILDESTSMLD 172
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
322-521 |
3.09e-05 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 45.78 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTY--GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVklgyfaqhsmdl 399
Cdd:PRK13635 3 EEIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV------------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 400 LDgESTIlqWLEERfpKAG---QAPLRALAG-------CFGFSG-----DDVEKRC-----RV------------LSGGE 447
Cdd:PRK13635 71 LS-EETV--WDVRR--QVGmvfQNPDNQFVGatvqddvAFGLENigvprEEMVERVdqalrQVgmedflnrephrLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 448 KARLVMAAMLFDPPNFLVLDEPTNHLD-------LDTkemlIKALSAYQG-TMLFVSHDrrfL--SALSNRVL------- 510
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDprgrrevLET----VRQLKEQKGiTVLSITHD---LdeAAQADRVIvmnkgei 218
|
250
....*....|...
gi 505055604 511 --ELTPDGINQYG 521
Cdd:PRK13635 219 leEGTPEEIFKSG 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-217 |
3.66e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 45.59 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVeKGMTIGYFDQDVGEMAGRSAVAEVMEGAgpvsavAAELR 100
Cdd:PRK13641 27 SFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITI-AGYHITPETGNKNLKKLRKKVSLVFQFP------EAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 ElETAMSDpdrmdemdaiVErYGEVQARYEELDGyalEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRP 180
Cdd:PRK13641 100 E-NTVLKD----------VE-FGPKNFGFSEDEA---KEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505055604 181 DAMLLDEPSNHLDLESLIWLENFLKGYDGA---LLMTSHD 217
Cdd:PRK13641 165 EILCLDEPAAGLDPEGRKEMMQLFKDYQKAghtVILVTHN 204
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
355-524 |
4.19e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 46.32 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVK--LGYFA-----QHSMDLLDGESTI---LQWLEeRFPKAGQAPLRA 424
Cdd:COG1245 104 ILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDevLKRFRgtelqDYFKKLANGEIKVahkPQYVD-LIPKVFKGTVRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 425 L---AGCFGFSGDDVEK---------RCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLdtKEML-----IKALSA 487
Cdd:COG1245 183 LlekVDERGKLDELAEKlglenildrDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI--YQRLnvarlIRELAE 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505055604 488 YQGTMLFVSHDRRFLSALSNRVLEL---------------TPDGINQYGGGY 524
Cdd:COG1245 261 EGKYVLVVEHDLAILDYLADYVHILygepgvygvvskpksVRVGINQYLDGY 312
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
332-496 |
4.27e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 46.41 E-value: 4.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 332 KTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLV---------TGTTNPDKGSVSLGASVKLGYFAQHsmDLLDG 402
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALagriqgnnfTGTILANNRKPTKQILKRTGFVTQD--DILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 403 ESTILQWLE----ERFPKAGQAPLRALAGCFGFSGDDVEKrC----------RVLSGGEKARLVMAAMLFDPPNFLVLDE 468
Cdd:PLN03211 154 HLTVRETLVfcslLRLPKSLTKQEKILVAESVISELGLTK-CentiignsfiRGISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|
gi 505055604 469 PTNHLDLDTKEMLIKALS--AYQGTMLFVS 496
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGslAQKGKTIVTS 262
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
315-509 |
4.42e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.42 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 315 LPAPRSGEDVVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGAsvKLGYFAQ 394
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 395 HSMDL----LDGESTILQWLEERFP------------------------KAGQAPLRALaGCFGFSGDDVEKRCRVLSGG 446
Cdd:PRK14246 79 DIFQIdaikLRKEVGMVFQQPNPFPhlsiydniayplkshgikekreikKIVEECLRKV-GLWKEVYDRLNSPASQLSGG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 447 EKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG--TMLFVSHDRRFLSALSNRV 509
Cdd:PRK14246 158 QQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYV 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-236 |
4.46e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.42 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 31 GLVGPNGAGKTTLFRMITGQELPDEGQVAVEKgmTIGYFDQDVGEMAG---RSAVAEVMEGAGPVSAVAAelreletams 107
Cdd:PRK14246 40 GIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQIDAiklRKEVGMVFQQPNPFPHLSI---------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 108 dpdrMDEMDAIVERYGEVQARyeeldgyALEGRAREVLAGLSFSQEMMD---GDVAKLSGGWKMRVALARILLMRPDAML 184
Cdd:PRK14246 108 ----YDNIAYPLKSHGIKEKR-------EIKKIVEECLRKVGLWKEVYDrlnSPASQLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 505055604 185 LDEPSNHLDLESLIWLENFLKGYDG--ALLMTSHDREFMNRIVTKIIEIDGGAL 236
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-193 |
4.57e-05 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 44.70 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGRSAVAEVMEGAgpvsavaaelr 100
Cdd:PRK10247 27 SFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFE--------GEDISTLKPEIYRQQVSYCA----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 elETAMSDPDRMdeMDAIVERYgevQARYEELDgyalEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRP 180
Cdd:PRK10247 88 --QTPTLFGDTV--YDNLIFPW---QIRNQQPD----PAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170
....*....|...
gi 505055604 181 DAMLLDEPSNHLD 193
Cdd:PRK10247 157 KVLLLDEITSALD 169
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
21-241 |
4.81e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 46.26 E-value: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfDQDVGEMAGrsavaevmegagpvSAVAAELR 100
Cdd:PRK10535 28 SLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVA--------GQDVATLDA--------------DALAQLRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 EletamsdpdrmdEMDAIVERYG-----------EVQARYEELDGYALEGRAREVLAGLSFSqEMMDGDVAKLSGGWKMR 169
Cdd:PRK10535 86 E------------HFGFIFQRYHllshltaaqnvEVPAVYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 170 VALARILLMRPDAMLLDEPSNHLDLESLIWLENFLK-----GYdgALLMTSHDREFMNRiVTKIIEIDGGALTTYSG 241
Cdd:PRK10535 153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHqlrdrGH--TVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPP 226
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
30-217 |
4.92e-05 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 44.62 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 30 IGLVGPNGAGKTTLFRMIT---------GQELPDEgqvAVEKGMTIGYFDQDVgEMAGRSAVAEVMEGagpvsavaaELR 100
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRyalygkarsRSKLRSD---LINVGSEEASVELEF-EHGGKRYRIERRQG---------EFA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 101 ELETAmSDPDRMDEMDAI--VERYGEVQARYEELDGyALEGRAREV-----LAGLSFSQEMMDGDVAKLSGGWKMRVALA 173
Cdd:COG0419 93 EFLEA-KPSERKEALKRLlgLEIYEELKERLKELEE-ALESALEELaelqkLKQEILAQLSGLDPIETLSGGERLRLALA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 505055604 174 RILlmrpdAMLLDEPsnHLDLESLIWLENFLKgydgALLMTSHD 217
Cdd:COG0419 171 DLL-----SLILDFG--SLDEERLERLLDALE----ELAIITHV 203
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-518 |
4.94e-05 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 45.97 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQElPD---EGQVavekgmtigYFDqdvGEMAGRSAVAEVmEGAGpVSAVAAEL- 99
Cdd:TIGR02633 24 VRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEI---------YWS---GSPLKASNIRDT-ERAG-IVIIHQELt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 100 --RELETAMSdpdrmdemdaiVERYGEVQARYEELDGYALEGRAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILL 177
Cdd:TIGR02633 89 lvPELSVAEN-----------IFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 178 MRPDAMLLDEPSNHL---DLESLIWLENFLKGYDGALLMTSHDREFMNRIVTKIIEIDGGalttysgdygfydEQRALNA 254
Cdd:TIGR02633 158 KQARLLILDEPSSSLtekETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG-------------QHVATKD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 255 RQQQAQFERQQAMLAKEIKFIErfkarashasqvqsrvkklekidrvepPRRRQTVAFEFLpaprsgeDVVNLKSVHKTY 334
Cdd:TIGR02633 225 MSTMSEDDIITMMVGREITSLY---------------------------PHEPHEIGDVIL-------EARNLTCWDVIN 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 335 GSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTnPDK--GSVSL-GASVKLGYFAQ---------------HS 396
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY-PGKfeGNVFInGKPVDIRNPAQairagiamvpedrkrHG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 397 M--DLLDGESTILQWLEeRFPKAGQAPLRALAGCFGFSgddvEKRCRV-----------LSGGEKARLVMAAMLFDPPNF 463
Cdd:TIGR02633 350 IvpILGVGKNITLSVLK-SFCFKMRIDAAAELQIIGSA----IQRLKVktaspflpigrLSGGNQQKAVLAKMLLTNPRV 424
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 464 LVLDEPTNHLDLDTKE---MLIKALSAYQGTMLFVSHDRRFLSALSNRVL-----ELTPDGIN 518
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYeiyKLINQLAQEGVAIIVVSSELAEVLGLSDRVLvigegKLKGDFVN 487
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-224 |
5.00e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 45.03 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITG-QELpdEGQVAVEKgmTIGYFDQDVGEMAG-- 78
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRmNEL--ESEVRVEG--RVEFFNQNIYERRVnl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 79 ---RSAVAEVMEGAG--PVSAVAAELRELETAMSDPDRmdEMDAIVERYGEVQARYEELdgyalegrarevlaglsfsQE 153
Cdd:PRK14258 84 nrlRRQVSMVHPKPNlfPMSVYDNVAYGVKIVGWRPKL--EIDDIVESALKDADLWDEI-------------------KH 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505055604 154 MMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD------LESLIwlENFLKGYDGALLMTSHDREFMNRI 224
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESLI--QSLRLRSELTMVIVSHNLHQVSRL 217
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
342-503 |
5.12e-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: 44.38 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 342 GLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVklGYFAQ----HSMDLLDgesTIL---QWLEERF 414
Cdd:cd03250 23 DINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI--AYVSQepwiQNGTIRE---NILfgkPFDEERY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 415 PKAGQA-----PLRALAGcfgfsGDDVE--KRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK----EMLIK 483
Cdd:cd03250 98 EKVIKAcalepDLEILPD-----GDLTEigEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGrhifENCIL 172
|
170 180
....*....|....*....|
gi 505055604 484 ALSAYQGTMLFVSHDRRFLS 503
Cdd:cd03250 173 GLLLNNKTRILVTHQLQLLP 192
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
27-193 |
5.53e-05 |
|
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: 45.97 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTT----LFR---------MITGQELPDEGQVAVEK--GM----------TIGYfdqdvgEMA-GRS 80
Cdd:COG5265 384 GKTVAIVGPSGAGKSTlarlLFRfydvtsgriLIDGQDIRDVTQASLRAaiGIvpqdtvlfndTIAY------NIAyGRP 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 81 AV--AEVMEgagpvsavAAELRELET-AMSDPDRMDEMdaiV-ERygevqaryeeldgyalegrarevlaGLsfsqemmd 156
Cdd:COG5265 458 DAseEEVEA--------AARAAQIHDfIESLPDGYDTR---VgER-------------------------GL-------- 493
|
170 180 190
....*....|....*....|....*....|....*..
gi 505055604 157 gdvaKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD 193
Cdd:COG5265 494 ----KLSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
330-521 |
6.29e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 45.46 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 330 VHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASV--------KLGYFAQH----- 395
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhGTDVsrlhardrKVGFVFQHyalfr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 SMDLLDGESTILQWLEERFPKAGQA------------PLRALAGCFGFSgddvekrcrvLSGGEKARLVMAAMLFDPPNF 463
Cdd:PRK10851 88 HMTVFDNIAFGLTVLPRRERPNAAAikakvtqllemvQLAHLADRYPAQ----------LSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 464 LVLDEPTNHLDLDTKEMLIKAL----SAYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLrqlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
24-58 |
7.58e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.60 E-value: 7.58e-05
10 20 30
....*....|....*....|....*....|....*
gi 505055604 24 LNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQV 58
Cdd:PRK11300 28 VREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTI 62
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
325-521 |
8.31e-05 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.02 E-value: 8.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLG---------ASVKLGYFAQ- 394
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekrmndvppAERGVGMVFQs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 395 -----HsMDLLDGES---------------------TILQW--LEERFPKAgqaplralagcfgfsgddvekrcrvLSGG 446
Cdd:PRK11000 84 yalypH-LSVAENMSfglklagakkeeinqrvnqvaEVLQLahLLDRKPKA-------------------------LSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 447 EKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK-EMLI---KALSAYQGTMLFVSHDRRFLSALSNRVLELTPDGINQYG 521
Cdd:PRK11000 138 QRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvQMRIeisRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
327-372 |
9.59e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 44.25 E-value: 9.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTG 372
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
322-498 |
9.81e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 44.36 E-value: 9.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 322 EDVVNLKSVHKTYGSRTIY--DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVslgasvklgYFAQHSMDL 399
Cdd:PRK13648 5 NSIIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI---------FYNNQAITD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 400 LDgestiLQWLEERFPKAGQAPLRALAG-------CFGFSGDDV--EKRCRV--------------------LSGGEKAR 450
Cdd:PRK13648 76 DN-----FEKLRKHIGIVFQNPDNQFVGsivkydvAFGLENHAVpyDEMHRRvsealkqvdmleradyepnaLSGGQKQR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 505055604 451 LVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG----TMLFVSHD 498
Cdd:PRK13648 151 VAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSehniTIISITHD 202
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
140-253 |
1.12e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.46 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 140 RAREVLAGLSFSQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES---LIWLENFLKGYDGALLMTSH 216
Cdd:PRK13631 155 LAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGeheMMQLILDAKANNKTVFVITH 234
|
90 100 110
....*....|....*....|....*....|....*..
gi 505055604 217 DREFMNRIVTKIIEIDGGALTTYSGDYGFYDEQRALN 253
Cdd:PRK13631 235 TMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHIIN 271
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-509 |
1.32e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.85 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKT----TLFRMI--TGQELPDEGQVAVEKG-MTIGYFDQDVGEMAG-RSA-----VAEVME 87
Cdd:PRK10261 36 SFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLLRRRSrQVIELSEQSAAQMRHvRGAdmamiFQEPMT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 88 GAGPVSAVAAELRE---LETAMSDPDRMDEMDAIVErygevQARYEEldgyalegrarevlaglsfSQEMMDGDVAKLSG 164
Cdd:PRK10261 116 SLNPVFTVGEQIAEsirLHQGASREEAMVEAKRMLD-----QVRIPE-------------------AQTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 165 GWKMRVALARILLMRPDAMLLDEPSNHLDL---ESLIWLENFL-KGYDGALLMTSHDREFMNRIVTKIIEI-DGGALTTY 239
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVtiqAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMyQGEAVETG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 240 SGDYGFYDEQ----RALNARqqqaqferqqamlakeikfIERFKARASHASQVQSRVKKLEKIDRVEPPRRRQTVAfefl 315
Cdd:PRK10261 252 SVEQIFHAPQhpytRALLAA-------------------VPQLGAMKGLDYPRRFPLISLEHPAKQEPPIEQDTVV---- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 316 paprSGEDVVNLKSVHKTYGSRTiydGLDFMVRRR--------------ERWCIMGINGAGKST----LLKLVTGT---- 373
Cdd:PRK10261 309 ----DGEPILQVRNLVTRFPLRS---GLLNRVTREvhavekvsfdlwpgETLSLVGESGSGKSTtgraLLRLVESQggei 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 374 --------TNPDKG---------------SVSLGASVKLGYFAQHSM---DLLDGESTI--LQWLEERfpkAGQAPLRAL 425
Cdd:PRK10261 382 ifngqridTLSPGKlqalrrdiqfifqdpYASLDPRQTVGDSIMEPLrvhGLLPGKAAAarVAWLLER---VGLLPEHAW 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 426 AGCFGFsgddvekrcrvlSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQGTM----LFVSHDRRF 501
Cdd:PRK10261 459 RYPHEF------------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiayLFISHDMAV 526
|
....*...
gi 505055604 502 LSALSNRV 509
Cdd:PRK10261 527 VERISHRV 534
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-193 |
1.37e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 44.25 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 19 EASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkGMTIGYFDQDVGEMAGRSAVAEVMEGAgpvsAVAAE 98
Cdd:PRK10070 46 DASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLID-GVDIAKISDAELREVRRKKIAMVFQSF----ALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 99 LRELETAmsdpdrmdemdaiverygevqARYEELDGYALEGRAREVLAGLSFS--QEMMDGDVAKLSGGWKMRVALARIL 176
Cdd:PRK10070 121 MTVLDNT---------------------AFGMELAGINAEERREKALDALRQVglENYAHSYPDELSGGMRQRVGLARAL 179
|
170
....*....|....*..
gi 505055604 177 LMRPDAMLLDEPSNHLD 193
Cdd:PRK10070 180 AINPDILLMDEAFSALD 196
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
327-381 |
1.46e-04 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 43.91 E-value: 1.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 327 LKSVHKTYGSR----TIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSV 381
Cdd:COG1135 4 LENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV 62
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
327-381 |
1.51e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.02 E-value: 1.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 327 LKSVHKTY--GSRTIY--DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSV 381
Cdd:PRK11153 4 LKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
325-507 |
1.61e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.49 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 325 VNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTgTTNPDKGSVSLGASVKlgYFAQH------SMD 398
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN-RMNELESEVRVEGRVE--FFNQNiyerrvNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 399 LLDGESTILQWLEERFPKA------------GQAPLRALAGCFGFSGDDVE----------KRCRVLSGGEKARLVMAAM 456
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSvydnvaygvkivGWRPKLEIDDIVESALKDADlwdeikhkihKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 457 LFDPPNFLVLDEPTNHLDLDTK---EMLIKALS-AYQGTMLFVSHDRRFLSALSN 507
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASmkvESLIQSLRlRSELTMVIVSHNLHQVSRLSD 219
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
443-509 |
1.61e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 1.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 443 LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQ----GTMLFVSHDRRFLSALSNRV 509
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNqnnnTTILLISHDLQMLSQWADKI 229
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1-216 |
1.65e-04 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 44.35 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENIS-KSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMTIGYFDQdvgemagR 79
Cdd:TIGR00954 451 GIKFENIPlVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQ-------R 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 80 SAVAevmegagpvsavaaeLRELETAMSDPDRMDEMDAIVERYGEVQARYEELD-GYALEgraREVlaGLSFSQEMMDgd 158
Cdd:TIGR00954 524 PYMT---------------LGTLRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQlTHILE---REG--GWSAVQDWMD-- 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 159 vaKLSGGWKMRVALARILLMRPDAMLLDEPSN--HLDLESLIWleNFLKGYDGALLMTSH 216
Cdd:TIGR00954 582 --VLSGGEKQRIAMARLFYHKPQFAILDECTSavSVDVEGYMY--RLCREFGITLFSVSH 637
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-58 |
1.69e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 44.40 E-value: 1.69e-04
10 20 30
....*....|....*....|....*....|....*...
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQV 58
Cdd:COG4615 352 DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEI 389
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
435-510 |
1.69e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 44.27 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 435 DVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKE---MLIKALSAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:PRK15439 396 HAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNdiyQLIRSIAAQNVAVLFISSDLEEIEQMADRVL 474
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
343-497 |
1.85e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.07 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 343 LDFMVRRRERWCIMGINGAGKSTLLKLVTGTTnPDKGSV--------SLGASV---KLGYFAQHSMdLLDGesTILQWLE 411
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLkingielrELDPESwrkHLSWVGQNPQ-LPHG--TLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 412 ERFPKAGQAPLRAL---AGCFGF-----SGDD--VEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEML 481
Cdd:PRK11174 445 LGNPDASDEQLQQAlenAWVSEFlpllpQGLDtpIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170
....*....|....*...
gi 505055604 482 IKAL-SAYQG-TMLFVSH 497
Cdd:PRK11174 525 MQALnAASRRqTTLMVTH 542
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
288-498 |
1.91e-04 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 43.87 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 288 VQSRVKKLEKIDRVEPPRrrqtvAFEFLPAPRSGEDVVNlksvhKTYGSRTIYDGlDFMVRRRERWCIMGINGAGKSTLL 367
Cdd:PRK10070 3 IKLEIKNLYKIFGEHPQR-----AFKYIEQGLSKEQILE-----KTGLSLGVKDA-SLAIEEGEIFVIMGLSGSGKSTMV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 368 KLVTGTTNPDKGSVSLG--------------------ASVKLGYFAQHSMDLLDGESTILQWL----EERFPKAGQAPLR 423
Cdd:PRK10070 72 RLLNRLIEPTRGQVLIDgvdiakisdaelrevrrkkiAMVFQSFALMPHMTVLDNTAFGMELAginaEERREKALDALRQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 424 ALAGCFGFSGDDVekrcrvLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLD----LDTKEMLIKALSAYQGTMLFVSHD 498
Cdd:PRK10070 152 VGLENYAHSYPDE------LSGGMRQRVGLARALAINPDILLMDEAFSALDplirTEMQDELVKLQAKHQRTIVFISHD 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
162-240 |
1.92e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 43.23 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFLKGY--DGALLMTSHDREFMNRIVTKIIEIDGGALTTY 239
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLkdDYTMLLVTRSMQQASRISDRTGFFLDGDLIEY 228
|
.
gi 505055604 240 S 240
Cdd:PRK14239 229 N 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
341-510 |
2.18e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 43.16 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASV-----------KLGYFAQHSMDLLDG---ESTI 406
Cdd:PRK13642 24 NGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnlrrKIGMVFQNPDNQFVGatvEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 407 LQWLEERFPKAGQAPLRALAGCFGFSGDDVEKRCRV-LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKAL 485
Cdd:PRK13642 104 AFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPArLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170 180
....*....|....*....|....*....
gi 505055604 486 ----SAYQGTMLFVSHDRRfLSALSNRVL 510
Cdd:PRK13642 184 heikEKYQLTVLSITHDLD-EAASSDRIL 211
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
354-521 |
2.48e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 354 CIMGINGAGKSTLLK---LVTGTTNPDKGSVSLgasVKLGYF-AQHSMDLLdgeSTILQwleerfpkagqaplralagcf 429
Cdd:cd03227 25 IITGPNGSGKSTILDaigLALGGAQSATRRRSG---VKAGCIvAAVSAELI---FTRLQ--------------------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 430 gfsgddvekrcrvLSGGEKAR----LVMAAMLFDPPNFLVLDEPTNHLDLDTKEML---IKALSAYQGTMLFVSHDRRfL 502
Cdd:cd03227 78 -------------LSGGEKELsalaLILALASLKPRPLYILDEIDRGLDPRDGQALaeaILEHLVKGAQVIVITHLPE-L 143
|
170
....*....|....*....
gi 505055604 503 SALSNRVLELTPDGINQYG 521
Cdd:cd03227 144 AELADKLIHIKKVITGVYK 162
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-58 |
2.73e-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: 41.59 E-value: 2.73e-04
10 20 30
....*....|....*....|....*....|...
gi 505055604 26 RGEKIGLVGPNGAGKTTLFRMITGQELPDEGQV 58
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV 33
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
33-205 |
2.95e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 42.85 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 33 VGPNGAGKTTLFR-------MITGQELpdEGQVAVeKGMTIgyFDQDVGEMAGRSAVAEVMEGAGPVS-------AVAAE 98
Cdd:PRK14243 42 IGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTF-HGKNL--YAPDVDPVEVRRRIGMVFQKPNPFPksiydniAYGAR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 99 LRELETamsdpdrmdEMDAIVERYGEVQARYEELdgyalEGRAREvlAGLSfsqemmdgdvakLSGGWKMRVALARILLM 178
Cdd:PRK14243 117 INGYKG---------DMDELVERSLRQAALWDEV-----KDKLKQ--SGLS------------LSGGQQQRLCIARAIAV 168
|
170 180
....*....|....*....|....*..
gi 505055604 179 RPDAMLLDEPSNHLDLESLIWLENFLK 205
Cdd:PRK14243 169 QPEVILMDEPCSALDPISTLRIEELMH 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-383 |
3.18e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.36 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 25 NRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVekgmtigyfdqDVGEMAGRSAVAEVMEGagpvsaVAAELRELET 104
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILI-----------DGQEMRFASTTAALAAG------VAIIYQELHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 105 AmsdPDrMDEMDAIVerYGEVQARYEELDGYALEGRAREVLAGLSfsqemMDGD----VAKLS-GGWKMrVALARILLMR 179
Cdd:PRK11288 91 V---PE-MTVAENLY--LGQLPHKGGIVNRRLLNYEAREQLEHLG-----VDIDpdtpLKYLSiGQRQM-VEIAKALARN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 180 PDAMLLDEPSNHL---DLESLIWLENFLKGYDGALLMTSHDREfmnrivtkiiEIDG--GALTTysgdygFYDEQRA--L 252
Cdd:PRK11288 159 ARVIAFDEPTSSLsarEIEQLFRVIRELRAEGRVILYVSHRME----------EIFAlcDAITV------FKDGRYVatF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 253 NARQQQAQFERQQAMLAKEIKFIERFKARASHASQVQsrvkklekIDRVEPPRRRQTVAFEFlpapRSGEDVvnlksvhk 332
Cdd:PRK11288 223 DDMAQVDRDQLVQAMVGREIGDIYGYRPRPLGEVRLR--------LDGLKGPGLREPISFSV----RAGEIV-------- 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 505055604 333 tygsrtiydGLdfmvrrrerwciMGINGAGKSTLLKLVTGTTNPDKGSVSL 383
Cdd:PRK11288 283 ---------GL------------FGLVGAGRSELMKLLYGATRRTAGQVYL 312
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
341-510 |
3.51e-04 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 42.28 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGAS---------------------VKLgyF------- 392
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQhieglpghqiarmgvvrtfqhVRL--Fremtvie 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 393 ----AQH---SMDLLDG----------ESTIL----QWLEerfpkagQAPLRALAgcfgfsgddvEKRCRVLSGGEKARL 451
Cdd:PRK11300 100 nllvAQHqqlKTGLFSGllktpafrraESEALdraaTWLE-------RVGLLEHA----------NRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505055604 452 VMAAMLFDPPNFLVLDEPTNHLD-LDTKEM--LIKAL-SAYQGTMLFVSHDRRFLSALSNRVL 510
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNpKETKELdeLIAELrNEHNVTVLLIEHDMKLVMGISDRIY 225
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
332-497 |
3.69e-04 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 41.52 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 332 KTYGSRTIYDGLDFMVrrrerwCIMGINGAGKSTLLKlvtgttnpdkgSVSLGasvkLGYFAQHSmdlldgESTILQWLE 411
Cdd:cd03239 10 KSYRDETVVGGSNSFN------AIVGPNGSGKSNIVD-----------AICFV----LGGKAAKL------RRGSLLFLA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 412 ERFPKAGQ--APLRAL--AGCFGFSGDDVEkrcRVLSGGEKA----RLVMAAMLFDPPNFLVLDEPTNHLDLDTKE---M 480
Cdd:cd03239 63 GGGVKAGInsASVEITfdKSYFLVLQGKVE---QILSGGEKSlsalALIFALQEIKPSPFYVLDEIDAALDPTNRRrvsD 139
|
170
....*....|....*..
gi 505055604 481 LIKALSAYQGTMLFVSH 497
Cdd:cd03239 140 MIKEMAKHTSQFIVITL 156
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
139-234 |
4.24e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.80 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 139 GRAREVLAGLSFSqEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLD--LESLIWLENFLKGYDGA-LLMTS 215
Cdd:NF000106 123 ARADELLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDprTRNEVWDEVRSMVRDGAtVLLTT 201
|
90
....*....|....*....
gi 505055604 216 HDREFMNRIVTKIIEIDGG 234
Cdd:NF000106 202 QYMEEAEQLAHELTVIDRG 220
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-205 |
5.19e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 42.01 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 32 LVGPNGAGKTTLFRmiTGQELPDE-------GQVAVEKGMTIGYfdQDVGEMAGRSAVAEVMEGAGPVSAVAAELRELET 104
Cdd:PRK14271 52 LMGPTGSGKTTFLR--TLNRMNDKvsgyrysGDVLLGGRSIFNY--RDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 105 AMSDPDRmdemdaivERYGEVQARYEELdgyALEGRAREVLAGLSFsqemmdgdvaKLSGGWKMRVALARILLMRPDAML 184
Cdd:PRK14271 128 HKLVPRK--------EFRGVAQARLTEV---GLWDAVKDRLSDSPF----------RLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180
....*....|....*....|.
gi 505055604 185 LDEPSNHLDLESLIWLENFLK 205
Cdd:PRK14271 187 LDEPTSALDPTTTEKIEEFIR 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
162-231 |
5.45e-04 |
|
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: 41.44 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 162 LSGGWKM------RVALARILLMRPDAMLLDEPSNHLD-------LESLIwlENFLKGYDGALLMTSHDREFMNRIvTKI 228
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeenieesLAEII--EERKSQKNFQLIVITHDEELVDAA-DHI 192
|
...
gi 505055604 229 IEI 231
Cdd:cd03240 193 YRV 195
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
422-509 |
5.57e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 41.02 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 422 LRALAGCFGFSGDDVE-KRCRV--------LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAY---- 488
Cdd:cd03222 42 VKILAGQLIPNGDNDEwDGITPvykpqyidLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLseeg 121
|
90 100
....*....|....*....|.
gi 505055604 489 QGTMLFVSHDRRFLSALSNRV 509
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRI 142
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
162-196 |
6.67e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 6.67e-04
10 20 30
....*....|....*....|....*....|....*
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES 196
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| EutP |
COG4917 |
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport ... |
29-75 |
8.35e-04 |
|
Ethanolamine utilization protein EutP, contains a P-loop NTPase domain [Amino acid transport and metabolism];
Pssm-ID: 443945 [Multi-domain] Cd Length: 145 Bit Score: 39.78 E-value: 8.35e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 505055604 29 KIGLVGPNGAGKTTLFRMITGQELPdegqvaVEKGMTIGYFDQDV---GE 75
Cdd:COG4917 3 RIMLIGRSGAGKTTLTQALNGEELE------YRKTQAVEYYDNIIdtpGE 46
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
343-482 |
8.36e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 41.31 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 343 LDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSL-GASVKLG---YFAQHSMDLLDGESTILQwLEERFPKAG 418
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIdDHPLHFGdysYRSQRIRMIFQDPSTSLN-PRQRISQIL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 419 QAPLRALAgcfGFSGDDVEKRC------------------RVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEM 480
Cdd:PRK15112 111 DFPLRLNT---DLEPEQREKQIietlrqvgllpdhasyypHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQ 187
|
..
gi 505055604 481 LI 482
Cdd:PRK15112 188 LI 189
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
27-241 |
8.84e-04 |
|
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: 41.10 E-value: 8.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDE---GQVAV-----EKGMT---IGYFDQDvGEMAGRSAVAEVMegagpvsAV 95
Cdd:cd03234 33 GQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFngqprKPDQFqkcVAYVRQD-DILLPGLTVRETL-------TY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 96 AAELReLETAMSDPDRmdemDAIVERYGEVQARYEELDGYALEGrarevlaglsfsqemmdgdvakLSGGWKMRVALARI 175
Cdd:cd03234 105 TAILR-LPRKSSDAIR----KKRVEDVLLRDLALTRIGGNLVKG----------------------ISGGERRRVSIAVQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 176 LLMRPDAMLLDEPSNHLDLESLIWLENFLKGY---DGALLMTSHD-REFMNRIVTKIIEIDGGALtTYSG 241
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLarrNRIVILTIHQpRSDLFRLFDRILLLSSGEI-VYSG 226
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-236 |
9.13e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 41.22 E-value: 9.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 2 IRIENISKSnSHRILYIEASAALNRGEKIGLVGPNGAGKTTL-----------FRMITGQELPDEGQVAVE--KGMTIGY 68
Cdd:PRK10418 5 IELRNIALQ-AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaalgilpagVRQTAGRVLLDGKPVAPCalRGRKIAT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 69 FDQdvgemAGRSAVaevmegaGPVSAVAAELRELETAMSDPDRMDEMDAIVERYGevqaryeeldgyaLEGRAReVLAGL 148
Cdd:PRK10418 84 IMQ-----NPRSAF-------NPLHTMHTHARETCLALGKPADDATLTAALEAVG-------------LENAAR-VLKLY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 149 SFsqEMmdgdvaklSGGWKMRVALARILLMRPDAMLLDEPSNHLDLES----LIWLENFLKGYDGALLMTSHDREFMNRI 224
Cdd:PRK10418 138 PF--EM--------SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAqariLDLLESIVQKRALGMLLVTHDMGVVARL 207
|
250
....*....|..
gi 505055604 225 VTKIIEIDGGAL 236
Cdd:PRK10418 208 ADDVAVMSHGRI 219
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
312-497 |
9.57e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 42.01 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 312 FEFLPAPRS--GEDVVNLKSvhktyGSRTIyDGLDFMVRRrERWCIMGIN---------------GAGKSTLLKLVTGTT 374
Cdd:PRK10790 319 FELMDGPRQqyGNDDRPLQS-----GRIDI-DNVSFAYRD-DNLVLQNINlsvpsrgfvalvghtGSGKSTLASLLMGYY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 375 NPDKGSV--------SLGASVKLGYFAQHSMD---LLD------------GESTILQWLE--------ERFPKAGQAPLr 423
Cdd:PRK10790 392 PLTEGEIrldgrplsSLSHSVLRQGVAMVQQDpvvLADtflanvtlgrdiSEEQVWQALEtvqlaelaRSLPDGLYTPL- 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 424 alagcfGFSGDDvekrcrvLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAY--QGTMLFVSH 497
Cdd:PRK10790 471 ------GEQGNN-------LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVreHTTLVVIAH 533
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
443-510 |
1.14e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 1.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 443 LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQGTM----LFVSHDRRFLSALSNRVL 510
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMsmgvIFITHDMGVVAEIADRVL 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
443-508 |
1.25e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.91 E-value: 1.25e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 443 LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDL----DTKEMLIKALSAYqgTMLFVSHDRRFLSALSNR 508
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPisagKIEETLLGLKDDY--TMLLVTRSMQQASRISDR 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
341-539 |
1.31e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.85 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 341 DGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPDKGSVSLGASVklGYFAQHSM---DLLDGESTILQWLEERFPKA 417
Cdd:TIGR00957 655 NGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSV--AYVPQQAWiqnDSLRENILFGKALNEKYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 418 GQAPLRALAGCFGF-SGDDVE--KRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKALSAYQG---- 490
Cdd:TIGR00957 733 VLEACALLPDLEILpSGDRTEigEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlkn 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505055604 491 -TMLFVSHDRRFLSALSnrVLELTPDGINQYGGGYSEYVERTGQEAPGLR 539
Cdd:TIGR00957 813 kTRILVTHGISYLPQVD--VIIVMSGGKISEMGSYQELLQRDGAFAEFLR 860
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
443-519 |
1.32e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 41.45 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 443 LSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTK-EM--LIKALsAYQG-TMLFVSHDRRFLSALSNRVL-----ELT 513
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKyEIykLINQL-VQQGvAIIVISSELPEVLGLSDRVLvmhegKLK 484
|
....*.
gi 505055604 514 PDGINQ 519
Cdd:PRK13549 485 GDLINH 490
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
163-217 |
1.43e-03 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 40.86 E-value: 1.43e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 505055604 163 SGGWKMRVALARILLMRPDAMLLDEPSNHLDL---ESLIWLENFLKG-YDGALLMTSHD 217
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVtvqAQIMTLLNELKReFNTAIIMITHD 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-188 |
1.91e-03 |
|
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: 39.34 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 3 RIENISKSNSHRilyiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfdqdvGEMAGRSAV 82
Cdd:cd03215 6 EVRGLSVKGAVR----DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLD------------GKPVTRRSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 83 AEvmegagpvsAVAAELreletamsdpdrmdemdaiverygevqaryeeldGYALEGRARE-VLAGLSFSQEMMDGDVak 161
Cdd:cd03215 70 RD---------AIRAGI----------------------------------AYVPEDRKREgLVLDLSVAENIALSSL-- 104
|
170 180
....*....|....*....|....*..
gi 505055604 162 LSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:cd03215 105 LSGGNQQKVVLARWLARDPRVLILDEP 131
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-508 |
2.18e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 40.08 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 334 YGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNP-----DKGSVSLGASVKLGY----------------- 391
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYrdvlefrrrvgmlfqrp 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 392 --FAQHSMD-LLDGESTILQWLEERFPKAGQAPLRALaGCFGFSGDDVEKRCRVLSGGEKARLVMAAMLFDPPNFLVLDE 468
Cdd:PRK14271 111 npFPMSIMDnVLAGVRAHKLVPRKEFRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 505055604 469 PTNHLDLDTKEML---IKALsAYQGTMLFVSHDRRFLSALSNR 508
Cdd:PRK14271 190 PTSALDPTTTEKIeefIRSL-ADRLTVIIVTHNLAQAARISDR 231
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
337-509 |
2.24e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.07 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 337 RTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTGTTNPdkGSVSLGASVklgyfaqhsmdLLDGE------------S 404
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRV-----------LLDGKpvapcalrgrkiA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 405 TILQwleerFPKAGQAPLRALAG-------CFGFSGDD-----------VEKRCRVL-------SGGEKARLVMA-AMLF 458
Cdd:PRK10418 83 TIMQ-----NPRSAFNPLHTMHTharetclALGKPADDatltaaleavgLENAARVLklypfemSGGMLQRMMIAlALLC 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505055604 459 DPPnFLVLDEPTNHLDLDTKEM---LIKALSAYQGT-MLFVSHDRRFLSALSNRV 509
Cdd:PRK10418 158 EAP-FIIADEPTTDLDVVAQARildLLESIVQKRALgMLLVTHDMGVVARLADDV 211
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
443-501 |
2.31e-03 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 40.44 E-value: 2.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505055604 443 LSGGEKARlVMAAM-LFDPPNFLVLDEPTNHLD-------LDtkemLIKALSAYQGT-MLFVSHD----RRF 501
Cdd:COG4172 157 LSGGQRQR-VMIAMaLANEPDLLIADEPTTALDvtvqaqiLD----LLKDLQRELGMaLLLITHDlgvvRRF 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
11-49 |
2.34e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 2.34e-03
10 20 30
....*....|....*....|....*....|....*....
gi 505055604 11 NSHRILYiEASAALNRGEKIGLVGPNGAGKTTLFRMITG 49
Cdd:PRK10938 271 NDRPILH-NLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
355-387 |
2.76e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.37 E-value: 2.76e-03
10 20 30
....*....|....*....|....*....|....
gi 505055604 355 IMGINGAGKSTLLKLVTGTTNPDKGSVS-LGASV 387
Cdd:PRK10762 35 LVGENGAGKSTMMKVLTGIYTRDAGSILyLGKEV 68
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1-216 |
2.77e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.08 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIgLVGPNGAGKTTLFRMITGQELPDEGQVAVEKGMT-------IGYFDQDV 73
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSITFLPSAITY-IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniakpyCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 74 GemagrsavaevmegagpvsavaaelreLETAMSdpdRMDEMDAIVERYGEVQARYEELDGYALegrarevlaglsfsQE 153
Cdd:PRK13541 80 G---------------------------LKLEMT---VFENLKFWSEIYNSAETLYAAIHYFKL--------------HD 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505055604 154 MMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEPSNHLDLESLIWLENFL---KGYDGALLMTSH 216
Cdd:PRK13541 116 LLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIvmkANSGGIVLLSSH 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
324-372 |
2.99e-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: 40.19 E-value: 2.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 505055604 324 VVNLKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTG 372
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG 49
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-188 |
3.07e-03 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 40.00 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 3 RIENISKSNSHRilyiEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVEkgmtigyfdqdvgemaGRSav 82
Cdd:COG1129 258 EVEGLSVGGVVR----DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD----------------GKP-- 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 83 aevMEGAGPVSAVAAELreletAMSDPDRMDE-----MD-------AIVERYgevqARYEELDGYALEGRAREVLAGLSF 150
Cdd:COG1129 316 ---VRIRSPRDAIRAGI-----AYVPEDRKGEglvldLSirenitlASLDRL----SRGGLLDRRRERALAEEYIKRLRI 383
|
170 180 190
....*....|....*....|....*....|....*...
gi 505055604 151 SQEMMDGDVAKLSGGWKMRVALARILLMRPDAMLLDEP 188
Cdd:COG1129 384 KTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
433-513 |
3.13e-03 |
|
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: 39.24 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 433 GDDVE--KRCRVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKAlsayqGTMLFVSHDRRFLSALSNRVL 510
Cdd:cd03290 129 GDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHLMQE-----GILKFLQDDKRTLVLVTHKLQ 203
|
...
gi 505055604 511 ELT 513
Cdd:cd03290 204 YLP 206
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-196 |
3.23e-03 |
|
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: 39.01 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTT----LFRMITgqelPDEGQVavekgmTIGYFD-QDVGEMAGRSAVAEVmegagPVSAV 95
Cdd:cd03244 24 SFSIKPGEKVGIVGRTGSGKSSlllaLFRLVE----LSSGSI------LIDGVDiSKIGLHDLRSRISII-----PQDPV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 96 --AAELRE-LetamsDPDRM---DEMDAIVERYG---EVQARYEELDGYALEGrarevlaGLSFSQemmdgdvaklsgGW 166
Cdd:cd03244 89 lfSGTIRSnL-----DPFGEysdEELWQALERVGlkeFVESLPGGLDTVVEEG-------GENLSV------------GQ 144
|
170 180 190
....*....|....*....|....*....|
gi 505055604 167 KMRVALARILLMRPDAMLLDEPSNHLDLES 196
Cdd:cd03244 145 RQLLCLARALLRKSKILVLDEATASVDPET 174
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-61 |
3.26e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.26 E-value: 3.26e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 505055604 21 SAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE 61
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
441-485 |
4.11e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 4.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 505055604 441 RVLSGGEKARLVMAAMLFDPPNFLVLDEPTNHLDLDTKEMLIKAL 485
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
334-497 |
4.45e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 39.05 E-value: 4.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 334 YGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTG--TTNPD---KGSVSL-GASV------------KLGYFAQH 395
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEarvEGEVRLfGRNIyspdvdpievrrEVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 396 S-----MDLLDGESTILQW-----LEERFPKAGQAPLRALAgcfgfSGDDVEKRCR----VLSGGEKARLVMAAMLFDPP 461
Cdd:PRK14267 94 PnpfphLTIYDNVAIGVKLnglvkSKKELDERVEWALKKAA-----LWDEVKDRLNdypsNLSGGQRQRLVIARALAMKP 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 505055604 462 NFLVLDEPTNHLD----LDTKEMLIKALSAYqgTMLFVSH 497
Cdd:PRK14267 169 KILLMDEPTANIDpvgtAKIEELLFELKKEY--TIVLVTH 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-61 |
5.06e-03 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 39.65 E-value: 5.06e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505055604 1 MIRIENISKSNSHRILYIEASAALNRGEKIGLVGPNGAGKTTLFRMITGQELPDEGQVAVE 61
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIG 71
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
327-372 |
8.24e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 38.76 E-value: 8.24e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 505055604 327 LKSVHKTYGSRTIYDGLDFMVRRRERWCIMGINGAGKSTLLKLVTG 372
Cdd:PRK13549 8 MKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
27-58 |
8.34e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.26 E-value: 8.34e-03
10 20 30
....*....|....*....|....*....|..
gi 505055604 27 GEKIGLVGPNGAGKTTLFRMITGQELPDEGQV 58
Cdd:PRK13546 50 GDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV 81
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
114-198 |
9.44e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.09 E-value: 9.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505055604 114 EMDAIVER-------YGEVQARyeeLDGYALEgrarevlaglsfsqemmdgdvakLSGGWKMRVALARILLMRPDAMLLD 186
Cdd:COG1117 126 ELDEIVEEslrkaalWDEVKDR---LKKSALG-----------------------LSGGQQQRLCIARALAVEPEVLLMD 179
|
90
....*....|....*...
gi 505055604 187 EPSNHLD------LESLI 198
Cdd:COG1117 180 EPTSALDpistakIEELI 197
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
2-48 |
9.65e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.48 E-value: 9.65e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 505055604 2 IRIENIsksNSHRILYIEASAALNrgekiGLVGPNGAGKTTLFRMIT 48
Cdd:pfam13476 1 LTIENF---RSFRDQTIDFSKGLT-----LITGPNGSGKTTILDAIK 39
|
|
| |
