|
Name |
Accession |
Description |
Interval |
E-value |
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-535 |
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: 618.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 6 ASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIPDYEKSESVYQ 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLRIGYLPQEPPLDDDLTVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 CIKSVFKELDTISKQLETIETKMIEERENINslvaRYGELQTYYEENGGYEIDAKIRKVTHGLNIAH-LLKAKWGDLSGG 164
Cdd:COG0488 81 TVLDGDAELRALEAELEELEAKLAEPDEDLE----RLAELQEEFEALGGWEAEARAEEILSGLGFPEeDLDRPVSELSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 165 ERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHFYNGNYSY 244
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLTLYPGNYSA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 245 FVEERDKRLLIEFEAYKTQQKKIKKMKESIKQLRTWASQAKppnaamfrRAKSMEKALNRIQRLEKPlLDSKKMHITLEE 324
Cdd:COG0488 237 YLEQRAERLEQEAAAYAKQQKKIAKEEEFIRRFRAKARKAK--------QAQSRIKALEKLEREEPP-RRDKTVEIRFPP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 325 GMNVSNRVIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQHE 403
Cdd:COG0488 308 PERLGKKVLELEGLSKSYGDkTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 404 FERDGNDTLLHTFRK-KVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDA 482
Cdd:COG0488 388 EELDPDKTVLDELRDgAPGGTEQEVRGYLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 483 KEIIEDALLDFNGTIITVSHDRYFLNKLFNTTYLLKNKTLEKFEGNYDYIKEK 535
Cdd:COG0488 468 LEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGGYDDYLEK 520
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
8-536 |
4.10e-111 |
|
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: 341.53 E-value: 4.10e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTED--ILFDhikITLN--SGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIPDYEKSESV 83
Cdd:TIGR03719 9 RVSKVVPPKkeILKD---ISLSffPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIKSVFKELDTISKQLETIETKMIEERENINSLVARYGELQTYYEENGGYEIDAKIRKVTHGLNIAHLlKAKWGDLSG 163
Cdd:TIGR03719 86 RENVEEGVAEIKDALDRFNEISAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALRCPPW-DADVTKLSG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHFYNGNYS 243
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNVAGWILELDRGRGIPWEGNYS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 244 YFVEERDKRLLIEFEAYKTQQKKIKKMKEsikqlrtWASQAkpPNAamfRRAKSmeKAlnRIQRLEKpLL--DSKK---- 317
Cdd:TIGR03719 245 SWLEQKQKRLEQEEKEESARQKTLKRELE-------WVRQS--PKG---RQAKS--KA--RLARYEE-LLsqEFQKrnet 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 318 MHITLEEGMNVSNRVIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKI 396
Cdd:TIGR03719 308 AEIYIPPGPRLGDKVIEAENLTKAFGDkLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 397 GYLSQH-----------EFERDGNDTLlhtfrkKVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTD 465
Cdd:TIGR03719 388 AYVDQSrdaldpnktvwEEISGGLDII------KLGKREIPSRAYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSG 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 466 YNLLVLDEPTNHLDIDAKEIIEDALLDFNGTIITVSHDRYFLNKLfnTTYLLK---NKTLEKFEGNY-DYIKEKM 536
Cdd:TIGR03719 462 GNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRI--ATHILAfegDSHVEWFEGNFsEYEEDKK 534
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
8-535 |
2.33e-104 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 323.99 E-value: 2.33e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTED--ILFDhikITLN--SGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIPDYEKSESV 83
Cdd:PRK11819 11 RVSKVVPPKkqILKD---ISLSffPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPGIKVGYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIKSVFKELDTISKQLETIETKMIEERENINSLVARYGELQTYYEENGGYEIDAKirkvthgLNIA-HLLK-----AK 157
Cdd:PRK11819 88 RENVEEGVAEVKAALDRFNEIYAAYAEPDADFDALAAEQGELQEIIDAADAWDLDSQ-------LEIAmDALRcppwdAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 158 WGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHF 237
Cdd:PRK11819 161 VTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNVAGWILELDRGRGIP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 238 YNGNYSYFVEERDKRLliefeayKTQQKKIKKMKESIKQLRTWASQAkpPNAamfRRAKSmeKAlnRIQRLEKpLL--DS 315
Cdd:PRK11819 241 WEGNYSSWLEQKAKRL-------AQEEKQEAARQKALKRELEWVRQS--PKA---RQAKS--KA--RLARYEE-LLseEY 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 316 KKMHITLE----EGMNVSNRVIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKT 390
Cdd:PRK11819 304 QKRNETNEifipPGPRLGDKVIEAENLSKSFGDrLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 391 ASNLKIGYLSQHE---------FER--DGNDTLlhtfrkKVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWA 459
Cdd:PRK11819 384 GETVKLAYVDQSRdaldpnktvWEEisGGLDII------KVGNREIPSRAYVGRFNFKGGDQQKKVGVLSGGERNRLHLA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 460 QLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNGTIITVSHDRYFLNKLfnTTYLL---KNKTLEKFEGNY-DYIKEK 535
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRI--ATHILafeGDSQVEWFEGNFqEYEEDK 535
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-537 |
7.20e-92 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 291.03 E-value: 7.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQipD---YEK 79
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNERLGKLRQ--DqfaFEE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 sesvyqciksvFKELDT-ISKQLETIETKmiEERENINSLVA-------RYGELQTYYEENGGYEIDAKIRKVTHGLNIA 151
Cdd:PRK15064 79 -----------FTVLDTvIMGHTELWEVK--QERDRIYALPEmseedgmKVADLEVKFAEMDGYTAEARAGELLLGVGIP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 152 hlLKAKWGDLSG---GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQII 228
Cdd:PRK15064 146 --EEQHYGLMSEvapGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSVCTHMA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 229 EIDQKKLHFYNGNYSYFveerdkrLLIEFEAYKTQQKKIKKMKESIKQLRTWASQAKPpNAAMFRRAKSMEKALNRIQRL 308
Cdd:PRK15064 224 DLDYGELRVYPGNYDEY-------MTAATQARERLLADNAKKKAQIAELQSFVSRFSA-NASKAKQATSRAKQIDKIKLE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 309 E-KPlldSKKMH--ITLEEGMNVSNRVIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSID 384
Cdd:PRK15064 296 EvKP---SSRQNpfIRFEQDKKLHRNALEVENLTKGFDNgPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 385 KGSIKTASNLKIGYLSQ---HEFERDGNDTLLHTFRKKVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQL 461
Cdd:PRK15064 373 SGTVKWSENANIGYYAQdhaYDFENDLTLFDWMSQWRQEGDDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 462 VNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNGTIITVSHDRYFLNKLFNTTYLLKNKTLEKFEGNY-DYIKEKML 537
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFSGTYeEYLRSQGI 529
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-530 |
3.88e-90 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 289.38 E-value: 3.88e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 17 ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQ-IPDYEKSESVYQCiksvfkELD 95
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQeTPALPQPALEYVI------DGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 96 TISKQLETiETKMIEERENINSLVARYGELQTYYeengGYEIDAKIRKVTHGLNIAH-LLKAKWGDLSGGERTKVGIAQM 174
Cdd:PRK10636 89 REYRQLEA-QLHDANERNDGHAIATIHGKLDAID----AWTIRSRAASLLHGLGFSNeQLERPVSDFSGGWRMRLNLAQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 175 LIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHFYNGNYSYFVEERDKRLL 254
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYTGNYSSFEVQRATRLA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 255 IEFEAYKTQQKKIKKMKESIKQLRTWASQAKppnaamfrRAKSMEKALNRIQRLEKPLLDSkKMHITLEEGMNVSNRVIE 334
Cdd:PRK10636 244 QQQAMYESQQERVAHLQSYIDRFRAKATKAK--------QAQSRIKMLERMELIAPAHVDN-PFHFSFRAPESLPNPLLK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 335 MENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQH--EFERDGNDT 411
Cdd:PRK10636 315 MEKVSAGYGDrIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFAQHqlEFLRADESP 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 LLHTFRKKVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALL 491
Cdd:PRK10636 395 LQHLARLAPQELEQKLRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALI 474
|
490 500 510
....*....|....*....|....*....|....*....
gi 488409350 492 DFNGTIITVSHDRYFLNKLFNTTYLLKNKTLEKFEGNYD 530
Cdd:PRK10636 475 DFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDGDLE 513
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-528 |
1.99e-83 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 271.82 E-value: 1.99e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIPDYEKS 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQDPPRNVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 ESVY-------QCIKSVFKELDTISKQLETietkmiEERE-NINSLvaryGELQTYYEENGGYEIDAKIRKVTH--GLNi 150
Cdd:PRK11147 81 GTVYdfvaegiEEQAEYLKRYHDISHLVET------DPSEkNLNEL----AKLQEQLDHHNLWQLENRINEVLAqlGLD- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 151 AHllkAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEI 230
Cdd:PRK11147 150 PD---AALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIRNMATRIVDL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 231 DQKKLHFYNGNYSYFVEERDKRLLIEFEAYKTQQKKIKK----MKESIKQLRTwasqakpPNAAMFRRAKSMEKAlnRIQ 306
Cdd:PRK11147 227 DRGKLVSYPGNYDQYLLEKEEALRVEELQNAEFDRKLAQeevwIRQGIKARRT-------RNEGRVRALKALRRE--RSE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 307 RLEkpLLDSKKMHItlEEGMNVSNRVIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDK 385
Cdd:PRK11147 298 RRE--VMGTAKMQV--EEASRSGKIVFEMENVNYQIDGkQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADS 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 386 GSIKTASNLKIGYLSQHEFERDGNDTLLHTF---RKKVNVSeDQARHILAH---FMFYGKDVFKKVNELSGGEKIRLRWA 459
Cdd:PRK11147 374 GRIHCGTKLEVAYFDQHRAELDPEKTVMDNLaegKQEVMVN-GRPRHVLGYlqdFLFHPKRAMTPVKALSGGERNRLLLA 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 460 QLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNGTIITVSHDRYFLNKLFNTTYLlknktlekFEGN 528
Cdd:PRK11147 453 RLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWI--------FEGN 513
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
24-533 |
1.02e-55 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 198.93 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 24 ITLNSGDTLGLVGRNGEGKTTLLKLLSgmerpSTGVISWKKDIKIGYLNQ--IPDyekSESVYQCI-------KSVFKEL 94
Cdd:PLN03073 198 VTLAFGRHYGLVGRNGTGKTTFLRYMA-----MHAIDGIPKNCQILHVEQevVGD---DTTALQCVlntdierTQLLEEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 DTISKQLETIETKMIEERENI--------NSLVARYGELQTYYEENGGYEIDAKIRKVTHGLNI-AHLLKAKWGDLSGGE 165
Cdd:PLN03073 270 AQLVAQQRELEFETETGKGKGankdgvdkDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFtPEMQVKATKTFSGGW 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 166 RTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHFYNGNYSYF 245
Cdd:PLN03073 350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKLVTYKGDYDTF 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 246 VEERDKRLLIEFEAYKTQQKKIKKMKESIKQLRTWASQAKppnaamfrRAKSMEKALNRIQ-----------RLEKPLLD 314
Cdd:PLN03073 430 ERTREEQLKNQQKAFESNERSRSHMQAFIDKFRYNAKRAS--------LVQSRIKALDRLGhvdavvndpdyKFEFPTPD 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 315 SKKmhitleegmnvSNRVIEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTAS 392
Cdd:PLN03073 502 DRP-----------GPPIISFSDASFGYPGgpLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 393 NLKIGYLSQHEFerDGND----TLLHTFRKKVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNL 468
Cdd:PLN03073 571 KVRMAVFSQHHV--DGLDlssnPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHI 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 469 LVLDEPTNHLDIDAKEIIEDALLDFNGTIITVSHDRYFLNKLFNTTYLLKNKTLEKFEGNY-DYIK 533
Cdd:PLN03073 649 LLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTFhDYKK 714
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
333-521 |
7.83e-52 |
|
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: 173.40 E-value: 7.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQheferdgndt 411
Cdd:cd03221 1 IELENLSKTYGGkLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 llhtfrkkvnvsedqarhilahfmfygkdvfkkvneLSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALL 491
Cdd:cd03221 71 ------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALK 114
|
170 180 190
....*....|....*....|....*....|
gi 488409350 492 DFNGTIITVSHDRYFLNKLFNTTYLLKNKT 521
Cdd:cd03221 115 EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-247 |
1.08e-49 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 178.72 E-value: 1.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIPDY-EKSE 81
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGETVKIGYFDQHQEElDPDK 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVYQCIKSVFKELDTISkqletietkmieerenINSLVARYGelqtyyeeNGGYEIDAKIrkvthglniahllkakwGDL 161
Cdd:COG0488 395 TVLDELRDGAPGGTEQE----------------VRGYLGRFL--------FSGDDAFKPV-----------------GVL 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHFYNGN 241
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYPGG 513
|
....*.
gi 488409350 242 YSYFVE 247
Cdd:COG0488 514 YDDYLE 519
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-234 |
9.35e-47 |
|
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: 159.92 E-value: 9.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQipdyeksesv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVKIGYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 yqciksvfkeldtiskqletietkmieereninslvarygelqtyyeenggyeidakirkvthglniahllkakwgdLSG 163
Cdd:cd03221 71 -----------------------------------------------------------------------------LSG 73
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKK 234
Cdd:cd03221 74 GEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
332-522 |
4.30e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.05 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------TASNLKIGYLSQHE- 403
Cdd:COG1121 6 AIELENLTVSYGGrPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRlfgkppRRARRRIGYVPQRAe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 404 ---------FE-----RDGNDTLLHTFRKKvnvSEDQARHIL-----AHFmfygKDvfKKVNELSGGEKIRLRWAQLVNT 464
Cdd:COG1121 86 vdwdfpitvRDvvlmgRYGRRGLFRRPSRA---DREAVDEALervglEDL----AD--RPIGELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 465 DYNLLVLDEPTNHLDIDAKEIIEDALLDFNG---TIITVSHDRYFLNKLFNTTYLLkNKTL 522
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRRegkTILVVTHDLGAVREYFDRVLLL-NRGL 216
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-253 |
1.24e-32 |
|
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: 131.60 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIPDYEKSE 81
Cdd:TIGR03719 321 KVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETVKLAYVDQSRDALDPN 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqciKSVFKEldtISKQLETIEtkmIEEREnINS--LVARY---GELQTyyeenggyeidakiRKVthglniahllka 156
Cdd:TIGR03719 401 ------KTVWEE---ISGGLDIIK---LGKRE-IPSraYVGRFnfkGSDQQ--------------KKV------------ 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 157 kwGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQII--EIDQKk 234
Cdd:TIGR03719 442 --GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAGCAVVISHDRWFLDRIATHILafEGDSH- 518
|
250
....*....|....*....
gi 488409350 235 LHFYNGNYSYFVEERDKRL 253
Cdd:TIGR03719 519 VEWFEGNFSEYEEDKKRRL 537
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-251 |
1.73e-32 |
|
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: 124.58 E-value: 1.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI---------KIGYLNQ 73
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgEDVrkeprearrQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 74 IPDYEKSESVyqciksvfkeldtiskqletietkmieeRENINSLVARYGelqtyyeeNGGYEIDAKIRKVTHGLNIAHL 153
Cdd:COG4555 82 ERGLYDRLTV----------------------------RENIRYFAELYG--------LFDEELKKRIEELIELLGLEEF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 154 LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVIVS-HDRYFLDETVNQIIEI 230
Cdd:COG4555 126 LDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRAlkKEGKTVLFSsHIMQEVEALCDRVVIL 205
|
250 260
....*....|....*....|.
gi 488409350 231 DQKKLHfYNGNYSYFVEERDK 251
Cdd:COG4555 206 HKGKVV-AQGSLDELREEIGE 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-503 |
6.84e-32 |
|
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: 128.87 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILF--DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMErPSTGVISWKKDIKIGYLNQIPDYEKS 80
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 ESvyqcIKSVFKELDTiskQL--ETIETKMIEERENINSlvarygelqtyyeenGGYEIDAKIRKVTHGLNIAHLLKAKW 158
Cdd:COG1123 83 RR----IGMVFQDPMT---QLnpVTVGDQIAEALENLGL---------------SRAEARARVLELLEAVGLERRLDRYP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 159 GDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKK 234
Cdd:COG1123 141 HQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGR 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 235 LhfyngnysyfVEERdkrlliefeayktqqkkikkmkesikqlrtwasqakpPNAAMFRRAKSMEKAlnriqrlekPLLD 314
Cdd:COG1123 221 I----------VEDG-------------------------------------PPEEILAAPQALAAV---------PRLG 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 315 SkkMHITLEEGMNVSNRVIEMENVTKAYD-------DVLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGS 387
Cdd:COG1123 245 A--ARGRAAPAAAAAEPLLEVRNLSKRYPvrgkggvRAV-DDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 388 IktasnlkigylsqhEFerDGNDTL------LHTFRKKV---------------NVSEDQARHILAHFMFYGKDVFKKVN 446
Cdd:COG1123 322 I--------------LF--DGKDLTklsrrsLRELRRRVqmvfqdpysslnprmTVGDIIAEPLRLHGLLSRAERRERVA 385
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 447 E------------------LSGGEKIRL---RwAQLVNTDynLLVLDEPTNHLDIDAKEIIEDALLD----FNGTIITVS 501
Cdd:COG1123 386 EllervglppdladrypheLSGGQRQRVaiaR-ALALEPK--LLILDEPTSALDVSVQAQILNLLRDlqreLGLTYLFIS 462
|
..
gi 488409350 502 HD 503
Cdd:COG1123 463 HD 464
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
334-522 |
1.67e-31 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.10 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 334 EMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------TASNLKIGYLSQH-EFE 405
Cdd:cd03235 1 EVEDLTVSYGGhPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRrSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 406 RD----GNDTLLHTFRKKVNvsedqarhilaHFMFYGKDVFKKVN-----------------ELSGGEKIRLRWAQLVNT 464
Cdd:cd03235 81 RDfpisVRDVVLMGLYGHKG-----------LFRRLSKADKAKVDealervglseladrqigELSGGQQQRVLLARALVQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 465 DYNLLVLDEPTNHLDIDAKEIIEDALLDFNG---TIITVSHDRYFLNKLFNTTYLLkNKTL 522
Cdd:cd03235 150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRRegmTILVVTHDLGLVLEYFDRVLLL-NRTV 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
4-234 |
2.79e-31 |
|
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: 120.28 E-value: 2.79e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkkdikigylNQIPDYEKSESV 83
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLW---------NGEPIRDAREDY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIKSVFkELDTISKQLeTIetkmieeRENINSLVARYGELQTyyeenggyeiDAKIRKVTHGLNIAHLLKAKWGDLSG 163
Cdd:COG4133 74 RRRLAYLG-HADGLKPEL-TV-------RENLRFWAALYGLRAD----------REAIDEALEAVGLAGLADLPVRQLSA 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSHDRYFLDETvnQIIEIDQKK 234
Cdd:COG4133 135 GQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIaahLARGGAVLLTTHQPLELAAA--RVLDLGDFK 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
8-524 |
8.23e-29 |
|
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: 119.91 E-value: 8.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGME--RPSTGVISWKKDI--KIGYLnQIPdyekSESV 83
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHVALceKCGYV-ERP----SKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIK--SVFKELDTISKQLETIETKMIEERENI--NSLVARYGElQTYYE------ENGGYEIDAKIRK-------VTH 146
Cdd:TIGR03269 80 EPCPVcgGTLEPEEVDFWNLSDKLRRRIRKRIAImlQRTFALYGD-DTVLDnvlealEEIGYEGKEAVGRavdliemVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 147 GLNIAHLLKakwgDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEW----LASYIKNNDSATVIVSHdryflde 222
Cdd:TIGR03269 159 SHRITHIAR----DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLvhnaLEEAVKASGISMVLTSH------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 223 tVNQIIEidqkklhfyngnysyfvEERDKRLLIEfeayktqQKKIKKMKESIKQLRTWASQAKppnaaMFRRAKSMEKAl 302
Cdd:TIGR03269 228 -WPEVIE-----------------DLSDKAIWLE-------NGEIKEEGTPDEVVAVFMEGVS-----EVEKECEVEVG- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 303 NRIQRLEkpllDSKKMHITLEEGmnvsnrviemenVTKAYDdvlfrNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS 382
Cdd:TIGR03269 277 EPIIKVR----NVSKRYISVDRG------------VVKAVD-----NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 383 IDKGSI------------KTASNLK------IGYLSQhEF----ERDGNDTL-----------------LHTFrKKVNVS 423
Cdd:TIGR03269 336 PTSGEVnvrvgdewvdmtKPGPDGRgrakryIGILHQ-EYdlypHRTVLDNLteaiglelpdelarmkaVITL-KMVGFD 413
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 424 EDQARHILAhfmfygkdvfKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLD----IDAKEIIEDALLDFNGTIIT 499
Cdd:TIGR03269 414 EEKAEEILD----------KYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpitkVDVTHSILKAREEMEQTFII 483
|
570 580
....*....|....*....|....*
gi 488409350 500 VSHDRYFLNKLFNTTYLLKNKTLEK 524
Cdd:TIGR03269 484 VSHDMDFVLDVCDRAALMRDGKIVK 508
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-216 |
1.03e-28 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 114.37 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI----------KIGYL 71
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgRDLaslsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 NQIPDYEKSESVYQciksvfkeldtiskqletietkmieereninsLVA--RY---GELQTYYEENggyeiDAKIRKVTH 146
Cdd:COG1120 81 PQEPPAPFGLTVRE--------------------------------LVAlgRYphlGLFGRPSAED-----REAVEEALE 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 147 GLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHD 216
Cdd:COG1120 124 RTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHqlevLELLRRLARERGRTVVMVLHD 197
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-253 |
1.38e-28 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 119.45 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIPDYEKSE 81
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETVKLAYVDQSRDALDPN 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqciKSVFKEldtISKQLETIetkMIEEREnINS--LVARYGElqtyyeeNGGyeiDAKiRKVthglniahllkakwG 159
Cdd:PRK11819 403 ------KTVWEE---ISGGLDII---KVGNRE-IPSraYVGRFNF-------KGG---DQQ-KKV--------------G 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 160 DLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQII--EIDQKkLHF 237
Cdd:PRK11819 445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPGCAVVISHDRWFLDRIATHILafEGDSQ-VEW 523
|
250
....*....|....*.
gi 488409350 238 YNGNYSYFVEERDKRL 253
Cdd:PRK11819 524 FEGNFQEYEEDKKRRL 539
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
334-519 |
4.48e-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: 109.64 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 334 EMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIktasnlkigylsqhefERDGNDTL 412
Cdd:cd00267 1 EIENLSFRYGGrTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEI----------------LIDGKDIA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 413 LHTFRKkvnvsedQARHILAhfmfygkdvfkkVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLD 492
Cdd:cd00267 65 KLPLEE-------LRRRIGY------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRE 125
|
170 180 190
....*....|....*....|....*....|
gi 488409350 493 FNG---TIITVSHDRYFLNKLFNTTYLLKN 519
Cdd:cd00267 126 LAEegrTVIIVTHDPELAELAADRVIVLKD 155
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-222 |
1.79e-27 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 110.54 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTG--------VISWKKDIK--IGYLNQ 73
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGevrvlgedVARDPAEVRrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 74 IPDYEKSESVyqciksvfkeldtiskqletietkmieeRENINsLVAR-YGelqtyyeeNGGYEIDAKIRKVTHGLNIAH 152
Cdd:COG1131 81 EPALYPDLTV----------------------------RENLR-FFARlYG--------LPRKEARERIDELLELFGLTD 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409350 153 LLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIVS-HDryfLDE 222
Cdd:COG1131 124 AADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRelAAEGKTVLLStHY---LEE 193
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-234 |
3.74e-27 |
|
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: 108.71 E-value: 3.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKY--TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIKigylnqipdYEKSESV 83
Cdd:cd03225 3 KNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgKDLT---------KLSLKEL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIKSVFKELDTiskQLetIETKMIEEreninslVARYGELQTYYEEnggyEIDAKIRKVTHGLNIAHLLKAKWGDLSG 163
Cdd:cd03225 74 RRKVGLVFQNPDD---QF--FGPTVEEE-------VAFGLENLGLPEE----EIEERVEEALELVGLEGLRDRSPFTLSG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVI-VSHDRYFLDETVNQIIEIDQKK 234
Cdd:cd03225 138 GQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKklKAEGKTIIiVTHDLDLLLELADRVIVLEDGK 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-237 |
5.52e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.33 E-value: 5.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW------KKDIKIGYLNQI 74
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkpprRARRRIGYVPQR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 PDYEKSE--SVYQCI-------KSVFKELDTiskqletietkmiEEREninslvarygelqtyyeenggyEIDAKIRKVt 145
Cdd:COG1121 84 AEVDWDFpiTVRDVVlmgrygrRGLFRRPSR-------------ADRE----------------------AVDEALERV- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 146 hglNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVI-VSHDRYFLDE 222
Cdd:COG1121 128 ---GLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRelRREGKTILvVTHDLGAVRE 204
|
250
....*....|....*
gi 488409350 223 TVNQIIEIDQKKLHF 237
Cdd:COG1121 205 YFDRVLLLNRGLVAH 219
|
|
| ABC_tran_Xtn |
pfam12848 |
ABC transporter; This domain is an extension of some members of pfam00005 and other ... |
228-320 |
1.09e-25 |
|
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: 100.34 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 228 IEIDQKKLHFYNGNYSYFVEERDKRLLIEFEAYKTQQKKIKKMKESIKQLRTWASQAKppnaamfrRAKSMEKALNRIQR 307
Cdd:pfam12848 1 VELERGKLTTYKGNYSTFLEQKEERLEQQEKAYEKQQKEIKKLEEFIDRFRAKASKAK--------QAQSRIKALEKMER 72
|
90
....*....|...
gi 488409350 308 LEKPLLDSKKMHI 320
Cdd:pfam12848 73 IEKPERDKPKLRF 85
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
6-216 |
1.09e-25 |
|
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: 103.67 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 6 ASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI--------SWK-KDI--KIGYLNQI 74
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgkdlaSLSpKELarKIAYVPQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 pdyeksesvyqciksvfkeldtiskqLETietkmieereninslvarygelqtyyeenggyeidakirkvthgLNIAHLL 154
Cdd:cd03214 82 --------------------------LEL--------------------------------------------LGLAHLA 91
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 155 KAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHD 216
Cdd:cd03214 92 DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHqielLELLRRLARERGKTVVMVLHD 157
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
332-535 |
1.31e-25 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 105.32 E-value: 1.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------KTASNL----KIGYLS 400
Cdd:COG4555 1 MIEVENLSKKYGKVPaLKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgedVRKEPRearrQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 401 QhEFERDGNDTLLHTFR-----KKVNVSEDQAR-HILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEP 474
Cdd:COG4555 81 D-ERGLYDRLTVRENIRyfaelYGLFDEELKKRiEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 475 TNHLDIDAKEIIEDALLDF---NGTIITVSHDRYFLNKLFNTTYLLKNKTLeKFEGNYDYIKEK 535
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDRVVILHKGKV-VAQGSLDELREE 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-237 |
2.42e-25 |
|
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: 104.34 E-value: 2.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDI-LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI----------KIGYL 71
Cdd:COG1122 1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgKDItkknlrelrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 NQIPDYeksesvyqciksvfkeldtiskQL--ETIEtkmiEEreninslVArYGeLqtyyeENGGY---EIDAKIRKVTH 146
Cdd:COG1122 81 FQNPDD----------------------QLfaPTVE----ED-------VA-FG-P-----ENLGLpreEIRERVEEALE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 147 GLNIAHLLKAKWGDLSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVI-VSHDRYFLDE 222
Cdd:COG1122 121 LVGLEHLADRPPHELSGGQKQRVAIAGVLAmEP-EVLVLDEPTAGLDPRGRRELLELLKrlNKEGKTVIiVTHDLDLVAE 199
|
250
....*....|....*
gi 488409350 223 TVNQIIEIDQKKLHF 237
Cdd:COG1122 200 LADRVIVLDDGRIVA 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
334-522 |
2.75e-25 |
|
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: 102.51 E-value: 2.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 334 EMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLK-------IGYLSQ 401
Cdd:cd03214 1 EVENLSVGYGGrTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEIlldgKDLASLSpkelarkIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 heferdgndtLLhtfrKKVNVSEdqarhiLAHfmfygkdvfKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDID 481
Cdd:cd03214 81 ----------AL----ELLGLAH------LAD---------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 482 AK----EIIEDALLDFNGTIITVSHDryfLN---KLFNTTYLLKNKTL 522
Cdd:cd03214 132 HQiellELLRRLARERGKTVVMVLHD---LNlaaRYADRVILLKDGRI 176
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-235 |
4.78e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 102.97 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI----------KIGYLN 72
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgKPLsampppewrrQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 73 QIPD-YEksESVYQciksVFKELDTISKQLETietkmieeRENINSLVARYGelqtyyeenggyeidakirkvthgLNiA 151
Cdd:COG4619 81 QEPAlWG--GTVRD----NLPFPFQLRERKFD--------RERALELLERLG------------------------LP-P 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 152 HLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHDRYFLDETVNQI 227
Cdd:COG4619 122 DILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENtrrvEELLREYLAEEGRAVLWVSHDPEQIERVADRV 201
|
....*...
gi 488409350 228 IEIDQKKL 235
Cdd:COG4619 202 LTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
333-519 |
6.53e-25 |
|
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: 101.32 E-value: 6.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK----------TASNLKIGYLSQ 401
Cdd:cd03230 1 IEVRNLSKRYGKKTaLDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKvlgkdikkepEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 heferdgndtllhtfrkkvnvsedqarhilaHFMFY----GKDVFKkvneLSGGEKIRLRWAQLVNTDYNLLVLDEPTNH 477
Cdd:cd03230 81 -------------------------------EPSLYenltVRENLK----LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488409350 478 LDIDAKEIIEDALLDFN---GTIITVSHDRYFLNKLFNTTYLLKN 519
Cdd:cd03230 126 LDPESRREFWELLRELKkegKTILLSSHILEEAERLCDRVAILNN 170
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-235 |
7.72e-25 |
|
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: 100.94 E-value: 7.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDI---------KIGYLNQ 73
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVlGKDIkkepeevkrRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 74 IPDYEKSESVyqciksvfkeldtiskqletietkmieeRENInslvarygelqtyyeenggyeidakirkvthglniahl 153
Cdd:cd03230 81 EPSLYENLTV----------------------------RENL-------------------------------------- 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 154 lkakwgDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIV-SHDRYFLDETVNQIIEI 230
Cdd:cd03230 95 ------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRelKKEGKTILLsSHILEEAERLCDRVAIL 168
|
....*
gi 488409350 231 DQKKL 235
Cdd:cd03230 169 NNGRI 173
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-242 |
9.64e-25 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 107.67 E-value: 9.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQ--IPDYEK 79
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQdhAYDFEN 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SESVYQCIkSVFKeldtiskqletietkmiEERENINSLVARYGELQTyyeenGGYEIDAKIrKVthglniahllkakwg 159
Cdd:PRK15064 398 DLTLFDWM-SQWR-----------------QEGDDEQAVRGTLGRLLF-----SQDDIKKSV-KV--------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 160 dLSGGERTKVGIAQ-MLIKPtDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHFY 238
Cdd:PRK15064 439 -LSGGEKGRMLFGKlMMQKP-NVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDF 516
|
....
gi 488409350 239 NGNY 242
Cdd:PRK15064 517 SGTY 520
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-239 |
1.35e-24 |
|
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: 101.46 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 6 ASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIS------WKKDIKIGYLNQIPDYEK 79
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRvfgkplEKERKRIGYVPQRRSIDR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SE--SVYQCIKSvfkeldtiskqletietkmieereninSLVARYGELQTYYEEnggyeidaKIRKVTHGL---NIAHLL 154
Cdd:cd03235 82 DFpiSVRDVVLM---------------------------GLYGHKGLFRRLSKA--------DKAKVDEALervGLSELA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 155 KAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVI-VSHDRYFLDETVNQIIEID 231
Cdd:cd03235 127 DRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRelRREGMTILvVTHDLGLVLEYFDRVLLLN 206
|
....*...
gi 488409350 232 qKKLHFYN 239
Cdd:cd03235 207 -RTVVASG 213
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-315 |
1.48e-24 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 107.56 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYL--NQIPDYEKS 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGIKLGYFaqHQLEFLRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 ESVYQciksvfkeldtiskQLETIETKMIEEreninslvarygELQTYYeenGGYEIDAKirKVTHglniahllkaKWGD 160
Cdd:PRK10636 392 ESPLQ--------------HLARLAPQELEQ------------KLRDYL---GGFGFQGD--KVTE----------ETRR 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHFYNG 240
Cdd:PRK10636 431 FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFDG 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 241 ---NYSYFV------EERDKRLLIEFEAYKTQQKKIKKMKESikQLRTwasQAKPPNAAMFRRAKSMEKALNRIQRLEKP 311
Cdd:PRK10636 511 dleDYQQWLsdvqkqENQTDEAPKENNANSAQARKDQKRREA--ELRT---QTQPLRKEIARLEKEMEKLNAQLAQAEEK 585
|
....
gi 488409350 312 LLDS 315
Cdd:PRK10636 586 LGDS 589
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-221 |
2.76e-24 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 106.82 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 25 TLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkkDIKIGYLNQI--PDYEksESVYQCIKSVFKELDTiskqle 102
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQYikPDYD--GTVEDLLRSITDDLGS------ 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 103 tietkmieereninslvarygelqTYYEEnggyEIdakirkvTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLL 182
Cdd:PRK13409 431 ------------------------SYYKS----EI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488409350 183 LLDEPTNHLDV-------KSIEwlaSYIKNNDSATVIVSHDRYFLD 221
Cdd:PRK13409 476 LLDEPSAHLDVeqrlavaKAIR---RIAEEREATALVVDHDIYMID 518
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
8-217 |
5.34e-24 |
|
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: 99.90 E-value: 5.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDI--------KIGYLNQipDYe 78
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdGRDVtgvpperrNIGMVFQ--DY- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 79 ksesvyqcikSVFKELdtiskqleTIEtkmieerENInslvaRYG-ELQTYYEEnggyEIDAKIRKVTHGLNIAHLLKAK 157
Cdd:cd03259 82 ----------ALFPHL--------TVA-------ENI-----AFGlKLRGVPKA----EIRARVRELLELVGLEGLLNRY 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 158 WGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHDR 217
Cdd:cd03259 128 PHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLreelREELKELQRELGITTIYVTHDQ 191
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
347-476 |
1.32e-23 |
|
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: 96.95 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 347 FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK-----------TASNLKIGYLSQHE--------FERD 407
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILldgqdltdderKSLRKEIGYVFQDPqlfprltvRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 408 GNDTLLHTFRKKvnVSEDQARHILAHFMFYGKD---VFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTN 476
Cdd:pfam00005 81 RLGLLLKGLSKR--EKDARAEEALEKLGLGDLAdrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
333-503 |
1.35e-23 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 99.37 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI--------KTASNLK--IGYLSQ 401
Cdd:COG1131 1 IEVRGLTKRYGDKTaLDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVrvlgedvaRDPAEVRrrIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 HEF---ERDGNDTLLHT---FRKKVNVSEDQARHILAHFMFYGK-DvfKKVNELSGGEKIRLRWAQ-LVNtDYNLLVLDE 473
Cdd:COG1131 81 EPAlypDLTVRENLRFFarlYGLPRKEARERIDELLELFGLTDAaD--RKVGTLSGGMKQRLGLALaLLH-DPELLILDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 488409350 474 PTNHLDIDAKEIIEDALLDFNG---TIITVSHD 503
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAegkTVLLSTHY 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-508 |
2.06e-23 |
|
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: 104.10 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 28 SGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI----SWKKDIKigylnqipDYEKSEsvyqcIKSVFKELdtISKQLET 103
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepSWDEVLK--------RFRGTE-----LQDYFKKL--ANGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 104 -IETKMIEereninsLVARY-----GELQTYYEENGgyeidaKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIK 177
Cdd:COG1245 163 aHKPQYVD-------LIPKVfkgtvRELLEKVDERG------KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLR 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 178 PTDLLLLDEPTNHLDVKSIEWLASYIK---NNDSATVIVSHDRYFLD---ETVNQI-----------------IEIDQkk 234
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIRelaEEGKYVLVVEHDLAILDylaDYVHILygepgvygvvskpksvrVGINQ-- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 235 lhFYNGnysYFVEE----RDKRllIEFEayktqqkkikkmkesikqlrtwasqAKPPnaamfRRAKSMEKalnriqrlek 310
Cdd:COG1245 308 --YLDG---YLPEEnvriRDEP--IEFE-------------------------VHAP-----RREKEEET---------- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 311 plldskkmhitleegmnvsnrVIEMENVTKAYDDvlFRnvnmL------IRRGEHVAIIGDNGTGKTTLLKIILGLTSID 384
Cdd:COG1245 341 ---------------------LVEYPDLTKSYGG--FS----LeveggeIREGEVLGIVGPNGIGKTTFAKILAGVLKPD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 385 KGSIKTasNLKIGYLSQ---HEFERDGNDTLLHTFRKKVNVS---EDQARHILAHFMFYgkdvfKKVNELSGGEKIRLRW 458
Cdd:COG1245 394 EGEVDE--DLKISYKPQyisPDYDGTVEEFLRSANTDDFGSSyykTEIIKPLGLEKLLD-----KNVKDLSGGELQRVAI 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 459 AQLVNTDYNLLVLDEPTNHLDID-----AKeIIEDALLDFNGTIITVSHDRYFLN 508
Cdd:COG1245 467 AACLSRDADLYLLDEPSAHLDVEqrlavAK-AIRRFAENRGKTAMVVDHDIYLID 520
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-221 |
2.21e-23 |
|
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: 104.10 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 25 TLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkKDIKIGYLNQ--IPDYEksESVYQCIKSVFKEldtiskqle 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--EDLKISYKPQyiSPDYD--GTVEEFLRSANTD--------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 103 TIETKMieereninslvarygelqtYYEEnggyeidakirkVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLL 182
Cdd:COG1245 429 DFGSSY-------------------YKTE------------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLY 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488409350 183 LLDEPTNHLDV-------KSIEwlaSYIKNNDSATVIVSHDRYFLD 221
Cdd:COG1245 478 LLDEPSAHLDVeqrlavaKAIR---RFAENRGKTAMVVDHDIYLID 520
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
333-522 |
2.42e-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: 98.56 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTasnlkigylsqheferDGND 410
Cdd:COG1122 1 IELENLSFSYPGgtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLV----------------DGKD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 411 TL---LHTFRKKV---------------------------NVSEDQARHI---------LAHFmfygKDvfKKVNELSGG 451
Cdd:COG1122 65 ITkknLRELRRKVglvfqnpddqlfaptveedvafgpenlGLPREEIRERveealelvgLEHL----AD--RPPHELSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 452 EKirlrwaQLV--------NTDYnlLVLDEPTNHLDIDAKEIIEDALLDFNG---TIITVSHDRYFLNKLFNTTYLLKNK 520
Cdd:COG1122 139 QK------QRVaiagvlamEPEV--LVLDEPTAGLDPRGRRELLELLKRLNKegkTVIIVTHDLDLVAELADRVIVLDDG 210
|
..
gi 488409350 521 TL 522
Cdd:COG1122 211 RI 212
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-189 |
3.74e-23 |
|
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: 95.41 E-value: 3.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 19 FDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkkdikigylnqipdyEKSESVYQCIKSVFKELDTIS 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILL---------------DGQDLTDDERKSLRKEIGYVF 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 99 KQLETIETKMIeeRENInslvARYGELQTYYEEnggyEIDAKIRKVTHGLNIAHLLKAKWGD----LSGGERTKVGIAQM 174
Cdd:pfam00005 66 QDPQLFPRLTV--RENL----RLGLLLKGLSKR----EKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARA 135
|
170
....*....|....*
gi 488409350 175 LIKPTDLLLLDEPTN 189
Cdd:pfam00005 136 LLTKPKLLLLDEPTA 150
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-508 |
6.24e-23 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 102.58 E-value: 6.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 24 ITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTG----VISWKKDIKIGYLNQIPDYekSESVYQC-IKSVFK--ELDT 96
Cdd:PRK13409 94 PIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeEPSWDEVLKRFRGTELQNY--FKKLYNGeIKVVHKpqYVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 97 ISKQLEtietkmieereninslvARYGELQTYYEENGgyeidaKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLI 176
Cdd:PRK13409 172 IPKVFK-----------------GKVRELLKKVDERG------KLDEVVERLGLENILDRDISELSGGELQRVAIAAALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 177 KPTDLLLLDEPTNHLDV-------KSIEWLAsyiknNDSATVIVSHDRYFLD---ETVNqIIeidqkklhfYN--GNYSY 244
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIrqrlnvaRLIRELA-----EGKYVLVVEHDLAVLDylaDNVH-IA---------YGepGAYGV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 245 FveerdkrlliefeayktqqKKIKKMKESIKQ-LRTwasqakppnaamFRRAKSMekalnRIQRleKPLLDSKKMHITLE 323
Cdd:PRK13409 294 V-------------------SKPKGVRVGINEyLKG------------YLPEENM-----RIRP--EPIEFEERPPRDES 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 324 EGmnvsNRVIEMENVTKAYDDvlFR-NVNM-LIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTasNLKIGYLSQ 401
Cdd:PRK13409 336 ER----ETLVEYPDLTKKLGD--FSlEVEGgEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP--ELKISYKPQ 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 HeFERDGNDTLLHTFRK-KVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDI 480
Cdd:PRK13409 408 Y-IKPDYDGTVEDLLRSiTDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 486
|
490 500 510
....*....|....*....|....*....|....*.
gi 488409350 481 DA--------KEIIEdallDFNGTIITVSHDRYFLN 508
Cdd:PRK13409 487 EQrlavakaiRRIAE----EREATALVVDHDIYMID 518
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
334-519 |
9.40e-23 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 96.38 E-value: 9.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 334 EMENVTKAYDD---VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTasnlkigylsqheFERDGND 410
Cdd:cd03225 1 ELKNLSFSYPDgarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLV-------------DGKDLTK 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 411 TLLHTFRKKVNV----SEDQ--ARHI-------LAHFMFYGKDVFKKVNE-----------------LSGGEKIRLRWAQ 460
Cdd:cd03225 68 LSLKELRRKVGLvfqnPDDQffGPTVeeevafgLENLGLPEEEIEERVEEalelvgleglrdrspftLSGGQKQRVAIAG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 461 LVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG---TIITVSHDRYFLNKLFNTTYLLKN 519
Cdd:cd03225 148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAegkTIIIVTHDLDLLLELADRVIVLED 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-235 |
1.62e-22 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 96.02 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTED-----ILfDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTG-VISWKKDIkigylNQIPDY 77
Cdd:cd03255 1 IELKNLSKTYGGGgekvqAL-KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGeVRVDGTDI-----SKLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 78 EKSESVYQCIKSVFKELDTISKQleTIetkmieeRENInslvarygELQTYYEENGGYEIDAKIRKVTHGLNIAHLLKAK 157
Cdd:cd03255 75 ELAAFRRRHIGFVFQSFNLLPDL--TA-------LENV--------ELPLLLAGVPKKERRERAEELLERVGLGDRLNHY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 158 WGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHDRyFLDETVNQIIEIDQK 233
Cdd:cd03255 138 PSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETgkevMELLRELNKEAGTTIVVVTHDP-ELAEYADRIIELRDG 216
|
..
gi 488409350 234 KL 235
Cdd:cd03255 217 KI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
6-234 |
2.02e-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: 93.85 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 6 ASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKdikigylnqipdyeksesvyq 85
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 ciksvfkeldtiskqlETIETKMIEERENINSLVarygeLQtyyeenggyeidakirkvthglniahllkakwgdLSGGE 165
Cdd:cd00267 61 ----------------KDIAKLPLEELRRRIGYV-----PQ----------------------------------LSGGQ 85
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 166 RTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK---NNDSATVIVSHDRYFLDETVNQIIEIDQKK 234
Cdd:cd00267 86 RQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRelaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
332-503 |
2.97e-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: 95.88 E-value: 2.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNL-------KIGYL 399
Cdd:COG1120 1 MLEAENLSVGYGGrPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVlldgRDLASLsrrelarRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQHEfERDGN----DTLL-----HTFRKKVNVSEDQ--ARHILA-----HFmfygKDvfKKVNELSGGEKirlrwaQLV- 462
Cdd:COG1120 81 PQEP-PAPFGltvrELVAlgrypHLGLFGRPSAEDReaVEEALErtgleHL----AD--RPVDELSGGER------QRVl 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488409350 463 -------NTDynLLVLDEPTNHLDIDAK----EIIEDALLDFNGTIITVSHD 503
Cdd:COG1120 148 iaralaqEPP--LLLLDEPTSHLDLAHQlevlELLRRLARERGRTVVMVLHD 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
332-507 |
4.71e-22 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 94.08 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----------KTASNLKIGYLs 400
Cdd:COG4133 2 MLEAENLSCRRGErLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVlwngepirdaREDYRRRLAYL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 401 qheFERDG-NDTL-----LHTFR--KKVNVSEDQARHILAHFmfyG----KDvfKKVNELSGGEKIRLRWAQLVNTDYNL 468
Cdd:COG4133 81 ---GHADGlKPELtvrenLRFWAalYGLRADREAIDEALEAV---GlaglAD--LPVRQLSAGQKRRVALARLLLSPAPL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488409350 469 LVLDEPTNHLDIDAKEIIEDALLDFN---GTIITVSHDRYFL 507
Cdd:COG4133 153 WLLDEPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLEL 194
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
333-503 |
5.28e-22 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 99.91 E-value: 5.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD---VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL--KIGY 398
Cdd:COG2274 474 IELENVSFRYPGdspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILidgidlrqiDPASLrrQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQHE--FerdgNDTLLH--TFRKKvNVSEDQARH----------ILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNT 464
Cdd:COG2274 554 VLQDVflF----SGTIREniTLGDP-DATDEEIIEaarlaglhdfIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488409350 465 DYNLLVLDEPTNHLDIDAKEIIEDALLDFNG--TIITVSHD 503
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKgrTVIIIAHR 669
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-236 |
7.28e-22 |
|
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: 93.48 E-value: 7.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 6 ASNISKKYTEDI-LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDIK-------IGYLNQIPD 76
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLnGKPIKakerrksIGYVMQDVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 77 YEKSEsvyqciKSVFKELDTISKQLetietkmieereninslvarygelqtyyeenggYEIDAKIRKVTHGLNIAHLLKA 156
Cdd:cd03226 82 YQLFT------DSVREELLLGLKEL---------------------------------DAGNEQAETVLKDLDLYALKER 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 157 KWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK---NNDSATVIVSHDRYFLDETVNQIIEIDQK 233
Cdd:cd03226 123 HPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRelaAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
...
gi 488409350 234 KLH 236
Cdd:cd03226 203 AIV 205
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-230 |
4.51e-21 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 92.03 E-value: 4.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MN-ILNASNISKKYTE-----DILfDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI------- 66
Cdd:COG1136 1 MSpLLELRNLTKSYGTgegevTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgQDIsslsere 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 67 -------KIGYlnqipdyeksesVYQciksvfkeldtiSKQLetietkmIEE---RENInslvarygELQTYYEENGGYE 136
Cdd:COG1136 80 larlrrrHIGF------------VFQ------------FFNL-------LPEltaLENV--------ALPLLLAGVSRKE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 137 IDAKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVI 212
Cdd:COG1136 121 RRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTgeevLELLRELNRELGTTIVM 200
|
250
....*....|....*...
gi 488409350 213 VSHDRyFLDETVNQIIEI 230
Cdd:COG1136 201 VTHDP-ELAARADRVIRL 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
333-504 |
5.00e-21 |
|
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: 91.40 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD------VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNL-------- 394
Cdd:cd03255 1 IELKNLSKTYGGggekvqAL-KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVrvdgTDISKLsekelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 ---KIGYLSQHeFerdgndTLLHTF-------------RKKVNVSEDQARHIL-----AHFMfygkdvFKKVNELSGGEK 453
Cdd:cd03255 80 rrrHIGFVFQS-F------NLLPDLtalenvelplllaGVPKKERRERAEELLervglGDRL------NHYPSELSGGQQ 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 454 IRLRWAQ-LVNtDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG----TIITVSHDR 504
Cdd:cd03255 147 QRVAIARaLAN-DPKIILADEPTGNLDSETGKEVMELLRELNKeagtTIVVVTHDP 201
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
333-503 |
6.53e-21 |
|
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: 91.79 E-value: 6.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKtASNLKIGYLSQHEFERdgndt 411
Cdd:cd03261 1 IELRGLTKSFGGrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL-IDGEDISGLSEAELYR----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 llhtFRKKV-------------NVSEDQARHILAHFMFYGKDVFKKVN-----------------ELSGGEKIRLRWAQL 461
Cdd:cd03261 75 ----LRRRMgmlfqsgalfdslTVFENVAFPLREHTRLSEEEIREIVLekleavglrgaedlypaELSGGMKKRVALARA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488409350 462 VNTDYNLLVLDEPTNHLDIDAKEIIEDALLD----FNGTIITVSHD 503
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIASGVIDDLIRSlkkeLGLTSIMVTHD 196
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
8-236 |
7.46e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 91.27 E-value: 7.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDIL-FDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW---------KKDI-----KIGYLN 72
Cdd:COG2884 6 NVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVngqdlsrlkRREIpylrrRIGVVF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 73 Q----IPDyeksesvyqciKSVFkeldtiskqletietkmieerENInSLVARYgelqTYYEENggyEIDAKIRKVTHGL 148
Cdd:COG2884 86 QdfrlLPD-----------RTVY---------------------ENV-ALPLRV----TGKSRK---EIRRRVREVLDLV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 149 NIAHLLKAKWGDLSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIV-SHDRYFLDETV 224
Cdd:COG2884 126 GLSDKAKALPHELSGGEQQRVAIARALVnRP-ELLLADEPTGNLDPETSWEIMELLEeiNRRGTTVLIaTHDLELVDRMP 204
|
250
....*....|..
gi 488409350 225 NQIIEIDQKKLH 236
Cdd:COG2884 205 KRVLELEDGRLV 216
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-215 |
2.05e-20 |
|
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: 90.53 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTG-VIS-----------WkkDIK- 67
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRlfgerrggedvW--ELRk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 68 -IGYLNQ--IPDYEKSESVYQCIKSVFkeLDTIskqletietkmieereninslvARYGElqtyYEEnggyEIDAKIRKV 144
Cdd:COG1119 79 rIGLVSPalQLRFPRDETVLDVVLSGF--FDSI----------------------GLYRE----PTD----EQRERAREL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 145 THGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSH 215
Cdd:COG1119 127 LELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGArellLALLDKLAAEGAPTLVLVTH 201
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
333-503 |
3.11e-20 |
|
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: 94.05 E-value: 3.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK----TASNL-------KIGYL 399
Cdd:COG4988 337 IELEDVSFSYPGgrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILingvDLSDLdpaswrrQIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQHEF-------------ERDGNDTLLHTFRKKVNVSE--DQARHILAHfmfygkdvfkKVNE----LSGGEKIRLRWAQ 460
Cdd:COG4988 417 PQNPYlfagtirenlrlgRPDASDEELEAALEAAGLDEfvAALPDGLDT----------PLGEggrgLSGGQAQRLALAR 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488409350 461 LVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSHD 503
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLakGRTVILITHR 531
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
332-534 |
3.75e-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: 89.65 E-value: 3.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTAsNLKIGYLSQHEFERdgnd 410
Cdd:COG1127 5 MIEVRNLTKSFGDrVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVD-GQDITGLSEKELYE---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 411 tllhtFRKKV-----------------NV----------SEDQARHI---------LAHFMfygkdvFKKVNELSGGEKI 454
Cdd:COG1127 80 -----LRRRIgmlfqggalfdsltvfeNVafplrehtdlSEAEIRELvleklelvgLPGAA------DKMPSELSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 455 RL---RwAqLVnTDYNLLVLDEPTNHLDIDAKEIIEDALLD----FNGTIITVSHDryfLNKLFNTT---YLLKNKTLEk 524
Cdd:COG1127 149 RValaR-A-LA-LDPEILLYDEPTAGLDPITSAVIDELIRElrdeLGLTSVVVTHD---LDSAFAIAdrvAVLADGKII- 221
|
250
....*....|
gi 488409350 525 FEGNYDYIKE 534
Cdd:COG1127 222 AEGTPEELLA 231
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
332-502 |
3.78e-20 |
|
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: 89.76 E-value: 3.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKII------------------LGLTSIDKgsIKTas 392
Cdd:COG1119 3 LLELRNVTVRRGGkTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdlpptygndvrlfgerRGGEDVWE--LRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 393 nlKIGYLS---QHEFERdgNDTLLHT-----------FRKkvnVSEDQ---ARHILAHF-MFYGKDvfKKVNELSGGEKI 454
Cdd:COG1119 79 --RIGLVSpalQLRFPR--DETVLDVvlsgffdsiglYRE---PTDEQrerARELLELLgLAHLAD--RPFGTLSQGEQR 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 455 RLRWAQ-LVnTDYNLLVLDEPTNHLDIDAKE----IIEDALLDFNGTIITVSH 502
Cdd:COG1119 150 RVLIARaLV-KDPELLILDEPTAGLDLGARElllaLLDKLAAEGAPTLVLVTH 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-237 |
5.38e-20 |
|
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: 88.40 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGdTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIK---------IGYLNQ 73
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDgQDVLkqpqklrrrIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 74 IPDYEKSESVYQCiksvfkeLDTISKqLETIETKMIEEReninslvarygelqtyyeenggyeIDAKIRKVthglNIAHL 153
Cdd:cd03264 80 EFGVYPNFTVREF-------LDYIAW-LKGIPSKEVKAR------------------------VDEVLELV----NLGDR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 154 LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN-NDSATVIVS-HDRYFLDETVNQIIEID 231
Cdd:cd03264 124 AKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSElGEDRIVILStHIVEDVESLCNQVAVLN 203
|
....*.
gi 488409350 232 QKKLHF 237
Cdd:cd03264 204 KGKLVF 209
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
333-502 |
6.38e-20 |
|
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: 87.27 E-value: 6.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD---VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI--------KTASNLK---IGY 398
Cdd:cd03246 1 LEVENVSFRYPGaepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNELgdhVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQheferdgNDTLLhtfrkKVNVSEdqarhilahfmfygkdvfkkvNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHL 478
Cdd:cd03246 81 LPQ-------DDELF-----SGSIAE---------------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 488409350 479 DIDAKEIIEDALLDFN---GTIITVSH 502
Cdd:cd03246 128 DVEGERALNQAIAALKaagATRIVIAH 154
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
331-504 |
9.67e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 92.35 E-value: 9.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 331 RVIEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNLK--IG 397
Cdd:TIGR02857 320 SSLEFSGVSVAYPGrrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAvngvpladaDADSWRdqIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 YLSQHEF-------------ERDGNDTLLHTFRKKVNVSE-DQARHILAHFMFyGKDvfkkVNELSGGEKIRLRWAQLVN 463
Cdd:TIGR02857 400 WVPQHPFlfagtiaenirlaRPDASDAEIREALERAGLDEfVAALPQGLDTPI-GEG----GAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488409350 464 TDYNLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSHDR 504
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRALaqGRTVLLVTHRL 517
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
333-520 |
1.08e-19 |
|
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: 86.05 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQHEFERDGnd 410
Cdd:cd03223 1 IELENLSLATPDgrVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGEDLLFLPQRPYLPLG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 411 TLlhtfrkkvnvsedqaRHILAhfmfYGKDvfkkvNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDAL 490
Cdd:cd03223 79 TL---------------REQLI----YPWD-----DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL 134
|
170 180 190
....*....|....*....|....*....|
gi 488409350 491 LDFNGTIITVSHdRYFLNKLFNTTYLLKNK 520
Cdd:cd03223 135 KELGITVISVGH-RPSLWKFHDRVLDLDGE 163
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
332-503 |
1.10e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.79 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD------VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNL------- 394
Cdd:COG1136 4 LLELRNLTKSYGTgegevtAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVlidgQDISSLserelar 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 ----KIGYLSQheferDGNdtLLHTF-------------RKKVNVSEDQARHILAHFMFYGKdVFKKVNELSGGEKIRL- 456
Cdd:COG1136 83 lrrrHIGFVFQ-----FFN--LLPELtalenvalplllaGVSRKERRERARELLERVGLGDR-LDHRPSQLSGGQQQRVa 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 457 --RwAqLVNtDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG----TIITVSHD 503
Cdd:COG1136 155 iaR-A-LVN-RPKLILADEPTGNLDSKTGEEVLELLRELNRelgtTIVMVTHD 204
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
333-519 |
1.30e-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: 86.47 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVLF-RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIktasnlkigylsqhEFerdgNDT 411
Cdd:cd03229 1 LELKNVSKRYGQKTVlNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSI--------------LI----DGE 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 LLHTFRKKVNVSEDQARHILAHF-MFYGKDVFKKVNE-LSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDA 489
Cdd:cd03229 63 DLTDLEDELPPLRRRIGMVFQDFaLFPHLTVLENIALgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRAL 142
|
170 180 190
....*....|....*....|....*....|....
gi 488409350 490 LLD----FNGTIITVSHDRYFLNKLFNTTYLLKN 519
Cdd:cd03229 143 LKSlqaqLGITVVLVTHDLDEAARLADRVVVLRD 176
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-235 |
1.92e-19 |
|
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: 91.82 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTED--ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKI-GY-LNQIPdyekSES 82
Cdd:COG2274 477 ENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG------RILIdGIdLRQID----PAS 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 VYQCIKSVFKEL----DTIskqletietkmieeRENInSLVARYGELQTYYE--ENGGyeIDAKIRKVTHGLNiaHLLKA 156
Cdd:COG2274 547 LRRQIGVVLQDVflfsGTI--------------RENI-TLGDPDATDEEIIEaaRLAG--LHDFIEALPMGYD--TVVGE 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 157 KWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNndSATVIVSHDRYFLDEtVNQIIEIDQ 232
Cdd:COG2274 608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETeaiiLENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDK 684
|
...
gi 488409350 233 KKL 235
Cdd:COG2274 685 GRI 687
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
332-510 |
1.96e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.03 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTA----SNLK---------- 395
Cdd:COG2884 1 MIRFENVSKRYPGgrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlSRLKrreipylrrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 396 IGYLSQhEFErdgndtLLhtFRKKV--NVS-------------EDQARHILAHFMFYGKDvFKKVNELSGGEKIRLRWAQ 460
Cdd:COG2884 81 IGVVFQ-DFR------LL--PDRTVyeNVAlplrvtgksrkeiRRRVREVLDLVGLSDKA-KALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 461 -LVNtdyN--LLVLDEPTNHLDIDAKEIIEDALLDFN--G-TIITVSHDRYFLNKL 510
Cdd:COG2884 151 aLVN---RpeLLLADEPTGNLDPETSWEIMELLEEINrrGtTVLIATHDLELVDRM 203
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
333-503 |
2.10e-19 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 86.76 E-value: 2.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-----VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------KTASNLKIGYLSQ 401
Cdd:cd03293 1 LEVRNVSKTYGGgggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlvdgepVTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 heferdgNDTLL--HTFRKKV-------NVSEDQARHILAHFM-FYG-KDVFKKV-NELSGGEKIRLRWAQLVNTDYNLL 469
Cdd:cd03293 81 -------QDALLpwLTVLDNValglelqGVPKAEARERAEELLeLVGlSGFENAYpHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 470 VLDEPTNHLDIDAKEIIEDALLD----FNGTIITVSHD 503
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDiwreTGKTVLLVTHD 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-235 |
2.18e-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: 91.37 E-value: 2.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTED--ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDIK----------IGY 70
Cdd:COG4987 334 LELEDVSFRYPGAgrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLRdldeddlrrrIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 71 LNQipdyekseSVYqciksVFkeLDTIskqletietkmieeRENInsLVARygelqtyyeENGGyeiDAKIRKVTHGLNI 150
Cdd:COG4987 414 VPQ--------RPH-----LF--DTTL--------------RENL--RLAR---------PDAT---DEELWAALERVGL 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 151 AHLLKAK------W-GD----LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVIVSHDR 217
Cdd:COG4987 451 GDWLAALpdgldtWlGEggrrLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEalAGRTVLLITHRL 530
|
250
....*....|....*...
gi 488409350 218 YFLdETVNQIIEIDQKKL 235
Cdd:COG4987 531 AGL-ERMDRILVLEDGRI 547
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-221 |
2.80e-19 |
|
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: 87.46 E-value: 2.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 25 TLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDiKIGYLNQ--IPDYEKSesVYQCIKSVFKELDTiskqle 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD-TVSYKPQyiKADYEGT--VRDLLSSITKDFYT------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 103 tietkmieereninslvarygelQTYYEEnggyeidakirKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLL 182
Cdd:cd03237 92 -----------------------HPYFKT-----------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIY 137
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488409350 183 LLDEPTNHLDVKSIEWLASYIK----NNDSATVIVSHDRYFLD 221
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRrfaeNNEKTAFVVEHDIIMID 180
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
341-503 |
3.64e-19 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 341 AYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQHEferDGNDTLLHTFRKK 419
Cdd:NF040873 1 GYGGrPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQRS---EVPDSLPLTVRDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 420 VNVS-------------EDQARhILAHFMFYGKDVFKK--VNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKE 484
Cdd:NF040873 78 VAMGrwarrglwrrltrDDRAA-VDDALERVGLADLAGrqLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRE 156
|
170 180
....*....|....*....|..
gi 488409350 485 IIEDALLDFNG---TIITVSHD 503
Cdd:NF040873 157 RIIALLAEEHArgaTVVVVTHD 178
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
333-502 |
4.17e-19 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 86.10 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD---VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNLK--IGY 398
Cdd:cd03245 3 IEFRNVSFSYPNqeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLldgtdirqlDPADLRrnIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQHEFE-----RDgNDTLLHTFrkkvnvSEDQArhILAHFMFYGKDVFKK---------VNE----LSGGEKIRLRWAQ 460
Cdd:cd03245 83 VPQDVTLfygtlRD-NITLGAPL------ADDER--ILRAAELAGVTDFVNkhpngldlqIGErgrgLSGGQRQAVALAR 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488409350 461 LVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG--TIITVSH 502
Cdd:cd03245 154 ALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGdkTLIIITH 197
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
8-234 |
5.95e-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: 84.36 E-value: 5.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDI--LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDIK----------IGYLNQI 74
Cdd:cd03228 5 NVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIdGVDLRdldleslrknIAYVPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 PdyeksesvyqcikSVFKelDTIskqletietkmieeRENInslvarygelqtyyeenggyeidakirkvthglniahll 154
Cdd:cd03228 85 P-------------FLFS--GTI--------------RENI--------------------------------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 155 kakwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVIVSHdRYFLDETVNQIIEIDQ 232
Cdd:cd03228 97 ------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAlaKGKTVIVIAH-RLSTIRDADRIIVLDD 169
|
..
gi 488409350 233 KK 234
Cdd:cd03228 170 GR 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
346-522 |
6.23e-19 |
|
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: 85.39 E-value: 6.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 346 LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLK----IGYLSQHE----FERDGNDTLL 413
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIllngKPIKAKErrksIGYVMQDVdyqlFTDSVREELL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 414 HTfRKKVNVSEDQARHILAHFMFYGkdvFKKVN--ELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALL 491
Cdd:cd03226 95 LG-LKELDAGNEQAETVLKDLDLYA---LKERHplSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
|
170 180 190
....*....|....*....|....*....|....
gi 488409350 492 DFNG---TIITVSHDRYFLNKLFNTTYLLKNKTL 522
Cdd:cd03226 171 ELAAqgkAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-216 |
6.62e-19 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 88.21 E-value: 6.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIkigylNQIPdyek 79
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgRDV-----TDLP---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 sesvyqciksvfkeldtiskqletietkmIEEReNInSLVArygelQTY--Y-----EENGGY----------EIDAKIR 142
Cdd:COG3839 72 -----------------------------PKDR-NI-AMVF-----QSYalYphmtvYENIAFplklrkvpkaEIDRRVR 115
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 143 KVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS-----IEwLASYIKNNDSATVIVSHD 216
Cdd:COG3839 116 EAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAKLrvemrAE-IKRLHRRLGTTTIYVTHD 193
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
326-503 |
8.60e-19 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 86.30 E-value: 8.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 326 MNVSNRVIEMENVTKAYDD-----VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------TASNL 394
Cdd:COG1116 1 MSAAAPALELRGVSKRFPTggggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLvdgkpvTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 KIGYLSQheferdgNDTLLH--TFR-------KKVNVSEDQARHI---------LAHFMfygkDvfKKVNELSGGEKIRL 456
Cdd:COG1116 81 DRGVVFQ-------EPALLPwlTVLdnvalglELRGVPKAERRERarellelvgLAGFE----D--AYPHQLSGGMRQRV 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488409350 457 RWAQ-LVNtDYNLLVLDEPTNHLDIDAKEIIEDALLD----FNGTIITVSHD 503
Cdd:COG1116 148 AIARaLAN-DPEVLLMDEPFGALDALTRERLQDELLRlwqeTGKTVLFVTHD 198
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-205 |
1.17e-18 |
|
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: 85.29 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIK-----------IGYL 71
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDgQDITklpmhkrarlgIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 NQIPdyeksesvyqcikSVFKELdtiskqleTIEtkmieerENInSLVArygELQTYYEEnggyEIDAKIRKVTHGLNIA 151
Cdd:cd03218 81 PQEA-------------SIFRKL--------TVE-------ENI-LAVL---EIRGLSKK----EREEKLEELLEEFHIT 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488409350 152 HLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN 205
Cdd:cd03218 125 HLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI 178
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
298-502 |
1.22e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.19 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 298 MEKALNRIQRLEKPLLDSKKMHITLEEGMN-----VSNRVIEMENVTKAY-DDVLFRNVNMLIRRGEHVAIIGDNGTGKT 371
Cdd:PRK13536 2 LTRAVAEEAPRRLELSPIERKHQGISEAKAsipgsMSTVAIDLAGVSKSYgDKAVVNGLSFTVASGECFGLLGPNGAGKS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 372 TLLKIILGLTSIDKGSIKT----------ASNLKIGYLSQH---EFERDGNDTLL---HTFRKKVNVSEDQARHILaHFM 435
Cdd:PRK13536 82 TIARMILGMTSPDAGKITVlgvpvpararLARARIGVVPQFdnlDLEFTVRENLLvfgRYFGMSTREIEAVIPSLL-EFA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 436 FYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIED---ALLDFNGTIITVSH 502
Cdd:PRK13536 161 RLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWErlrSLLARGKTILLTTH 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
333-503 |
1.79e-18 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 88.67 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV---LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL--KIGY 398
Cdd:COG4987 334 LELEDVSFRYPGAgrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITlggvdlrdlDEDDLrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQ--HEFerdgNDTLLHTFR-KKVNVSEDQARHILahfmfygkdvfKKVN-----------------E----LSGGEKI 454
Cdd:COG4987 414 VPQrpHLF----DTTLRENLRlARPDATDEELWAAL-----------ERVGlgdwlaalpdgldtwlgEggrrLSGGERR 478
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488409350 455 RLRWAQLVNTDYNLLVLDEPTNHLDID-AKEIIEDaLLDF--NGTIITVSHD 503
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAAtEQALLAD-LLEAlaGRTVLLITHR 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-214 |
3.14e-18 |
|
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: 83.57 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKY----TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI--------SWKKDIK--I 68
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdvvKEPAEARrrL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 69 GYLNQipdyekSESVYqciksvfkeldtiskqletietKMIEERENINSLVARYGeLQtyyeengGYEIDAKIRKVTHGL 148
Cdd:cd03266 81 GFVSD------STGLY----------------------DRLTARENLEYFAGLYG-LK-------GDELTARLEELADRL 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 149 NIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSA--TVIVS 214
Cdd:cd03266 125 GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALgkCILFS 192
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2-203 |
3.44e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 3.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDikigylNQIPDYEKSE 81
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG------DIDDPDVAEA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVYQCIKSVFKELDTIskqletietkmieeRENINSLVARYGelqtyyeeNGGYEIDAKIRKVthGL-NIAHLlkaKWGD 160
Cdd:PRK13539 75 CHYLGHRNAMKPALTV--------------AENLEFWAAFLG--------GEELDIAAALEAV--GLaPLAHL---PFGY 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI 203
Cdd:PRK13539 128 LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
18-216 |
3.81e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 82.67 E-value: 3.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 18 LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQipdyeksesvyqciksvfkeldti 97
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ------------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 skQLETIETKMIEEREninsLV-----ARYGELQTYYEENGGYEIDAKIRkvthgLNIAHLLKAKWGDLSGGERTKVGIA 172
Cdd:NF040873 63 --RSEVPDSLPLTVRD----LVamgrwARRGLWRRLTRDDRAAVDDALER-----VGLADLAGRQLGELSGGQRQRALLA 131
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488409350 173 QMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVI-VSHD 216
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLAEehARGATVVvVTHD 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-235 |
4.36e-18 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 82.65 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKkdikigylnqIPDYEKSESVYQC 86
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFD----------GKSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 87 IKS------VFKELdTISKQLETIETKMIEERENINSLVARygelqtyyeenggyeidakirkvthgLNIAHLLKAKWGD 160
Cdd:cd03268 74 IGAlieapgFYPNL-TARENLRLLARLLGIRKKRIDEVLDV--------------------------VGLKDSAKKKVKG 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI--KNNDSATVIV-SHDRYFLDETVNQIIEIDQKKL 235
Cdd:cd03268 127 FSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELIlsLRDQGITVLIsSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
329-502 |
6.95e-18 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 84.47 E-value: 6.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 329 SNRVIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTA----------SNLKIG 397
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDkLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCgepvpsrarhARQRVG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 YLSQHEfERDGNDTL---LHTFRKKVNVSEDQARHILAHFMFYGKDVFK---KVNELSGGEKIRLRWAQLVNTDYNLLVL 471
Cdd:PRK13537 84 VVPQFD-NLDPDFTVrenLLVFGRYFGLSAAAARALVPPLLEFAKLENKadaKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190
....*....|....*....|....*....|....
gi 488409350 472 DEPTNHLDIDAKEIIED---ALLDFNGTIITVSH 502
Cdd:PRK13537 163 DEPTTGLDPQARHLMWErlrSLLARGKTILLTTH 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
332-503 |
8.55e-18 |
|
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: 82.55 E-value: 8.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-----VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNlKIGYLSQHEFER 406
Cdd:cd03257 1 LLEVKNLSVSFPTgggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGK-DLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 407 DGN--------------------DTLLHTFRKKVNVSEDQARHILAHFMFYG----KDVFKK-VNELSGGEKIRLRWAQL 461
Cdd:cd03257 80 RRKeiqmvfqdpmsslnprmtigEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpEEVLNRyPHELSGGQRQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488409350 462 VNTDYNLLVLDEPTNHLDIDAKEIIEDALLD----FNGTIITVSHD 503
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKlqeeLGLTLLFITHD 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-230 |
8.97e-18 |
|
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: 82.55 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILF----DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIPDYE 78
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkalDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 79 KSEsvyqcIKSVFKE----LD---TISKQLEtiETkmieereninslvarygelqtyYEENGGYEIDAKIRKVTHGLNIA 151
Cdd:cd03257 81 RKE-----IQMVFQDpmssLNprmTIGEQIA--EP----------------------LRIHGKLSKKEARKEAVLLLLVG 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 152 HLLKAKWGD-----LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHD----RY 218
Cdd:cd03257 132 VGLPEEVLNrypheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDlgvvAK 211
|
250
....*....|....*.
gi 488409350 219 FLDETV----NQIIEI 230
Cdd:cd03257 212 IADRVAvmyaGKIVEE 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
333-502 |
1.23e-17 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 80.17 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTasnlkigylsqheferDGNDT 411
Cdd:cd03216 1 LELRGITKRFGGVKaLDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV----------------DGKEV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 LLHtfrkkvNVSEDQARHIlahFMFYgkdvfkkvnELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLdiDAKEIieDALL 491
Cdd:cd03216 65 SFA------SPRDARRAGI---AMVY---------QLSVGERQMVEIARALARNARLLILDEPTAAL--TPAEV--ERLF 122
|
170
....*....|....*...
gi 488409350 492 DF------NG-TIITVSH 502
Cdd:cd03216 123 KVirrlraQGvAVIFISH 140
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-216 |
1.64e-17 |
|
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: 82.00 E-value: 1.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIKigylNQIPDYEKSES 82
Cdd:cd03299 1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgKDIT----NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 VYQCiKSVFKELdTISKQLETIETKMIEEREninslvarygelqtyyeenggyEIDAKIRKVTHGLNIAHLLKAKWGDLS 162
Cdd:cd03299 76 VPQN-YALFPHM-TVYKNIAYGLKKRKVDKK----------------------EIERKVLEIAEMLGIDHLLNRKPETLS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 163 GGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHD 216
Cdd:cd03299 132 GGEQQRVAIARALVVNPKILLLDEPFSALDVRTkeklREELKKIRKEFGVTVLHVTHD 189
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-215 |
2.32e-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: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIK-----------IGY 70
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDgQDIThlpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 71 LNQIPdyeksesvyqcikSVFKEL---DTISKQLETIETKMIEERENinslvarygELQTYYEEnggyeidakirkvthg 147
Cdd:TIGR04406 81 LPQEA-------------SIFRKLtveENIMAVLEIRKDLDRAEREE---------RLEALLEE---------------- 122
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 148 LNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD---VKSIEWLASYIKNNDSATVIVSH 215
Cdd:TIGR04406 123 FQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVDpiaVGDIKKIIKHLKERGIGVLITDH 193
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-217 |
3.75e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.89 E-value: 3.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDI---------KIGYLNQ 73
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLnGRDLftnlpprerRVGFVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 74 ipDYeksesvyqcikSVFKELdtiskqleTIetkmieeRENIN-SL-VARYGElqtyyeenggyeidAKIRKVTHGL--- 148
Cdd:COG1118 83 --HY-----------ALFPHM--------TV-------AENIAfGLrVRPPSK--------------AEIRARVEELlel 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 149 -NIAHLLKAKWGDLSGGERTKVGIAQML-IKPtDLLLLDEPTNHLDV---KSIE-WLASYIKNNDSATVIVSHDR 217
Cdd:COG1118 121 vQLEGLADRYPSQLSGGQRQRVALARALaVEP-EVLLLDEPFGALDAkvrKELRrWLRRLHDELGGTTVFVTHDQ 194
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-485 |
3.88e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 84.30 E-value: 3.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIkigylnQIPDYEKSE 81
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEPV------RFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 S-----VYQciksvfkELDTISkQLeTIEtkmieerENI--NSLVARYGELQTYyeenggyEIDAKIRKVTHGLNIAHLL 154
Cdd:COG1129 78 AagiaiIHQ-------ELNLVP-NL-SVA-------ENIflGREPRRGGLIDWR-------AMRRRARELLARLGLDIDP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 155 KAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSHdryFLDEtvnqIIEI- 230
Cdd:COG1129 135 DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIrrlKAQGVAIIYISH---RLDE----VFEIa 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 231 DQkklhfyngnYSYFveeRDKRLLIEFEAYKTQQKKIKKMkesikqlrtwasqakppnaaMF-RRAKSMEKAlnRIQRLE 309
Cdd:COG1129 208 DR---------VTVL---RDGRLVGTGPVAELTEDELVRL--------------------MVgRELEDLFPK--RAAAPG 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 310 KPLLdskkmhitleegmnvsnrviEMENVTKAYddvLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK 389
Cdd:COG1129 254 EVVL--------------------EVEGLSVGG---VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIR 310
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 390 ------------TASNLKIGYLSQhefER--DG---------NDTL--LHTFRKKVNVSEDQARHILAHFMfygK----- 439
Cdd:COG1129 311 ldgkpvrirsprDAIRAGIAYVPE---DRkgEGlvldlsireNITLasLDRLSRGGLLDRRRERALAEEYI---Krlrik 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 488409350 440 --DVFKKVNELSGG--EKIRL-RWaqlVNTDYNLLVLDEPTNHLDIDAK-EI 485
Cdd:COG1129 385 tpSPEQPVGNLSGGnqQKVVLaKW---LATDPKVLILDEPTRGIDVGAKaEI 433
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
333-504 |
4.62e-17 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 79.87 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNL-----KIGYLSQh 402
Cdd:cd03259 1 LELKGLSKTYGSVrALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEIlidgRDVTGVpperrNIGMVFQ- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 eferdgNDTLLHTF-----------RKKVNVSEDQARHILAHFMFyGKDVF--KKVNELSGGEKIRLRWAQLVNTDYNLL 469
Cdd:cd03259 80 ------DYALFPHLtvaeniafglkLRGVPKAEIRARVRELLELV-GLEGLlnRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 470 VLDEPTNHLDIDAKEIIED---ALLDFNG-TIITVSHDR 504
Cdd:cd03259 153 LLDEPLSALDAKLREELREelkELQRELGiTTIYVTHDQ 191
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
333-503 |
5.26e-17 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 80.30 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLtsIDKGSIKTASNlKIGYLSQHEFERDGNDT 411
Cdd:cd03260 1 IELRDLNVYYGDKhALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRL--NDLIPGAPDEG-EVLLDGKDIYDLDVDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 LLHT-----------FRKKV--NVS---------EDQARHILAHFMFYGKDVFKKVN------ELSGGEKIRLRWAQLVN 463
Cdd:cd03260 78 ELRRrvgmvfqkpnpFPGSIydNVAyglrlhgikLKEELDERVEEALRKAALWDEVKdrlhalGLSGGQQQRLCLARALA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488409350 464 TDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG--TIITVSHD 503
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKeyTIVIVTHN 199
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-240 |
5.98e-17 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 79.70 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTED----ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-------KDIKIGYL 71
Cdd:TIGR02211 1 LLKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNgqslsklSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 NQipdyEKSESVYQciksvFKELDTISKQLETIETKMIEERENINSlvarygelqtyyEENGGYEIdakIRKVthglNIA 151
Cdd:TIGR02211 81 RN----KKLGFIYQ-----FHHLLPDFTALENVAMPLLIGKKSVKE------------AKERAYEM---LEKV----GLE 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 152 HLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSAT--VIVSHDRyfldetvnQI 227
Cdd:TIGR02211 133 HRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNNAKIIFDLMLelNRELNTsfLVVTHDL--------EL 204
|
250
....*....|...
gi 488409350 228 IEIDQKKLHFYNG 240
Cdd:TIGR02211 205 AKKLDRVLEMKDG 217
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-216 |
7.56e-17 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 79.26 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 28 SGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI---------SWKK------DIKIGYLNQipDYeksesvyqcikSVFK 92
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfdSRKKinlppqQRKIGLVFQ--QY-----------ALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 93 ELDTiskqletietkmieeRENINslvarYGelqtyYEENGGYEIDAKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIA 172
Cdd:cd03297 89 HLNV---------------RENLA-----FG-----LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALA 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 173 QMLIKPTDLLLLDEPTNHLDVKSIEWLASYI----KNNDSATVIVSHD 216
Cdd:cd03297 144 RALAAQPELLLLDEPFSALDRALRLQLLPELkqikKNLNIPVIFVTHD 191
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-203 |
7.99e-17 |
|
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: 78.94 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkkdikigylNQIPDYEKSESV 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRW---------NGTPLAEQRDEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIkSVFKELDTIsKQLETIetkmieeRENInslvarygelqTYYEENGGYE---IDAKIRKVthGLN-IAHLLKAKwg 159
Cdd:TIGR01189 72 HENI-LYLGHLPGL-KPELSA-------LENL-----------HFWAAIHGGAqrtIEDALAAV--GLTgFEDLPAAQ-- 127
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488409350 160 dLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI 203
Cdd:TIGR01189 128 -LSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLL 170
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-222 |
9.52e-17 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 79.09 E-value: 9.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKY--TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdikigYLNQIPDYEKSE 81
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTA---------YINGYSIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVYQCIKSVFKElDTISKQLETIETKMIeereninslvarYGELQTYYEEnggyEIDAKIRKVTHGLNIAHLLKAKWGDL 161
Cdd:cd03263 72 AARQSLGYCPQF-DALFDELTVREHLRF------------YARLKGLPKS----EIKEEVELLLRVLGLTDKANKRARTL 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDV--KSIEW--LASYIKNndSATVIVSHDryfLDE 222
Cdd:cd03263 135 SGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPasRRAIWdlILEVRKG--RSIILTTHS---MDE 194
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-216 |
9.83e-17 |
|
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: 78.00 E-value: 9.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKdikigylnqipdyeksesv 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDG------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 yqciksvfKELDTISKQLEtietkmiEERENINSLVARYGELQ--TYYEenggyeidakirkvthglNIAHLlkakwgdL 161
Cdd:cd03229 62 --------EDLTDLEDELP-------PLRRRIGMVFQDFALFPhlTVLE------------------NIALG-------L 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN---NDSATVI-VSHD 216
Cdd:cd03229 102 SGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSlqaQLGITVVlVTHD 160
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-235 |
1.28e-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: 78.79 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKK-DIK----------IGYLNQIPdyeksesvyqcik 88
Cdd:cd03245 21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGtDIRqldpadlrrnIGYVPQDV------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 89 SVFKelDTIskqletietkmieeRENINsLVARYGELQTYYE--ENGGyeIDAKIRKVTHGLNiahLLKAKWGD-LSGGE 165
Cdd:cd03245 88 TLFY--GTL--------------RDNIT-LGAPLADDERILRaaELAG--VTDFVNKHPNGLD---LQIGERGRgLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 166 RTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKnnDSATVIVSHdRYFLDETVNQIIEIDQKKL 235
Cdd:cd03245 146 RQAVALARALLNDPPILLLDEPTSAMDMNSeerlKERLRQLLG--DKTLIIITH-RPSLLDLVDRIIVMDSGRI 216
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
289-502 |
1.49e-16 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 82.52 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 289 AAMFRRAKSmekALNRIQRL--EKPLLDSKKMHITLEEGmnvsNRVIEMENVTKAYDD---VLfRNVNMLIRRGEHVAII 363
Cdd:COG1132 301 LNQLQRALA---SAERIFELldEPPEIPDPPGAVPLPPV----RGEIEFENVSFSYPGdrpVL-KDISLTIPPGETVALV 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 364 GDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL--KIGYLSQHEFerdgndtLLH-TFRK-----KVNVSEDQ 426
Cdd:COG1132 373 GPSGSGKSTLVNLLLRFYDPTSGRILidgvdirdlTLESLrrQIGVVPQDTF-------LFSgTIREnirygRPDATDEE 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 427 ----ARHILAHfmfygkDVFKK--------VNE----LSGGEKIRL---RwAQLVNTDynLLVLDEPTNHLDIDAKEIIE 487
Cdd:COG1132 446 veeaAKAAQAH------EFIEAlpdgydtvVGErgvnLSGGQRQRIaiaR-ALLKDPP--ILILDEATSALDTETEALIQ 516
|
250
....*....|....*..
gi 488409350 488 DALLDF--NGTIITVSH 502
Cdd:COG1132 517 EALERLmkGRTTIVIAH 533
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-503 |
1.77e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.15 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------TASNL-KIGYLSQhe 403
Cdd:COG4152 1 MLELKGLTKRFGDKTaVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLwdgeplDPEDRrRIGYLPE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 404 fERdGndtlLHtfrKKVNVSE-------------DQARHILAHFMfygkDVF-------KKVNELSGGE--KIrlrwaQL 461
Cdd:COG4152 79 -ER-G----LY---PKMKVGEqlvylarlkglskAEAKRRADEWL----ERLglgdranKKVEELSKGNqqKV-----QL 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 462 VNT---DYNLLVLDEPTNHLDIDAKEIIEDALLDF--NG-TIITVSHD 503
Cdd:COG4152 141 IAAllhDPELLILDEPFSGLDPVNVELLKDVIRELaaKGtTVIFSSHQ 188
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
333-514 |
1.83e-16 |
|
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: 78.22 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAY--DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTA----SNLK---IGYLSQHE 403
Cdd:cd03292 1 IEFINVTKTYpnGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqdvSDLRgraIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 404 ferdgnDTLLHTFR--KKVNVSEDQArhiLAHFMFY--GKDVFKKV-----------------NELSGGEKIRLRWAQLV 462
Cdd:cd03292 81 ------GVVFQDFRllPDRNVYENVA---FALEVTGvpPREIRKRVpaalelvglshkhralpAELSGGEQQRVAIARAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 463 NTDYNLLVLDEPTNHLDIDAKEIIEDALLDFN---GTIITVSHDRyflnKLFNTT 514
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINkagTTVVVATHAK----ELVDTT 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
333-503 |
1.97e-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: 78.76 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD---VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL-----K 395
Cdd:cd03256 1 IEVENLSKTYPNgkkAL-KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLidgtdinklKGKALrqlrrQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 396 IGYLSQHE-------------FERDGNDTLLHTFRKKVNVSEDQ-ARHILAHFMFYGKdVFKKVNELSGGEKIRLRWAQL 461
Cdd:cd03256 80 IGMIFQQFnlierlsvlenvlSGRLGRRSTWRSLFGLFPKEEKQrALAALERVGLLDK-AYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488409350 462 VNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG----TIITVSHD 503
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINReegiTVIVSLHQ 204
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-188 |
2.40e-16 |
|
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: 78.24 E-value: 2.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTE-DILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIK-----------IGY 70
Cdd:cd03224 1 LEVENLNAGYGKsQILFG-VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDgRDITglppheraragIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 71 LNQIPDyeksesvyqciksVFKELdtiskqleTIEtkmieerENInsLVARYGelqtyyeeNGGYEIDAKIRKVthgLNI 150
Cdd:cd03224 80 VPEGRR-------------IFPEL--------TVE-------ENL--LLGAYA--------RRRAKRKARLERV---YEL 118
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488409350 151 AHLLKAKW----GDLSGGERTKVGIAQMLIKPTDLLLLDEPT 188
Cdd:cd03224 119 FPRLKERRkqlaGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
333-504 |
2.71e-16 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 80.53 E-value: 2.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVLF-RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLK-----IGYLSQh 402
Cdd:COG3842 6 LELENVSKRYGDVTAlDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRIlldgRDVTGLPpekrnVGMVFQ- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 eferdgNDTLlhtF--------------RKKVNVSEDQAR--HILAhfMF----YGKdvfKKVNELSGGEKIRLRWAQ-L 461
Cdd:COG3842 85 ------DYAL---FphltvaenvafglrMRGVPKAEIRARvaELLE--LVglegLAD---RYPHQLSGGQQQRVALARaL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488409350 462 VNtDYNLLVLDEPTNHLDIDAKEIIEDALLD----FNGTIITVSHDR 504
Cdd:COG3842 151 AP-EPRVLLLDEPLSALDAKLREEMREELRRlqreLGITFIYVTHDQ 196
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
8-216 |
2.85e-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: 78.38 E-value: 2.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTED--ILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkkdikigYLNQIPDYEKSEsvyq 85
Cdd:cd03256 5 NLSKTYPNGkkALKD-VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLI-------DGTDINKLKGKA---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 cIKSVFKELDTISKQLETIE--TKMieerENInsLVARYGELQTYYEENGGYEiDAKIRKVTHGL---NIAHLLKAKWGD 160
Cdd:cd03256 73 -LRQLRRQIGMIFQQFNLIErlSVL----ENV--LSGRLGRRSTWRSLFGLFP-KEEKQRALAALervGLLDKAYQRADQ 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK---NNDSATVIVS-HD 216
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKrinREEGITVIVSlHQ 204
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
8-235 |
3.28e-16 |
|
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: 77.45 E-value: 3.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDIL-FDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIKIGYLNQIPDYEKSesvyq 85
Cdd:cd03292 5 NVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgQDVSDLRGRAIPYLRRK----- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 cIKSVFKELDTISKqLETIETKMIeereninSLVARYgelqtyyeeNGGYEIDAKIRKVTHGLNIAHLLKAKWGDLSGGE 165
Cdd:cd03292 80 -IGVVFQDFRLLPD-RNVYENVAF-------ALEVTG---------VPPREIRKRVPAALELVGLSHKHRALPAELSGGE 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409350 166 RTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIVS-HDRYFLDETVNQIIEIDQKKL 235
Cdd:cd03292 142 QQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKkiNKAGTTVVVAtHAKELVDTTRHRVIALERGKL 214
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-223 |
3.59e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 77.30 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKdikigylnqipdyekses 82
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER------------------ 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 vyqciKSVFKELDTISKQLetietKMIEERENIN-SLVARYGELQTYYEENGGYEIDAKIRKvthgLNIAHLLKAKWGDL 161
Cdd:PRK13540 63 -----QSIKKDLCTYQKQL-----CFVGHRSGINpYLTLRENCLYDIHFSPGAVGITELCRL----FSLEHLIDYPCGLL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDS---ATVIVSHDRYFLDET 223
Cdd:PRK13540 129 SSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAkggAVLLTSHQDLPLNKA 193
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
8-216 |
6.90e-16 |
|
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: 76.52 E-value: 6.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKIG--YLNQIPDYEKSES-VY 84
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSG------RIYIGgrDVTDLPPKDRDIAmVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 85 QCI-----KSVFkelDTISKQLetietKMIEERENinslvarygelqtyyeenggyEIDAKIRKVTHGLNIAHLLKAKWG 159
Cdd:cd03301 79 QNYalyphMTVY---DNIAFGL-----KLRKVPKD---------------------EIDERVREVAELLQIEHLLDRKPK 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 160 DLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN----NDSATVIVSHD 216
Cdd:cd03301 130 QLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqqrLGTTTIYVTHD 190
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-235 |
8.10e-16 |
|
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: 80.19 E-value: 8.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 6 ASNISKKYTEDI-LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI-------------SWKKdiKIGYL 71
Cdd:COG4988 339 LEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSIlingvdlsdldpaSWRR--QIAWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 NQIPdyeksesvyqcikSVFKelDTIskqletietkmieeRENInsLVARygelqtyyeenggyeIDAKIRKVTHGLNIA 151
Cdd:COG4988 417 PQNP-------------YLFA--GTI--------------RENL--RLGR---------------PDASDEELEAALEAA 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 152 HL------LKAKW----GD----LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVIVSH 215
Cdd:COG4988 451 GLdefvaaLPDGLdtplGEggrgLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRlaKGRTVILITH 530
|
250 260
....*....|....*....|
gi 488409350 216 DRYFLDEtVNQIIEIDQKKL 235
Cdd:COG4988 531 RLALLAQ-ADRILVLDDGRI 549
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
333-502 |
1.41e-15 |
|
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: 76.11 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL--KIGYL 399
Cdd:cd03253 1 IEFENVTFAYDPgrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILidgqdirevTLDSLrrAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQHE--FerdgNDTLLHTFR-KKVNVSEDQ------ARHILAHFMFYGKDVFKKVNE----LSGGEKIRLRWAQLVNTDY 466
Cdd:cd03253 81 PQDTvlF----NDTIGYNIRyGRPDATDEEvieaakAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNP 156
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 467 NLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSH 502
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVskGRTTIVIAH 194
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
11-240 |
1.42e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.22 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 11 KKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKIGYLnqIPDYEKSESVYQcIKSV 90
Cdd:cd03267 29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSG------EVRVAGL--VPWKRRKKFLRR-IGVV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 91 FKELDTISKQLETIETkmieerenINSLVARYGELQTYYEENggyeidakIRKVTHGLNIAHLLKAKWGDLSGGERTKVG 170
Cdd:cd03267 100 FGQKTQLWWDLPVIDS--------FYLLAAIYDLPPARFKKR--------LDELSELLDLEELLDTPVRQLSLGQRMRAE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 171 IAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIV--SHDRYFLDETVNQIIEIDQKKLhFYNG 240
Cdd:cd03267 164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKeyNRERGTTVLltSHYMKDIEALARRVLVIDKGRL-LYDG 236
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-217 |
1.49e-15 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 78.22 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI--------KIGYL 71
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgRDVtglppekrNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 NQipDYeksesvyqcikSVFKELdTIskqletietkmieeRENInslvaRYG-ELQTYYEEnggyEIDAKIRKVTHGLNI 150
Cdd:COG3842 83 FQ--DY-----------ALFPHL-TV--------------AENV-----AFGlRMRGVPKA----EIRARVAELLELVGL 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 151 AHLLKAKWGDLSGGERTKVGIAQML-IKPtDLLLLDEPTNHLDVKSIE----WLASYIKNNDSATVIVSHDR 217
Cdd:COG3842 126 EGLADRYPHQLSGGQQQRVALARALaPEP-RVLLLDEPLSALDAKLREemreELRRLQRELGITFIYVTHDQ 196
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
332-475 |
1.97e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.92 E-value: 1.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------------KTASNLKIGY 398
Cdd:COG3845 5 ALELRGITKRFGGVVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpvrirspRDAIALGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQHeFerdgndTLLHTF------------RKKVNVSEDQARHILAHFM-FYGKDV--FKKVNELSGGEKIR---LRwaQ 460
Cdd:COG3845 85 VHQH-F------MLVPNLtvaenivlglepTKGGRLDRKAARARIRELSeRYGLDVdpDAKVEDLSVGEQQRveiLK--A 155
|
170
....*....|....*
gi 488409350 461 LVNtDYNLLVLDEPT 475
Cdd:COG3845 156 LYR-GARILILDEPT 169
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
333-502 |
2.00e-15 |
|
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: 74.95 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI--------KTASNLK-IG----- 397
Cdd:cd03268 1 LKTNDLTKTYGKKrVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItfdgksyqKNIEALRrIGaliea 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 -----YLSQHEFERdgNDTLLHTFRKKvNVSEDQARHILAHfmfYGKdvfKKVNELSGGEKIRLRWAQLVNTDYNLLVLD 472
Cdd:cd03268 81 pgfypNLTARENLR--LLARLLGIRKK-RIDEVLDVVGLKD---SAK---KKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190
....*....|....*....|....*....|....
gi 488409350 473 EPTNHLDIDA----KEIIEDaLLDFNGTIITVSH 502
Cdd:cd03268 152 EPTNGLDPDGikelRELILS-LRDQGITVLISSH 184
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
333-503 |
2.34e-15 |
|
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: 75.55 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-------------KTAS------ 392
Cdd:cd03219 1 LEVRGLTKRFGGLVaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlfdgeditglpphEIARlgigrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 393 --------------NLKIGYLSQHeferdGNDTLLHTFRKKVNVSEDQARHILAhFMFYGKDVFKKVNELSGGEKIRLRW 458
Cdd:cd03219 81 fqiprlfpeltvleNVMVAAQART-----GSGLLLARARREEREARERAEELLE-RVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488409350 459 AQLVNTDYNLLVLDEPT---NHLDIDA-KEIIEDaLLDFNGTIITVSHD 503
Cdd:cd03219 155 ARALATDPKLLLLDEPAaglNPEETEElAELIRE-LRERGITVLLVEHD 202
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
357-503 |
2.75e-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: 75.02 E-value: 2.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 357 GEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK--------TASNL-------KIGYLSQheferdgNDTLL-H------ 414
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVlngtvlfdSRKKInlppqqrKIGLVFQ-------QYALFpHlnvren 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 415 ----TFRKKVNVSEDQARHILAHFMFyGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEII---- 486
Cdd:cd03297 96 lafgLKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLlpel 174
|
170
....*....|....*..
gi 488409350 487 EDALLDFNGTIITVSHD 503
Cdd:cd03297 175 KQIKKNLNIPVIFVTHD 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
333-502 |
3.45e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 74.62 E-value: 3.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-------KTASNLKIGYLSQhef 404
Cdd:cd03269 1 LEVENVTKRFGRVtALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVlfdgkplDIAARNRIGYLPE--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 405 ERdG-------NDTLLHTFRKKvNVSEDQARH----ILAHFMFYGKDvFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDE 473
Cdd:cd03269 78 ER-GlypkmkvIDQLVYLAQLK-GLKKEEARRrideWLERLELSEYA-NKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190
....*....|....*....|....*....|..
gi 488409350 474 PTNHLDIDAKEIIEDALLDF---NGTIITVSH 502
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELaraGKTVILSTH 186
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-229 |
4.00e-15 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.49 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILF---------DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkKDIKIGYL 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGGLSgkhqhqtvlNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSW-RGEPLAKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 N--QIPDYEKSesvyqcIKSVFKelDTISKqletietkmIEERENINSLVA---RYgeLQTYYEENGGYEIDAKIRKVth 146
Cdd:PRK10419 80 NraQRKAFRRD------IQMVFQ--DSISA---------VNPRKTVREIIReplRH--LLSLDKAERLARASEMLRAV-- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 147 GLNIAHLLKAKwGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDV----KSIEWLASYIKNNDSATVIVSHD----RY 218
Cdd:PRK10419 139 DLDDSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLvlqaGVIRLLKKLQQQFGTACLFITHDlrlvER 217
|
250
....*....|....*..
gi 488409350 219 F------LDEtvNQIIE 229
Cdd:PRK10419 218 FcqrvmvMDN--GQIVE 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
333-479 |
4.00e-15 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 74.15 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-VLFRNVNMLIRRGEHvAIIGDNGTGKTTLLKIILGLTSIDKGSI--------KTASNL--KIGYLSQ 401
Cdd:cd03264 1 LQLENLTKRYGKkRALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIridgqdvlKQPQKLrrRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 hEFERDGNDTLLHTFR-----KKVNVSEDQAR--HILAHFMFYG-KDvfKKVNELSGGEKIRLRWAQLVNTDYNLLVLDE 473
Cdd:cd03264 80 -EFGVYPNFTVREFLDyiawlKGIPSKEVKARvdEVLELVNLGDrAK--KKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
....*.
gi 488409350 474 PTNHLD 479
Cdd:cd03264 157 PTAGLD 162
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
316-521 |
5.54e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.22 E-value: 5.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 316 KKMHITLEEGMNVSNRVIE-MENVTKAYDDV---LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS--IDKGSIK 389
Cdd:COG2401 11 MRVTKVYSSVLDLSERVAIvLEAFGVELRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 390 tasnlkigyLSQHEFERDGndTLLHTFRKKVNVseDQARHILAH------FMFygkdvFKKVNELSGGEKIRLRWAQLVN 463
Cdd:COG2401 91 ---------VPDNQFGREA--SLIDAIGRKGDF--KDAVELLNAvglsdaVLW-----LRRFKELSTGQKFRFRLALLLA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 464 TDYNLLVLDEPTNHLDID-AKEI---IEDALLDFNGTIITVSHDRYFLNKLFNTTYLLKNKT 521
Cdd:COG2401 153 ERPKLLVIDEFCSHLDRQtAKRVarnLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVGYG 214
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-187 |
5.55e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.68 E-value: 5.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDIK-----------I 68
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLdGEDIThlpmhkrarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 69 GYLNQipdyeksESvyqcikSVFKEL---DTISKQLETIETKMIEERENINSLVarygelqtyyEEnggyeidakirkvt 145
Cdd:COG1137 81 GYLPQ-------EA------SIFRKLtveDNILAVLELRKLSKKEREERLEELL----------EE-------------- 123
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488409350 146 hgLNIAHLLKAKWGDLSGGERTKVGIAQML-IKPtDLLLLDEP 187
Cdd:COG1137 124 --FGITHLRKSKAYSLSGGERRRVEIARALaTNP-KFILLDEP 163
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
348-503 |
7.37e-15 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 74.29 E-value: 7.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 348 RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNL----KIGYLSQHEF-------------ERDGND 410
Cdd:cd03267 38 KGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwkrRKKFLRRIGVvfgqktqlwwdlpVIDSFY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 411 TLLHTFRkkvnVSEDQARHILAHF---MFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIE 487
Cdd:cd03267 118 LLAAIYD----LPPARFKKRLDELselLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180
....*....|....*....|
gi 488409350 488 DALLDFN----GTIITVSHD 503
Cdd:cd03267 194 NFLKEYNrergTTVLLTSHY 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
333-503 |
8.87e-15 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 73.56 E-value: 8.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGS--------IKTASNLK--IGYLSQ 401
Cdd:cd03265 1 IEVENLVKKYGDFEaVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvVREPREVRrrIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 hefERDGNDTL-----LHTFRKKVNVSEDQARHILAH---FMFYGKDVFKKVNELSGGEKIRLRWAQ-LVNTDyNLLVLD 472
Cdd:cd03265 81 ---DLSVDDELtgwenLYIHARLYGVPGAERRERIDElldFVGLLEAADRLVKTYSGGMRRRLEIARsLVHRP-EVLFLD 156
|
170 180 190
....*....|....*....|....*....|....*
gi 488409350 473 EPTNHLDIDAK----EIIEDALLDFNGTIITVSHD 503
Cdd:cd03265 157 EPTIGLDPQTRahvwEYIEKLKEEFGMTILLTTHY 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
332-503 |
9.54e-15 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 9.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQhEFERDGnd 410
Cdd:PRK09544 4 LVSLENVSVSFGQrRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ-KLYLDT-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 411 TLLHT----FRKKVNVSED---------QARHILAHFMfygkdvfkkvNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNH 477
Cdd:PRK09544 81 TLPLTvnrfLRLRPGTKKEdilpalkrvQAGHLIDAPM----------QKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190
....*....|....*....|....*....|
gi 488409350 478 LDIDAK----EIIEDALLDFNGTIITVSHD 503
Cdd:PRK09544 151 VDVNGQvalyDLIDQLRRELDCAVLMVSHD 180
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-216 |
1.05e-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: 73.63 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIkigylNQIPDYEKSES 82
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgEDI-----TGLPPHEIARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 ----VYQcIKSVFKELdTIskqletietkmieeRENInsLVARYGELQTYYEENGGY----EIDAKIRKVTHGLNIAHLL 154
Cdd:cd03219 76 gigrTFQ-IPRLFPEL-TV--------------LENV--MVAAQARTGSGLLLARARreerEARERAEELLERVGLADLA 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 155 KAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATV-IVSHD 216
Cdd:cd03219 138 DRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRelRERGITVlLVEHD 202
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
333-506 |
1.10e-14 |
|
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: 72.95 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD--VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-----------KTASNL--KIG 397
Cdd:cd03262 1 IEIKNLHKSFGDfhVL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIiidglkltddkKNINELrqKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 YLSQH--EFERD---GNDTLLHTFRKKVNVSEDQARhilahfmfyGKDVFKKV----------NELSGGEKIRLRWAQLV 462
Cdd:cd03262 80 MVFQQfnLFPHLtvlENITLAPIKVKGMSKAEAEER---------ALELLEKVgladkadaypAQLSGGQQQRVAIARAL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488409350 463 NTDYNLLVLDEPTNHLDidaKEIIEDAL-----LDFNG-TIITVSHDRYF 506
Cdd:cd03262 151 AMNPKVMLFDEPTSALD---PELVGEVLdvmkdLAEEGmTMVVVTHEMGF 197
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
333-503 |
1.44e-14 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 73.14 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLK-----IGYLSQHE 403
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKIllngKDITNLPpekrdISYVPQNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 404 F---ERDGNDTLLHTFRKKVNVSEDQARHIL--AHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHL 478
Cdd:cd03299 81 AlfpHMTVYKNIAYGLKKRKVDKKEIERKVLeiAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180
....*....|....*....|....*....
gi 488409350 479 DIDAKEIIEDALLD----FNGTIITVSHD 503
Cdd:cd03299 161 DVRTKEKLREELKKirkeFGVTVLHVTHD 189
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-201 |
1.46e-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: 72.53 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkkdikigylNQIPDYEKSESV 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL---------NGGPLDFQRDSI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIKSVfKELDTISKQLETietkmieeRENinslvarygeLQTYYEENGgyeiDAKIRKVTHGLNIAHLLKAKWGDLSG 163
Cdd:cd03231 72 ARGLLYL-GHAPGIKTTLSV--------LEN----------LRFWHADHS----DEQVEEALARVGLNGFEDRPVAQLSA 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLAS 201
Cdd:cd03231 129 GQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
333-479 |
1.54e-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: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLK-----IGYLSQH 402
Cdd:cd03296 3 IEVRNVSKRFGDfVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggEDATDVPvqernVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 E--FE----RDGNDTLLHTFRKKVNVSEDQAR---HILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDE 473
Cdd:cd03296 83 YalFRhmtvFDNVAFGLRVKPRSERPPEAEIRakvHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
....*.
gi 488409350 474 PTNHLD 479
Cdd:cd03296 163 PFGALD 168
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
4-216 |
1.55e-14 |
|
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: 73.70 E-value: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigylnqiPDYEksesv 83
Cdd:TIGR03873 2 LRLSRVSWSAGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVD-------------LAGV----- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 yqciksvfkELDTISKQLETIETKMIEERENIN-SLVARYGEL--QTYYEENGGYEIDAKIRKVTHGL---NIAHLLKAK 157
Cdd:TIGR03873 64 ---------DLHGLSRRARARRVALVEQDSDTAvPLTVRDVVAlgRIPHRSLWAGDSPHDAAVVDRALartELSHLADRD 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 158 WGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVIVS-HD 216
Cdd:TIGR03873 135 MSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRElaATGVTVVAAlHD 196
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-216 |
2.04e-14 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 72.60 E-value: 2.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGM-----ERPSTGVISWK-KDIkigylnqipdY 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDgKDI----------Y 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 78 EKSESVYQCIKS---VFKELDTISKqleTIetkmieeRENInslvaRYGelQTYYEENGGYEIDAKIRKVthgLNIAHL- 153
Cdd:cd03260 71 DLDVDVLELRRRvgmVFQKPNPFPG---SI-------YDNV-----AYG--LRLHGIKLKEELDERVEEA---LRKAALw 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 154 ----LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS---IEWLasyIK--NNDSATVIVSHD 216
Cdd:cd03260 131 devkDRLHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPIStakIEEL---IAelKKEYTIVIVTHN 199
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-222 |
2.14e-14 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 74.76 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI--------SWKKDI-------KIGYlnqipdyeksesVYQc 86
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfDSRKGIflppekrRIGY------------VFQ- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 87 IKSVFKELDTiskqletietkmieeRENInslvaRYGelqtyYEENGGYEIDAKIRKVTHGLNIAHLLKAKWGDLSGGER 166
Cdd:TIGR02142 83 EARLFPHLSV---------------RGNL-----RYG-----MKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEK 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 167 TKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVI----VSHDryfLDE 222
Cdd:TIGR02142 138 QRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIpilyVSHS---LQE 194
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
326-510 |
3.14e-14 |
|
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: 72.08 E-value: 3.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 326 MNVsnrVIEMENVTKAYddVL----------FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------ 389
Cdd:COG4778 1 MTT---LLEVENLSKTF--TLhlqggkrlpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILvrhdgg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 390 -----TAS-----NLK---IGYLSQheFER-----------------DGNDTllhtfrkkvNVSEDQARHILAHFmfygk 439
Cdd:COG4778 76 wvdlaQASpreilALRrrtIGYVSQ--FLRviprvsaldvvaeplleRGVDR---------EEARARARELLARL----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 440 dvfkKVNE---------LSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAK----EIIEDALLdfNGT-IITVSHDRY 505
Cdd:COG4778 140 ----NLPErlwdlppatFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKA--RGTaIIGIFHDEE 213
|
....*
gi 488409350 506 FLNKL 510
Cdd:COG4778 214 VREAV 218
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
17-216 |
3.18e-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: 75.09 E-value: 3.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 17 ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigyLNQIPDYEKSESVYQCIKSVFKE--- 93
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT---------LDGVPVSSLDQDEVRRRVSVCAQdah 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 94 -LDTiskqleTIetkmieeRENInsLVARygelqtyyEENGGYEIDAKIRKVTHGLNIAHL---LKAKWGD----LSGGE 165
Cdd:TIGR02868 420 lFDT------TV-------RENL--RLAR--------PDATDEELWAALERVGLADWLRALpdgLDTVLGEggarLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 166 RTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDS--ATVIVSHD 216
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSgrTVVLITHH 529
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
333-510 |
3.27e-14 |
|
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: 71.40 E-value: 3.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS--IDKGSIkTASNLKIGYLSQHEFERDGn 409
Cdd:cd03217 1 LEIKDLHVSVGGKeILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEI-LFKGEDITDLPPEERARLG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 410 dtLLHTFRKKVNVSEDQarhiLAHFMFYgkdvfkkVNE-LSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIED 488
Cdd:cd03217 79 --IFLAFQYPPEIPGVK----NADFLRY-------VNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180
....*....|....*....|....*
gi 488409350 489 A---LLDFNGTIITVSHDRYFLNKL 510
Cdd:cd03217 146 VinkLREEGKSVLIITHYQRLLDYI 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-192 |
4.30e-14 |
|
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: 71.84 E-value: 4.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYT----EDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTG-VISWKKDIKigylnqipdyEKSEs 82
Cdd:cd03258 6 NVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGsVLVDGTDLT----------LLSG- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 vyqciksvfKELDTISKQLetietKMIeeRENINSLVARygelqTYYE------ENGGYEIDAKIRKVTHGLNI---AHL 153
Cdd:cd03258 75 ---------KELRKARRRI-----GMI--FQHFNLLSSR-----TVFEnvalplEIAGVPKAEIEERVLELLELvglEDK 133
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 154 LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:cd03258 134 ADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
333-503 |
6.15e-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: 74.32 E-value: 6.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-----------KTASNLKIGYL 399
Cdd:TIGR02868 335 LELRDLSAGYPGapPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVtldgvpvssldQDEVRRRVSVC 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQ--HEFERDGNDTLLHTfrkKVNVSEDQ----------ARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYN 467
Cdd:TIGR02868 415 AQdaHLFDTTVRENLRLA---RPDATDEElwaalervglADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAP 491
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 468 LLVLDEPTNHLDID-AKEIIEDALLDFNG-TIITVSHD 503
Cdd:TIGR02868 492 ILLLDEPTEHLDAEtADELLEDLLAALSGrTVVLITHH 529
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-235 |
6.40e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.92 E-value: 6.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdIKIGYLNQIPDYEKSE 81
Cdd:PRK10619 4 NKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIV----VNGQTINLVRDKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVYQciksvfkeldtiSKQLETIETK--MIEERENINS-LVARYGELQTYYEENGGYEIDAKIRKVTH--GLNIAHLLKA 156
Cdd:PRK10619 80 KVAD------------KNQLRLLRTRltMVFQHFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYlaKVGIDERAQG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 157 KW-GDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD---VKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQ 232
Cdd:PRK10619 148 KYpVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDpelVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQ 227
|
...
gi 488409350 233 KKL 235
Cdd:PRK10619 228 GKI 230
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-235 |
8.83e-14 |
|
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: 70.99 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI-------------KIGYLN 72
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgEDIsglseaelyrlrrRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 73 QIPDYEKSESVYQCIKSVFKEldtiskqletiETKMIEERenINSLVArygelqtyyeenggyeidAKIRKVthGL-NIA 151
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLRE-----------HTRLSEEE--IREIVL------------------EKLEAV--GLrGAE 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 152 HLLKAkwgDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN----NDSATVIVSHDRYFLDETVNQI 227
Cdd:cd03261 131 DLYPA---ELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkkeLGLTSIMVTHDLDTAFAIADRI 207
|
....*...
gi 488409350 228 IEIDQKKL 235
Cdd:cd03261 208 AVLYDGKI 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
333-502 |
1.15e-13 |
|
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: 69.26 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD---VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIktasnlkigYLSQHEFErdgn 409
Cdd:cd03247 1 LSINNVSFSYPEqeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVPVS---- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 410 dTLLHTFRKKVNVSeDQARHILAHFMfyGKDVFKKvneLSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLD-IDAKEIIEd 488
Cdd:cd03247 68 -DLEKALSSLISVL-NQRPYLFDTTL--RNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDpITERQLLS- 139
|
170
....*....|....*.
gi 488409350 489 ALLDF--NGTIITVSH 502
Cdd:cd03247 140 LIFEVlkDKTLIWITH 155
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-216 |
1.41e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 70.23 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTE-----DILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDikigYLNQIPDY 77
Cdd:PRK11629 5 LLQCDNLCKRYQEgsvqtDVLHN-VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ----PMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 78 EKSE-------SVYQciksvFKELDTISKQLETIETKMIEERENINslvarygelqtyyeenggyEIDAKIRKVTHGLNI 150
Cdd:PRK11629 80 AKAElrnqklgFIYQ-----FHHLLPDFTALENVAMPLLIGKKKPA-------------------EINSRALEMLAAVGL 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 151 AHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVK---SI-EWLASYIKNNDSATVIVSHD 216
Cdd:PRK11629 136 EHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARnadSIfQLLGELNRLQGTAFLVVTHD 205
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-215 |
1.88e-13 |
|
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: 68.40 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTED---ILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI--------SWKKDIK---IG 69
Cdd:cd03246 1 LEVENVSFRYPGAeppVLRN-VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVrldgadisQWDPNELgdhVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 70 YLNQipDYEksesvyqciksVFKelDTIskqletietkmieeRENInslvarygelqtyyeenggyeidakirkvthgln 149
Cdd:cd03246 80 YLPQ--DDE-----------LFS--GSI--------------AENI---------------------------------- 96
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 150 iahllkakwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN---NDSATVIVSH 215
Cdd:cd03246 97 -----------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAAlkaAGATRIVIAH 154
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-192 |
2.80e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.60 E-value: 2.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigyLNQIPDYEKSES 82
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIS---------LCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 VYQCIkSVFKELDTISKQLETIETKMIeereninslVARYGELQTyyeenggyeidAKIRKVTHG-LNIAHL---LKAKW 158
Cdd:PRK13537 78 ARQRV-GVVPQFDNLDPDFTVRENLLV---------FGRYFGLSA-----------AAARALVPPlLEFAKLenkADAKV 136
|
170 180 190
....*....|....*....|....*....|....
gi 488409350 159 GDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:PRK13537 137 GELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-216 |
3.38e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 69.54 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGM-ERPSTGVISWKKDIK-----------I 68
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvPRDAGNIIIDDEDISllplhararrgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 69 GYLNQIPDYEKSESVYQCIKSVFKELDTISKqletietkmiEERENinslvaRYGELQtyyEEnggyeidakirkvthgL 148
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSA----------EQRED------RANELM---EE----------------F 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 149 NIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD---VKSIEWLASYIKNNDSATVIVSHD 216
Cdd:PRK10895 126 HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRDSGLGVLITDHN 196
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-222 |
3.77e-13 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 69.35 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTED----ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW------KKDIKIGY 70
Cdd:COG1116 5 APALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVdgkpvtGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 71 lnqipdyeksesvyqciksVFKElDTIskqLE--TIetkmieeRENInslvaRYG-ELQTYYEENGGYEIDAKIRKVthG 147
Cdd:COG1116 85 -------------------VFQE-PAL---LPwlTV-------LDNV-----ALGlELRGVPKAERRERARELLELV--G 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 148 LniAHLLKAKWGDLSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDV--KSI--EWLASYIKNNDSATVIVSHDryfLDE 222
Cdd:COG1116 128 L--AGFEDAYPHQLSGGMRQRVAIARALAnDP-EVLLMDEPFGALDAltRERlqDELLRLWQETGKTVLFVTHD---VDE 201
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
343-502 |
4.15e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 68.36 E-value: 4.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 343 DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK--------TASNLKIGYLSQH------------ 402
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKldggdiddPDVAEACHYLGHRnamkpaltvaen 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 -EFERD---GNDTLLHTFRKKVNVSEdqarhiLAHFMFygkdvfkkvNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHL 478
Cdd:PRK13539 94 lEFWAAflgGEELDIAAALEAVGLAP------LAHLPF---------GYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
|
170 180
....*....|....*....|....*..
gi 488409350 479 DIDAKEIIEDAL---LDFNGTIITVSH 502
Cdd:PRK13539 159 DAAAVALFAELIrahLAQGGIVIAATH 185
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-224 |
4.69e-13 |
|
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: 68.65 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKY----TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIS------WKKDIKIGYLNQ 73
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLvdgepvTGPGPDRGYVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 74 ----IPdyeksesvyqcIKSVfkeLDTISKQLETIETKMIEERENINSLVARYGelqtyyeenggyeidakirkvthgln 149
Cdd:cd03293 81 qdalLP-----------WLTV---LDNVALGLELQGVPKAEARERAEELLELVG-------------------------- 120
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 150 IAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDV----KSIEWLASYIKNNDSATVIVSHDryfLDETV 224
Cdd:cd03293 121 LSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAltreQLQEELLDIWRETGKTVLLVTHD---IDEAV 196
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
333-502 |
5.09e-13 |
|
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: 68.80 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD----VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL--KIG 397
Cdd:cd03251 1 VEFKNVTFRYPGdgppVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILidghdvrdyTLASLrrQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 YLSQ--HEFerdgNDTLLHTFR-KKVNVSEDQARHI--LAHFM-F-------YGKDVFKKVNELSGGEKIRLRWAQLVNT 464
Cdd:cd03251 80 LVSQdvFLF----NDTVAENIAyGRPGATREEVEEAarAANAHeFimelpegYDTVIGERGVKLSGGQRQRIAIARALLK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488409350 465 DYNLLVLDEPTNHLDIDAKEIIEDAL--LDFNGTIITVSH 502
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALerLMKNRTTFVIAH 195
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
333-502 |
5.65e-13 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 68.41 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD---VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL--KIGY 398
Cdd:cd03254 3 IEFENVNFSYDEkkpVL-KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILidgidirdiSRKSLrsMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQHEFERdgNDTLLHTFRKKVNVSED-------QARHILAHFMFYGKDVFKKVNE----LSGGEKIRLRWAQLVNTDYN 467
Cdd:cd03254 82 VLQDTFLF--SGTIMENIRLGRPNATDeevieaaKEAGAHDFIMKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPK 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 488409350 468 LLVLDEPTNHLDIDAKEIIEDAL--LDFNGTIITVSH 502
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALekLMKGRTSIIIAH 196
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-483 |
6.60e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 71.01 E-value: 6.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPST--GVISWK-KDIKIgylNQIPDYEK 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSgSPLKA---SNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SEsvyqcIKSVFKELdTISKQLETIETKMIEERENINSLVARYGELqTYYEENGGYEIDAKIRKVTHGLniahllkakwG 159
Cdd:TIGR02633 78 AG-----IVIIHQEL-TLVPELSVAENIFLGNEITLPGGRMAYNAM-YLRAKNLLRELQLDADNVTRPV----------G 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 160 DLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN---NDSATVIVSHDryfLDEtvnqiieidqkklh 236
Cdd:TIGR02633 141 DYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDlkaHGVACVYISHK---LNE-------------- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 237 fyngnysyfveerdkrlliefeayktqqkkIKKMKESIKQLRTWASQAKPPNAAMfrrakSMEKALNRIQRLEKPLLDSK 316
Cdd:TIGR02633 204 ------------------------------VKAVCDTICVIRDGQHVATKDMSTM-----SEDDIITMMVGREITSLYPH 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 317 KMHITLEEgmnvsnrVIEMENVT---------KAYDDVLFRnvnmlIRRGEHVAIIGDNGTGKTTLLKIILGL-TSIDKG 386
Cdd:TIGR02633 249 EPHEIGDV-------ILEARNLTcwdvinphrKRVDDVSFS-----LRRGEILGVAGLVGAGRTELVQALFGAyPGKFEG 316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 387 SIktasnlkigYLSQHEFE-RDGNDTLLHtfrKKVNVSEDQARHILAHFMFYGKDV------------------------ 441
Cdd:TIGR02633 317 NV---------FINGKPVDiRNPAQAIRA---GIAMVPEDRKRHGIVPILGVGKNItlsvlksfcfkmridaaaelqiig 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 442 -------------FKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAK 483
Cdd:TIGR02633 385 saiqrlkvktaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAK 439
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-218 |
7.65e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 7.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIkigylNQIPDyekse 81
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdKPI-----SMLSS----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqciKSVFKELDTISKQLETIETKMIEE-----RENINSLVARYGElqtyyeenggyEIDAKIRKVTHGLNIAHLLKA 156
Cdd:PRK11231 72 ------RQLARRLALLPQHHLTPEGITVRElvaygRSPWLSLWGRLSA-----------EDNARVNQAMEQTRINHLADR 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 157 KWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVI-VSHD-----RY 218
Cdd:PRK11231 135 RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRelNTQGKTVVtVLHDlnqasRY 204
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-203 |
7.72e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 7.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIK------------IGY 70
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQgEPIRrqrdeyhqdllyLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 71 LNQIPDyeksesvyqciksvfkELdtiskqleTIEtkmieerENINSLVARYGELQtyyeenggyeiDAKIRKVTHGLNI 150
Cdd:PRK13538 82 QPGIKT----------------EL--------TAL-------ENLRFYQRLHGPGD-----------DEALWEALAQVGL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 151 AHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI 203
Cdd:PRK13538 120 AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-232 |
7.75e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 69.73 E-value: 7.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNIlNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK---------KDIKIGYL 71
Cdd:PRK10851 1 MSI-EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHgtdvsrlhaRDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 NQipDYeksesvyqcikSVFKEL---DTISKQLetietKMIEERENINSlvarygelqtyyeenggYEIDAKIRKVTHGL 148
Cdd:PRK10851 80 FQ--HY-----------ALFRHMtvfDNIAFGL-----TVLPRRERPNA-----------------AAIKAKVTQLLEMV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 149 NIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDS----ATVIVSHDRYFLDETV 224
Cdd:PRK10851 125 QLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEelkfTSVFVTHDQEEAMEVA 204
|
....*...
gi 488409350 225 NQIIEIDQ 232
Cdd:PRK10851 205 DRVVVMSQ 212
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
8-238 |
7.98e-13 |
|
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: 68.08 E-value: 7.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI-------------KIGYLNQ 73
Cdd:COG1127 10 NLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgQDItglsekelyelrrRIGMLFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 74 IP---DyekSESVYQCIksVF--KELDTISKqletietKMIEEReninslvarygelqtyyeenggyeIDAKIRKVthGL 148
Cdd:COG1127 90 GGalfD---SLTVFENV--AFplREHTDLSE-------AEIREL------------------------VLEKLELV--GL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 149 -NIAHLLKAkwgDLSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLD-VKSIEwLASYIKN-NDS---ATVIVSHDRYFLD 221
Cdd:COG1127 132 pGAADKMPS---ELSGGMRKRVALARALAlDP-EILLYDEPTAGLDpITSAV-IDELIRElRDElglTSVVVTHDLDSAF 206
|
250
....*....|....*..
gi 488409350 222 ETVNQIIEIDQKKLHFY 238
Cdd:COG1127 207 AIADRVAVLADGKIIAE 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-236 |
8.40e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 68.89 E-value: 8.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKY--TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIS-----------WKKDIKI 68
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITvggmvlseetvWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 69 GYLNQIPDYEKSESVYQciksvfkelDTISKQLETI---ETKMIEereninslvarygelqtyyeenggyEIDAKIRKVt 145
Cdd:PRK13635 84 GMVFQNPDNQFVGATVQ---------DDVAFGLENIgvpREEMVE-------------------------RVDQALRQV- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 146 hglNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS-IEWLASY--IKNNDSATVI-VSHDryfLD 221
Cdd:PRK13635 129 ---GMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGrREVLETVrqLKEQKGITVLsITHD---LD 202
|
250
....*....|....*..
gi 488409350 222 ETV--NQIIEIDQKKLH 236
Cdd:PRK13635 203 EAAqaDRVIVMNKGEIL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-230 |
8.66e-13 |
|
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: 66.30 E-value: 8.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKkdikigylnqipdyeksesv 83
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 yqciksvfkeldtiskqletietkmiEERENINSLvarygelqtyyeenggyeIDAKirkvTHGLNIAHllkakwgDLSG 163
Cdd:cd03216 61 --------------------------GKEVSFASP------------------RDAR----RAGIAMVY-------QLSV 85
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVI-VSHdryFLDEtvnqIIEI 230
Cdd:cd03216 86 GERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRlrAQGVAVIfISH---RLDE----VFEI 148
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
8-192 |
9.89e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKIG--YLNQIPDYEKSesvyq 85
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSG------DLFIGekRMNDVPPAERG----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 cIKSVFKELdtiskqletietkmieereninslvARYGELQTYyeENGGY----------EIDAKIRKVTHGLNIAHLLK 155
Cdd:PRK11000 77 -VGMVFQSY-------------------------ALYPHLSVA--ENMSFglklagakkeEINQRVNQVAEVLQLAHLLD 128
|
170 180 190
....*....|....*....|....*....|....*..
gi 488409350 156 AKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:PRK11000 129 RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-192 |
1.11e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdiKIGYlnQIPDYEKSESVYQC 86
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKIT-----VLGV--PVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 87 IKSVFKELDtiskqLE-TIetkmieeRENInsLV-ARYGELQTYyeenggyEIDAKIRKVthgLNIAHLLK---AKWGDL 161
Cdd:PRK13536 118 VVPQFDNLD-----LEfTV-------RENL--LVfGRYFGMSTR-------EIEAVIPSL---LEFARLESkadARVSDL 173
|
170 180 190
....*....|....*....|....*....|.
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
332-390 |
1.59e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 67.41 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAY-----------DDVL------------FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkELLLrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
..
gi 488409350 389 KT 390
Cdd:COG1134 84 EV 85
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
350-508 |
1.76e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 67.17 E-value: 1.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 350 VNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSiDKGSIK---------TASNL--KIGYLSQHEferdgndtlLHTFRK 418
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILlngrplsdwSAAELarHRAYLSQQQ---------SPPFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 419 KV----------NVSEDQARHILAH----FM---FYGKDVfkkvNELSGGEKIRLRWA----QL---VNTDYNLLVLDEP 474
Cdd:COG4138 85 PVfqylalhqpaGASSEAVEQLLAQlaeaLGledKLSRPL----TQLSGGEWQRVRLAavllQVwptINPEGQLLLLDEP 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 475 TNHLDIdAKEIIEDALL----DFNGTIITVSHDryfLN 508
Cdd:COG4138 161 MNSLDV-AQQAALDRLLrelcQQGITVVMSSHD---LN 194
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
354-508 |
1.77e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 354 IRRGEHVAIIGDNGTGKTTLLKIILGLTSiDKGSIK---------TASNLKI--GYLSQHE---FERDGNDTL-LHTFRK 418
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQfagqpleawSAAELARhrAYLSQQQtppFAMPVFQYLtLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 419 KVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWA----QL---VNTDYNLLVLDEPTNHLDIdAKEIIEDALL 491
Cdd:PRK03695 98 TRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAavvlQVwpdINPAGQLLLLDEPMNSLDV-AQQAALDRLL 176
|
170 180
....*....|....*....|.
gi 488409350 492 D----FNGTIITVSHDryfLN 508
Cdd:PRK03695 177 SelcqQGIAVVMSSHD---LN 194
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-188 |
1.91e-12 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 66.93 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTE-DILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIK----------- 67
Cdd:COG0410 1 MPMLEVENLHAGYGGiHVLHG-VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDgEDITglpphriarlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 68 IGYlnqIPdyEKSEsvyqciksVFKELdtiskqleTIEtkmieerENInsLVARYGelqtyyeENGGYEIDAKIRKVtHG 147
Cdd:COG0410 80 IGY---VP--EGRR--------IFPSL--------TVE-------ENL--LLGAYA-------RRDRAEVRADLERV-YE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488409350 148 L--NIAHLLKAKWGDLSGGERtkvgiaQML-------IKPtDLLLLDEPT 188
Cdd:COG0410 122 LfpRLKERRRQRAGTLSGGEQ------QMLaigralmSRP-KLLLLDEPS 164
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-204 |
1.96e-12 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 66.62 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 6 ASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkKDIKIGYlnqipDYEK-SESVY 84
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSG-----RATVAGH-----DVVRePREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 85 QCIKSVFKELdTISKQLETietkmieeRENinslVARYGELQTYyeenGGYEIDAKIRKVTHGLNIAHLLKAKWGDLSGG 164
Cdd:cd03265 73 RRIGIVFQDL-SVDDELTG--------WEN----LYIHARLYGV----PGAERRERIDELLDFVGLLEAADRLVKTYSGG 135
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488409350 165 ERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK 204
Cdd:cd03265 136 MRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIE 175
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
332-502 |
2.01e-12 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 66.84 E-value: 2.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-----VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTA---------SNL--- 394
Cdd:cd03258 1 MIELKNVSKVFGDtggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtdltllsgKELrka 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 --KIGYLSQHeF----ERD--GNDTL----LHTFRKKVnvsEDQARHILAHFMFYGKDVFKKvNELSGGEKIRLRWAQLV 462
Cdd:cd03258 81 rrRIGMIFQH-FnllsSRTvfENVALpleiAGVPKAEI---EERVLELLELVGLEDKADAYP-AQLSGGQKQRVGIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488409350 463 NTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG----TIITVSH 502
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRelglTIVLITH 199
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-217 |
2.29e-12 |
|
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: 69.24 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 24 ITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigyLNQIPDYEKSESVYQciksvfkelDTIS--KQL 101
Cdd:TIGR02857 343 FTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIA---------VNGVPLADADADSWR---------DQIAwvPQH 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 102 ETIETKMIeeRENInsLVARygelqtyyeengGYEIDAKIRKVTHGLNIAHLLKA-------KWGD----LSGGERTKVG 170
Cdd:TIGR02857 405 PFLFAGTI--AENI--RLAR------------PDASDAEIREALERAGLDEFVAAlpqgldtPIGEggagLSGGQAQRLA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488409350 171 IAQMLIKPTDLLLLDEPTNHLD-------VKSIEWLAsyiknNDSATVIVSHDR 217
Cdd:TIGR02857 469 LARAFLRDAPLLLLDEPTAHLDaeteaevLEALRALA-----QGRTVLLVTHRL 517
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-194 |
2.36e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 68.71 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDikigyLNQIPDYEKSe 81
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgVD-----LSHVPPYQRP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqcIKSVFKELDTISKQleTIEtkmieerENInslvaRYGELQTYYEENggyEIDAKIRKVTHGLNIAHLLKAKWGDL 161
Cdd:PRK11607 93 -----INMMFQSYALFPHM--TVE-------QNI-----AFGLKQDKLPKA---EIASRVNEMLGLVHMQEFAKRKPHQL 150
|
170 180 190
....*....|....*....|....*....|...
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVK 194
Cdd:PRK11607 151 SGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
333-502 |
2.45e-12 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 66.24 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL-----FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----------KTASNLKIG 397
Cdd:cd03266 2 ITADALTKRFRDVKktvqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFAtvdgfdvvkePAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 YLSQHE--FERDGNDTLLHTFRKKVNVSEDQAR---HILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLD 472
Cdd:cd03266 82 FVSDSTglYDRLTARENLEYFAGLYGLKGDELTarlEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190
....*....|....*....|....*....|...
gi 488409350 473 EPTNHLDIDAKEIIED---ALLDFNGTIITVSH 502
Cdd:cd03266 162 EPTTGLDVMATRALREfirQLRALGKCILFSTH 194
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
24-400 |
2.86e-12 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.89 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 24 ITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkdikigylnqipdyEKSESVYQCIKSVFKELDT-ISKQLE 102
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSG-------------------ERQSQFSHITRLSFEQLQKlVSDEWQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 103 TIETKMIEERENINSLVARygE-LQTYYEENGGYEIDAKIrkvthgLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDL 181
Cdd:PRK10938 85 RNNTDMLSPGEDDTGRTTA--EiIQDEVKDPARCEQLAQQ------FGITALLDRRFKYLSTGETRKTLLCQALMSEPDL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 182 LLLDEPTNHLDVKSIEWLASYIKNndsatviVSHDRYFLDETVNQIIEIDqkklhfyngNYSYFVEERDKRLLIEfeayk 261
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLAS-------LHQSGITLVLVLNRFDEIP---------DFVQFAGVLADCTLAE----- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 262 tQQKKIKKMKES-IKQLrtwasqakppnaamfrrAKSmEKALNriqrLEKPLLDSKKMHITLEEGMNvsnrVIEMENVTK 340
Cdd:PRK10938 216 -TGEREEILQQAlVAQL-----------------AHS-EQLEG----VQLPEPDEPSARHALPANEP----RIVLNNGVV 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 341 AYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILG-----------LTSIDKGSIKTASNLK--IGYLS 400
Cdd:PRK10938 269 SYNDrPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGSGETIWDIKkhIGYVS 342
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
289-502 |
3.16e-12 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 68.97 E-value: 3.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 289 AAMFRRAKSMEKALNRIQRLEKP------LLDSKkmhITLEEGMNVSNRV---IEMENVTKAY--DDV-LFRNVNMLIRR 356
Cdd:TIGR02203 281 IALIRPLKSLTNVNAPMQRGLAAaeslftLLDSP---PEKDTGTRAIERArgdVEFRNVTFRYpgRDRpALDSISLVIEP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 357 GEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI---------KTASNLK--IGYLSQHEFERdgNDTLLHTFR--KKVNVS 423
Cdd:TIGR02203 358 GETVALVGRSGSGKSTLVNLIPRFYEPDSGQIlldghdladYTLASLRrqVALVSQDVVLF--NDTIANNIAygRTEQAD 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 424 EDQARHILAhfMFYGKDVFKKVNE------------LSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDAL- 490
Cdd:TIGR02203 436 RAEIERALA--AAYAQDFVDKLPLgldtpigengvlLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALe 513
|
250
....*....|...
gi 488409350 491 -LDFNGTIITVSH 502
Cdd:TIGR02203 514 rLMQGRTTLVIAH 526
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
354-510 |
4.08e-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: 66.28 E-value: 4.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 354 IRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTaSNLKIGYLSQhEFERDGNDTLLHTFRKKVNVSEDQArhilah 433
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI-ELDTVSYKPQ-YIKADYEGTVRDLLSSITKDFYTHP------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 434 fmFYGKDVFK----------KVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDID----AKEIIEDALLDFNGTIIT 499
Cdd:cd03237 94 --YFKTEIAKplqieqildrEVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlmASKVIRRFAENNEKTAFV 171
|
170
....*....|.
gi 488409350 500 VSHDRYFLNKL 510
Cdd:cd03237 172 VEHDIIMIDYL 182
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
348-503 |
4.12e-12 |
|
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: 65.95 E-value: 4.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 348 RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIktasnlkigYLSQHEFERDGNDTLL----------HTFR 417
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGV---------ILEGKQITEPGPDRMVvfqnysllpwLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 418 KKVNVSEDQARHILA----------HFMFYG--KDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEI 485
Cdd:TIGR01184 73 ENIALAVDRVLPDLSkserraiveeHIALVGltEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
|
170 180
....*....|....*....|..
gi 488409350 486 IEDALL----DFNGTIITVSHD 503
Cdd:TIGR01184 153 LQEELMqiweEHRVTVLMVTHD 174
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-214 |
4.24e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 67.06 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK------KDI-KIGYLnqiP 75
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgepldpEDRrRIGYL---P 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 76 D----YeKSESVYQCIkSVFKELDTISKQletietkmiEERENINSLVARygelqtyyeenggyeidakirkvthgLNIA 151
Cdd:COG4152 78 EerglY-PKMKVGEQL-VYLARLKGLSKA---------EAKRRADEWLER--------------------------LGLG 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 152 HLLKAKWGDLSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIVS 214
Cdd:COG4152 121 DRANKKVEELSKGNQQKVQLIAALLhDP-ELLILDEPFSGLDPVNVELLKDVIRelAAKGTTVIFS 185
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-192 |
4.46e-12 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 65.59 E-value: 4.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 21 HIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigyLNQIpDYEKSESVYQCIKSVFKELDTISKQ 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVL---------INGV-DVTAAPPADRPVSMLFQENNLFAHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 101 leTIETkmieereniNSLVARYGELQTYYEENGgyeidaKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTD 180
Cdd:cd03298 86 --TVEQ---------NVGLGLSPGLKLTAEDRQ------AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKP 148
|
170
....*....|..
gi 488409350 181 LLLLDEPTNHLD 192
Cdd:cd03298 149 VLLLDEPFAALD 160
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
19-230 |
4.63e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 68.27 E-value: 4.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 19 FDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDIKigylnqipDYEKsESVYQCIKSVFKE--L- 94
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdGVDIR--------DLTL-ESLRRQIGVVPQDtfLf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 -DTIskqletietkmieeRENInslvaRYGELQTYYEE--------NggyeIDAKIRKVTHGLNiaHLLKAKWGDLSGGE 165
Cdd:COG1132 427 sGTI--------------RENI-----RYGRPDATDEEveeaakaaQ----AHEFIEALPDGYD--TVVGERGVNLSGGQ 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 166 RTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNN--DSATVIVSH--------DR-YFLDEtvNQIIEI 230
Cdd:COG1132 482 RQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLmkGRTTIVIAHrlstirnaDRiLVLDD--GRIVEQ 555
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
333-503 |
6.06e-12 |
|
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: 65.34 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLKIgylsqheFERD 407
Cdd:cd03300 1 IELENVSKFYGGfVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEIlldgKDITNLPP-------HKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 408 GNdTLLHTF-----------------RKKVNVSEDQAR-HILAHFMFYGKDVFKKVNELSGGEKIRLRWAQ-LVNtDYNL 468
Cdd:cd03300 74 VN-TVFQNYalfphltvfeniafglrLKKLPKAEIKERvAEALDLVQLEGYANRKPSQLSGGQQQRVAIARaLVN-EPKV 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 469 LVLDEPTNHLDIDAKEIIE---DALLDFNG-TIITVSHD 503
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQlelKRLQKELGiTFVFVTHD 190
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
332-503 |
6.28e-12 |
|
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: 64.38 E-value: 6.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYddvLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIktasnlkigylsqhefERDGNDT 411
Cdd:cd03215 4 VLEVRGLSVKG---AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEI----------------TLDGKPV 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 LLHTFRKKVN-----VSEDQARH------------ILAHFmfygkdvfkkvneLSGG--EKIRL-RWaqlVNTDYNLLVL 471
Cdd:cd03215 65 TRRSPRDAIRagiayVPEDRKREglvldlsvaeniALSSL-------------LSGGnqQKVVLaRW---LARDPRVLIL 128
|
170 180 190
....*....|....*....|....*....|....*
gi 488409350 472 DEPTNHLDIDAKEIIEDALLDF---NGTIITVSHD 503
Cdd:cd03215 129 DEPTRGVDVGAKAEIYRLIRELadaGKAVLLISSE 163
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
326-504 |
7.25e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 65.12 E-value: 7.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 326 MNVSNRVIEMENVT-KAYDDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLK----- 395
Cdd:PRK10247 1 MQENSPLLQLQNVGyLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegEDISTLKpeiyr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 396 --IGYLSQHE--FERDGNDTLLHTFR-KKVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLrwAQLVNTDY--NL 468
Cdd:PRK10247 81 qqVSYCAQTPtlFGDTVYDNLIFPWQiRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRI--SLIRNLQFmpKV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488409350 469 LVLDEPTNHLDIDAK----EIIEDALLDFNGTIITVSHDR 504
Cdd:PRK10247 159 LLLDEITSALDESNKhnvnEIIHRYVREQNIAVLWVTHDK 198
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-60 |
7.75e-12 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 65.49 E-value: 7.75e-12
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488409350 19 FDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI 60
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-221 |
7.78e-12 |
|
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: 65.47 E-value: 7.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 28 SGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI----SWKKDIKIGYLNQIPDY---EKSESVYQCIKSVFkeLDTISKQ 100
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppDWDEILDEFRGSELQNYftkLLEGDVKVIVKPQY--VDLIPKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 101 LEtietkmieereninslvARYGELQTYYEENGgyeidaKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTD 180
Cdd:cd03236 103 VK-----------------GKVGELLKKKDERG------KLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488409350 181 LLLLDEPTNHLDVKSIEWLASYIK---NNDSATVIVSHDRYFLD 221
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRelaEDDNYVLVVEHDLAVLD 203
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
333-388 |
9.44e-12 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 66.64 E-value: 9.44e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 333 IEMENVTKAYDDVLF-RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:COG3839 4 LELENVSKSYGGVEAlKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEI 60
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-192 |
1.02e-11 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 65.01 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTED-ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDI----------KIGYlnqi 74
Cdd:cd03295 4 ENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgEDIreqdpvelrrKIGY---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 pdyeksesVYQCIkSVFKELdtiskqleTIEtkmieerENInSLVARygeLQTYYEEnggyEIDAKIRKVTH--GLNIAH 152
Cdd:cd03295 80 --------VIQQI-GLFPHM--------TVE-------ENI-ALVPK---LLKWPKE----KIRERADELLAlvGLDPAE 127
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488409350 153 LLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:cd03295 128 FADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-215 |
1.07e-11 |
|
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: 64.22 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK---KDI----KIGYLnqiPD 76
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgkpLDIaarnRIGYL---PE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 77 ----YEKSESVYQCIksVFKELDTISKQletietkmiEERENINSLVARYGelqtyyeenggyeidakirkvthglnIAH 152
Cdd:cd03269 78 erglYPKMKVIDQLV--YLAQLKGLKKE---------EARRRIDEWLERLE--------------------------LSE 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 153 LLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSH 215
Cdd:cd03269 121 YANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIrelARAGKTVILSTH 186
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
350-503 |
1.13e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.80 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 350 VNMLIRRGEHVAIIGDNGTGKTTLLKIILGLtsiDKGSIKTASNL------------------KIGYLSQhEFerdgndT 411
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGL---DDGSSGEVSLVgqplhqmdeearaklrakHVGFVFQ-SF------M 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 LLHTFRKKVNV-------------SEDQARHILAHFMFyGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHL 478
Cdd:PRK10584 99 LIPTLNALENVelpallrgessrqSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180
....*....|....*....|....*....
gi 488409350 479 DIDAKEIIEDALL----DFNGTIITVSHD 503
Cdd:PRK10584 178 DRQTGDKIADLLFslnrEHGTTLILVTHD 206
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-216 |
1.28e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQipdyeks 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQ------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 eSVYqciksvfkeLDTiskqletietkmieereNINSLVARYGELQTYYEenggyeiDAKIRKVTHGLNIAHLLKAKWGD 160
Cdd:PRK09544 75 -KLY---------LDT-----------------TLPLTVNRFLRLRPGTK-------KEDILPALKRVQAGHLIDAPMQK 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNN----DSATVIVSHD 216
Cdd:PRK09544 121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLrrelDCAVLMVSHD 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
332-502 |
1.32e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.97 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------------KTASNLKIGY 398
Cdd:COG1129 4 LLEMRGISKSFGGVKaLDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEIlldgepvrfrspRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQ-----------------HEFERDGndtLLHtfRKKVNvseDQARHILAHFMFyGKDVFKKVNELSGGEKirlrwaQL 461
Cdd:COG1129 84 IHQelnlvpnlsvaeniflgREPRRGG---LID--WRAMR---RRARELLARLGL-DIDPDTPVGDLSVAQQ------QL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488409350 462 V------NTDYNLLVLDEPTNHLdiDAKEIieDALLDF------NG-TIITVSH 502
Cdd:COG1129 149 VeiaralSRDARVLILDEPTASL--TEREV--ERLFRIirrlkaQGvAIIYISH 198
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-216 |
1.64e-11 |
|
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: 64.67 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKytedilF------DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIK------ 67
Cdd:COG0411 2 DPLLEVRGLTKR------FgglvavDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgRDITglpphr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 68 -----IGYLNQIPdyeksesvyqcikSVFKELdtiskqleTIetkmieeRENInsLVARYGELQTYYEENGGY------- 135
Cdd:COG0411 76 iarlgIARTFQNP-------------RLFPEL--------TV-------LENV--LVAAHARLGRGLLAALLRlprarre 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 136 --EIDAKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLI-KPtDLLLLDEPT---NHLDVKSI-EWLASyIKNNDS 208
Cdd:COG0411 126 erEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALAtEP-KLLLLDEPAaglNPEETEELaELIRR-LRDERG 203
|
....*....
gi 488409350 209 ATV-IVSHD 216
Cdd:COG0411 204 ITIlLIEHD 212
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
333-507 |
1.67e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 63.64 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV------LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASnlKIGYLSQHEFER 406
Cdd:cd03250 1 ISVEDASFTWDSGeqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--SIAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 407 dgNDTLlhtfrkKVNvsedqarhILAHfMFYGKDVFKKVNE-------------------------LSGGEKIRLRWAQL 461
Cdd:cd03250 79 --NGTI------REN--------ILFG-KPFDEERYEKVIKacalepdleilpdgdlteigekginLSGGQKQRISLARA 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488409350 462 VNTDYNLLVLDEPTNHLDID-AKEIIEDALLDF---NGTIITVSHDRYFL 507
Cdd:cd03250 142 VYSDADIYLLDDPLSAVDAHvGRHIFENCILGLllnNKTRILVTHQLQLL 191
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
289-502 |
1.76e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 66.75 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 289 AAMFRRAKSMEKALNRIQRLEKPLLdskkmHITLEEGmnvsnRVIEMENVT--KAYDDVLFRNVNMLIRRGEHVAIIGDN 366
Cdd:COG4178 329 RATVDRLAGFEEALEAADALPEAAS-----RIETSED-----GALALEDLTlrTPDGRPLLEDLSLSLKPGERLLITGPS 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 367 GTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQHEFERDGN--DTLLHTFRKKvNVSEDQARHILahfmfygkdvfKK 444
Cdd:COG4178 399 GSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQRPYLPLGTlrEALLYPATAE-AFSDAELREAL-----------EA 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 445 VN----------------ELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLD--FNGTIITVSH 502
Cdd:COG4178 467 VGlghlaerldeeadwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREelPGTTVISVGH 542
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
8-501 |
1.81e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKK------DIKIGYLNQIpdyeksE 81
Cdd:PRK09700 10 GIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynklDHKLAAQLGI------G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVYQCIkSVFKELDTiskqLETIETKMIEERENINSLVARYGELQtyyeenggyeIDAKIRKVTHGLNIAhlLKAKWGDL 161
Cdd:PRK09700 84 IIYQEL-SVIDELTV----LENLYIGRHLTKKVCGVNIIDWREMR----------VRAAMMLLRVGLKVD--LDEKVANL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSHdryfldeTVNQIIEIDQKKLHFY 238
Cdd:PRK09700 147 SISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMnqlRKEGTAIVYISH-------KLAEIRRICDRYTVMK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 239 NGNY--SYFVEERDKRLLIEFEAYKTQQKKIKKMKESIKQLRTwasqakppnaamfrraksmekalnriqrlekplldsk 316
Cdd:PRK09700 220 DGSSvcSGMVSDVSNDDIVRLMVGRELQNRFNAMKENVSNLAH------------------------------------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 317 kmhitleegmnvsNRVIEMENVTKaYDDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-------K 389
Cdd:PRK09700 263 -------------ETVFEVRNVTS-RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIrlngkdiS 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 390 TASNLK-----IGYLSqhEFERDgnDTLLHTFRKKVNVS-------------------------EDQARHILAhfmFYGK 439
Cdd:PRK09700 329 PRSPLDavkkgMAYIT--ESRRD--NGFFPNFSIAQNMAisrslkdggykgamglfhevdeqrtAENQRELLA---LKCH 401
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 440 DVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAK-EI--IEDALLDFNGTIITVS 501
Cdd:PRK09700 402 SVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKaEIykVMRQLADDGKVILMVS 466
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
326-503 |
1.93e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.63 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 326 MNVSNRVIEMENVTKAYDD---VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------TASNL-- 394
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNsenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKidgitiSKENLke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 ---KIGYLsqheFERDGNDTLLHTFRKKV-------NVSEDQARHILahfmfygKDVFKKVN----------ELSGGEKI 454
Cdd:PRK13632 81 irkKIGII----FQNPDNQFIGATVEDDIafglenkKVPPKKMKDII-------DDLAKKVGmedyldkepqNLSGGQKQ 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 455 RLRWAQLVNTDYNLLVLDEPTNHLD----IDAKEIIEDALLDFNGTIITVSHD 503
Cdd:PRK13632 150 RVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRKKTLISITHD 202
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
333-503 |
3.89e-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: 62.66 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLK-----IGYLSQ- 401
Cdd:cd03301 1 VELENVTKRFGNVTaLDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIyiggRDVTDLPpkdrdIAMVFQn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 -----HEFERDgNDTLLHTFRKKVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTN 476
Cdd:cd03301 81 yalypHMTVYD-NIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190
....*....|....*....|....*....|.
gi 488409350 477 HLD----IDAKEIIEDALLDFNGTIITVSHD 503
Cdd:cd03301 160 NLDaklrVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
316-501 |
3.94e-11 |
|
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: 66.09 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 316 KKMHITLEegMNVSNRVIEMENVTKAY-----------------------DDVLF------------RNVNMLIRRGEHV 360
Cdd:TIGR01271 378 KEEYKTLE--YNLTTTEVEMVNVTASWdegigelfekikqnnkarkqpngDDGLFfsnfslyvtpvlKNISFKLEKGQLL 455
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 361 AIIGDNGTGKTTLLKIILGLTSIDKGSIKTASnlKIGYLSQHEFERDGN--DTLL-----HTFRKKVNVSEDQARHILAH 433
Cdd:TIGR01271 456 AVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG--RISFSPQTSWIMPGTikDNIIfglsyDEYRYTSVIKACQLEEDIAL 533
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 434 FMFYGKDVFKKVN-ELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDI-DAKEIIEDAL--LDFNGTIITVS 501
Cdd:TIGR01271 534 FPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVvTEKEIFESCLckLMSNKTRILVT 605
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
6-216 |
4.53e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 63.95 E-value: 4.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 6 ASNISKKY-----TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIKIGYLNQIPDYEK 79
Cdd:PRK13651 5 VKNIVKIFnkklpTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfKDEKNKKKTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SESVYQCIKS-VFKELDTISKQL-------------ETIETKMIeereninslvarYGELQTYYEENGGYEIDAKIRKVT 145
Cdd:PRK13651 85 EKLVIQKTRFkKIKKIKEIRRRVgvvfqfaeyqlfeQTIEKDII------------FGPVSMGVSKEEAKKRAAKYIELV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 146 hGLNIAHLLKAKWgDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD---VKSIEWLASYIKNNDSATVIVSHD 216
Cdd:PRK13651 153 -GLDESYLQRSPF-ELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpqgVKEILEIFDNLNKQGKTIILVTHD 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-231 |
4.66e-11 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 62.84 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MN-ILNASNISKKYT------------EDILFdhikiTLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKK--- 64
Cdd:COG4778 1 MTtLLEVENLSKTFTlhlqggkrlpvlDGVSF-----SVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdgg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 65 --DI--------------KIGYLNQipdyeksesvyqciksvFkeLDTISKQ--LETIETKMIE---EREninslVARyg 123
Cdd:COG4778 76 wvDLaqaspreilalrrrTIGYVSQ-----------------F--LRVIPRVsaLDVVAEPLLErgvDRE-----EAR-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 124 elqtyyeenggyeidAKIRKVTHGLNIAHLLkakWgDL-----SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEW 198
Cdd:COG4778 130 ---------------ARARELLARLNLPERL---W-DLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAV 190
|
250 260 270
....*....|....*....|....*....|....*.
gi 488409350 199 LASYI---KNNDSATVIVSHDRYFLDETVNQIIEID 231
Cdd:COG4778 191 VVELIeeaKARGTAIIGIFHDEEVREAVADRVVDVT 226
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-216 |
4.68e-11 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 63.13 E-value: 4.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILnASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW------KKDIK---IGYL 71
Cdd:cd03296 1 MSIE-VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatDVPVQernVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 72 NQipDYeksesvyqcikSVFKELdTIskqletietkmieeRENINslvarYG-ELQTYYEENGGYEIDAKIRKVTHGLNI 150
Cdd:cd03296 80 FQ--HY-----------ALFRHM-TV--------------FDNVA-----FGlRVKPRSERPPEAEIRAKVHELLKLVQL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 151 AHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIE----WLASYIKNNDSATVIVSHD 216
Cdd:cd03296 127 DWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKelrrWLRRLHDELHVTTVFVTHD 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-249 |
5.08e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 63.11 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMerpSTGVISWKKDIKI--------GYLNQi 74
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGL---ITGDKSAGSHIELlgrtvqreGRLAR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 pDYEKSESVYQCIksvFKELDTISKqLETIEtkmieereniNSLVARYGE-------LQTYYEENGGYEIDAKIRkvthg 147
Cdd:PRK09984 80 -DIRKSRANTGYI---FQQFNLVNR-LSVLE----------NVLIGALGStpfwrtcFSWFTREQKQRALQALTR----- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 148 LNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASY---IKNNDSATVIVS-HDRYFLDET 223
Cdd:PRK09984 140 VGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTlrdINQNDGITVVVTlHQVDYALRY 219
|
250 260
....*....|....*....|....*.
gi 488409350 224 VNQIIEIDQKKLhFYNGNYSYFVEER 249
Cdd:PRK09984 220 CERIVALRQGHV-FYDGSSQQFDNER 244
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
347-519 |
5.56e-11 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 62.55 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 347 FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKT----ASNLKIGYLSQHEFE-RDgNDTLLHTFRkkvN 421
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVrgrvSSLLGLGGGFNPELTgRE-NIYLNGRLL---G 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 422 VSEDQARHIL---AHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPT----NHLDIDAKEIIEDaLLDFN 494
Cdd:cd03220 114 LSRKEIDEKIdeiIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdAAFQEKCQRRLRE-LLKQG 192
|
170 180
....*....|....*....|....*
gi 488409350 495 GTIITVSHDRYFLNKLFNTTYLLKN 519
Cdd:cd03220 193 KTVILVSHDPSSIKRLCDRALVLEK 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
332-503 |
5.85e-11 |
|
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: 63.13 E-value: 5.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAY------DDVLFRnvnmlIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-------------KTAS 392
Cdd:COG0411 4 LLEVRGLTKRFgglvavDDVSLE-----VERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIlfdgrditglpphRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 393 --------------------NLKIGYLSQHEFERDGNDTLLHTFRKKVNVSEDQARHILAHFMFYGKdVFKKVNELSGGE 452
Cdd:COG0411 79 lgiartfqnprlfpeltvleNVLVAAHARLGRGLLAALLRLPRARREEREARERAEELLERVGLADR-ADEPAGNLSYGQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 453 KIRLRWAQLVNTDYNLLVLDEPT---NHLDIDA-KEIIEDALLDFNGTIITVSHD 503
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAaglNPEETEElAELIRRLRDERGITILLIEHD 212
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-232 |
7.37e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.46 E-value: 7.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwKKDIKIgylnqipDYEKS 80
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIR-VGDITI-------DTARS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 ES--------VYQCIKSVFKELDTISKQ--LET-IETKMIEERENINSLVARYGELQTYYEENGgyEIDAKIRKvthgln 149
Cdd:PRK11264 73 LSqqkglirqLRQHVGFVFQNFNLFPHRtvLENiIEGPVIVKGEPKEEATARARELLAKVGLAG--KETSYPRR------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 150 iahllkakwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD-------VKSIEWLASyiknNDSATVIVSHDRYFLDE 222
Cdd:PRK11264 145 -----------LSGGQQQRVAIARALAMRPEVILFDEPTSALDpelvgevLNTIRQLAQ----EKRTMVIVTHEMSFARD 209
|
250
....*....|
gi 488409350 223 TVNQIIEIDQ 232
Cdd:PRK11264 210 VADRAIFMDQ 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
18-216 |
7.47e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 62.88 E-value: 7.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 18 LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdikigYLNQIPDYEKSEsvyqciKSVFKELDTI 97
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEI---------LLDAQPLESWSS------KAFARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 SKQLETIETKMIEEreninsLVA--RY---GELQTYYEENGGyEIDAKIRKVthGLN-IAHLLKakwGDLSGGERTKVGI 171
Cdd:PRK10575 91 PQQLPAAEGMTVRE------LVAigRYpwhGALGRFGAADRE-KVEEAISLV--GLKpLAHRLV---DSLSGGERQRAWI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488409350 172 AQMLIKPTDLLLLDEPTNHLDV-KSIEWLA--SYIKNNDSATVI-VSHD 216
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIaHQVDVLAlvHRLSQERGLTVIaVLHD 207
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-234 |
7.49e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 63.14 E-value: 7.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 15 EDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIS------WKKDIK-------IGYLNQIPDYEkse 81
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIidgvdiTDKKVKlsdirkkVGLVFQYPEYQ--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqciksVFKEldTISKQLETIETKMIEERENINSLVARYGELQtyyeenggyeidakirkvthGLNIAHLLKAKWGDL 161
Cdd:PRK13637 96 --------LFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIV--------------------GLDYEDYKDKSPFEL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN----NDSATVIVSHDRYFLDETVNQIIEIDQKK 234
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElhkeYNMTIILVSHSMEDVAKLADRIIVMNKGK 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
333-388 |
7.95e-11 |
|
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: 62.07 E-value: 7.95e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 333 IEMENVTKAYDD--VLFrNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:cd03224 1 LEVENLNAGYGKsqILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI 57
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
333-502 |
7.99e-11 |
|
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: 62.12 E-value: 7.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVT---KAYDDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-----------KTASNLKIGY 398
Cdd:cd03252 1 ITFEHVRfryKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlaladPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQHE--FERDGNDTLLHT----FRKKVnvsEDQARHILAH-FMF-----YGKDVFKKVNELSGGEKIRLRWAQLVNTDY 466
Cdd:cd03252 81 VLQENvlFNRSIRDNIALAdpgmSMERV---IEAAKLAGAHdFISelpegYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 467 NLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSH 502
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDIcaGRTVIIIAH 195
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-216 |
8.86e-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: 61.87 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIkigylNQIPDYEK-SESVY 84
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDgKDI-----TNLPPHKRpVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 85 QCIkSVFKELDTIskqletietkmieerENInslvaRYGeLQTyyEENGGYEIDAKIRKVTHGLNIAHLLKAKWGDLSGG 164
Cdd:cd03300 79 QNY-ALFPHLTVF---------------ENI-----AFG-LRL--KKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGG 134
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 165 ERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSAT----VIVSHD 216
Cdd:cd03300 135 QQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgitfVFVTHD 190
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
19-61 |
1.05e-10 |
|
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: 61.78 E-value: 1.05e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488409350 19 FDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIS 61
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
17-242 |
1.08e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 64.50 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 17 ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQIP----DYEKSESVY--QCIKSV 90
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHvdglDLSSNPLLYmmRCFPGV 602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 91 fkeldtiskqletIETKMieeRENINSL-VARYGELQTYYEenggyeidakirkvthglniahllkakwgdLSGGERTKV 169
Cdd:PLN03073 603 -------------PEQKL---RAHLGSFgVTGNLALQPMYT------------------------------LSGGQKSRV 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409350 170 GIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKLHFYNGNY 242
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKVTPFHGTF 709
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
335-519 |
1.13e-10 |
|
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: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 335 MENVTKAYDDVLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS--IDKGSIKTasnlkigylsqheferDGNDTL 412
Cdd:cd03213 14 KSSPSKSGKQLL-KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLI----------------NGRPLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 413 LHTFRKKVnvsedqaRHILAHFMFYGKD-VFK------KVNELSGGEKIRLRWA-QLVnTDYNLLVLDEPTNHLD-IDAK 483
Cdd:cd03213 77 KRSFRKII-------GYVPQDDILHPTLtVREtlmfaaKLRGLSGGERKRVSIAlELV-SNPSLLFLDEPTSGLDsSSAL 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 484 EIIE--DALLDFNGTIITVSHD-RYFLNKLFNTTYLLKN 519
Cdd:cd03213 149 QVMSllRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQ 187
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-187 |
1.14e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 61.69 E-value: 1.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDIL-FDhikITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIkigylNQIPDYEKSe 81
Cdd:COG3840 2 LRLDDLTYRYGDFPLrFD---LTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNgQDL-----TALPPAERP- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqcIKSVFKE------LDTiskqletietkmieeRENIN-----SLvaRYGELQTyyeenggyeidAKIRKVTHGLNI 150
Cdd:COG3840 73 -----VSMLFQEnnlfphLTV---------------AQNIGlglrpGL--KLTAEQR-----------AQVEQALERVGL 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 488409350 151 AHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEP 187
Cdd:COG3840 120 AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEP 156
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-235 |
1.22e-10 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 61.95 E-value: 1.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNI-LNasNISKKY-TEDILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikIGY----LNQI 74
Cdd:COG4161 1 MSIqLK--NINCFYgSHQALFD-INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLN------IAGhqfdFSQK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 PDYEKSESVYQCIKSVFKELD-----TISKQLetIET-----KMIEE--RENINSLVARYgELQTYYEenggyeidakiR 142
Cdd:COG4161 72 PSEKAIRLLRQKVGMVFQQYNlwphlTVMENL--IEApckvlGLSKEqaREKAMKLLARL-RLTDKAD-----------R 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 143 KVTHglniahllkakwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIkNNDSAT----VIVSHDRY 218
Cdd:COG4161 138 FPLH--------------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSQTgitqVIVTHEVE 202
|
250
....*....|....*..
gi 488409350 219 FLDETVNQIIEIDQKKL 235
Cdd:COG4161 203 FARKVASQVVYMEKGRI 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-503 |
1.23e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 62.80 E-value: 1.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDdV-------------LFR----------NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:COG4586 1 IIEVENLSKTYR-VyekepglkgalkgLFRreyreveavdDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 389 KTASnlKIGYLSQHEFERD-----GNDT-------LLHTFR--KKV-NVSEDQARHILAHF--MFYGKDVFKK-VNELSG 450
Cdd:COG4586 80 RVLG--YVPFKRRKEFARRigvvfGQRSqlwwdlpAIDSFRllKAIyRIPDAEYKKRLDELveLLDLGELLDTpVRQLSL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 451 GEKIRlrwAQLVNT---DYNLLVLDEPTNHLDIDAKEIIEDALLDFN----GTIITVSHD 503
Cdd:COG4586 158 GQRMR---CELAAAllhRPKILFLDEPTIGLDVVSKEAIREFLKEYNrergTTILLTSHD 214
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
323-502 |
1.24e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.88 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 323 EEGMNVSNRV---IEMENVTKAY---DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------- 389
Cdd:PRK11176 329 DEGKRVIERAkgdIEFRNVTFTYpgkEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILldghdlr 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 390 --TASNLK--IGYLSQ--HEFerdgNDTLLH--TFRKKVNVSEDQARHilAHFMFYGKDVFKKVNE------------LS 449
Cdd:PRK11176 409 dyTLASLRnqVALVSQnvHLF----NDTIANniAYARTEQYSREQIEE--AARMAYAMDFINKMDNgldtvigengvlLS 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 450 GGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDAL--LDFNGTIITVSH 502
Cdd:PRK11176 483 GGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALdeLQKNRTSLVIAH 537
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
343-502 |
1.28e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 343 DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKtasnlkigYLSQ------HEFERD--------G 408
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVL--------WQGEpirrqrDEYHQDllylghqpG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 409 NDTLLHTF-------RKKVNVSEDQARHILAHFMFYG-KDVfkKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDI 480
Cdd:PRK13538 85 IKTELTALenlrfyqRLHGPGDDEALWEALAQVGLAGfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK 162
|
170 180
....*....|....*....|....*
gi 488409350 481 DAKEIIEDAL---LDFNGTIITVSH 502
Cdd:PRK13538 163 QGVARLEALLaqhAEQGGMVILTTH 187
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
302-502 |
1.43e-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: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 302 LNRIQRLEKPLLDSKKMHITleegmNVSNRVIEMENVTKAY---DDVLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIIL 378
Cdd:TIGR01193 448 LNEVYLVDSEFINKKKRTEL-----NNLNGDIVINDVSYSYgygSNIL-SDISLTIKMNSKTTIVGMSGSGKSTLAKLLV 521
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 379 GLTSIDKGSI-----------KTASNLKIGYLSQHEFERDGN--DTLLHTFRKKVNVSEDQARHILAHF--------MFY 437
Cdd:TIGR01193 522 GFFQARSGEIllngfslkdidRHTLRQFINYLPQEPYIFSGSilENLLLGAKENVSQDEIWAACEIAEIkddienmpLGY 601
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 438 GKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLD-IDAKEIIEDALLDFNGTIITVSH 502
Cdd:TIGR01193 602 QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDtITEKKIVNNLLNLQDKTIIFVAH 667
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
340-503 |
1.45e-10 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 61.37 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 340 KAYDDVLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS------IDKG-SIKTAS--------NLKIGYLSQ-HE 403
Cdd:PRK11629 19 SVQTDVL-HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTptsgdvIFNGqPMSKLSsaakaelrNQKLGFIYQfHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 404 FERDGN---DTLLHTFRKKVNVSEDQARhilAHFMFYGKDVFKKVN----ELSGGEKIRLRWAQ-LVNTDyNLLVLDEPT 475
Cdd:PRK11629 98 LLPDFTaleNVAMPLLIGKKKPAEINSR---ALEMLAAVGLEHRANhrpsELSGGERQRVAIARaLVNNP-RLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|..
gi 488409350 476 NHLDIDAKEIIEDALLDFN---GT-IITVSHD 503
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNrlqGTaFLVVTHD 205
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
326-502 |
1.48e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.58 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 326 MNVSNRVIEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS--IDKGSIK------------T 390
Cdd:CHL00131 1 MNKNKPILEIKNLHASVNENeILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILfkgesildlepeE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 391 ASNLKIGYLSQHEFERDG--NDTLL----HTFRKKVNVSEdqarhiLAHFMFYG-----------KDVF--KKVNE-LSG 450
Cdd:CHL00131 81 RAHLGIFLAFQYPIEIPGvsNADFLrlayNSKRKFQGLPE------LDPLEFLEiineklklvgmDPSFlsRNVNEgFSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 451 GEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDA---LLDFNGTIITVSH 502
Cdd:CHL00131 155 GEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGinkLMTSENSIILITH 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-235 |
1.72e-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: 60.02 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDI--LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdikigYLNQIPdyeksE 81
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEI---------TLDGVP-----V 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVYQCiksvfkeldTISKQLETIETKMieereninslvarygelqtyyeenggYEIDAKIRKvthglNIAHllkakwgDL 161
Cdd:cd03247 67 SDLEK---------ALSSLISVLNQRP--------------------------YLFDTTLRN-----NLGR-------RF 99
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKnnDSATVIVSHdRYFLDETVNQIIEIDQKKL 235
Cdd:cd03247 100 SGGERQRLALARILLQDAPIVLLDEPTVGLDPITerqlLSLIFEVLK--DKTLIWITH-HLTGIEHMDKILFLENGKI 174
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
326-503 |
1.97e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 62.94 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 326 MNVSNRVIEMENVTkAYDDVLFRnvnmlIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTA----SNLKIGYLSQ 401
Cdd:PRK09536 4 IDVSDLSVEFGDTT-VLDGVDLS-----VREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAgddvEALSARAASR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 H----------EFERDGNDTLL-----HTFRKKVNVSEDQA-------RHILAHFmfygkdVFKKVNELSGGEKIRLRWA 459
Cdd:PRK09536 78 RvasvpqdtslSFEFDVRQVVEmgrtpHRSRFDTWTETDRAaverameRTGVAQF------ADRPVTSLSGGERQRVLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 460 QLVNTDYNLLVLDEPTNHLDIDAK----EIIEDaLLDFNGTIITVSHD 503
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQvrtlELVRR-LVDDGKTAVAAIHD 198
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
333-502 |
1.98e-10 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 60.45 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYD-DVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---TASNLKIGYLSQHEF---E 405
Cdd:TIGR01189 1 LAARNLACSRGeRMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRwngTPLAEQRDEPHENILylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 406 RDG---------NDTLLHTF--RKKVNVSEDQARHILAHFmfygKDVfkKVNELSGGEKIRLRWAQLVNTDYNLLVLDEP 474
Cdd:TIGR01189 81 LPGlkpelsaleNLHFWAAIhgGAQRTIEDALAAVGLTGF----EDL--PAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 488409350 475 TNHLDIDAKEIIE---DALLDFNGTIITVSH 502
Cdd:TIGR01189 155 TTALDKAGVALLAgllRAHLARGGIVLLTTH 185
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
4-61 |
2.59e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.94 E-value: 2.59e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIS 61
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVR 60
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-485 |
2.99e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.64 E-value: 2.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPST--GVISWKKDIKIGYlnQIPDYEKS 80
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQAS--NIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 EsvyqcIKSVFKELdTISKQLETIETKMIEE------RENINSLVARYGELqtyyeenggyeidakIRKVTHGLNIAhll 154
Cdd:PRK13549 83 G-----IAIIHQEL-ALVKELSVLENIFLGNeitpggIMDYDAMYLRAQKL---------------LAQLKLDINPA--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 155 kAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSHDryfLDEtvnqiieid 231
Cdd:PRK13549 139 -TPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIrdlKAHGIACIYISHK---LNE--------- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 232 qkklhfyngnysyfveerdkrlliefeayktqqkkIKKMKESIKQLRTWASQAKPPNAAMfrrakSMEKALNRIQRLEKP 311
Cdd:PRK13549 206 -----------------------------------VKAISDTICVIRDGRHIGTRPAAGM-----TEDDIITMMVGRELT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 312 LLDSKKMHITLEEgmnvsnrVIEMENVTkAYDDVLFR-----NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGL------ 380
Cdd:PRK13549 246 ALYPREPHTIGEV-------ILEVRNLT-AWDPVNPHikrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAypgrwe 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 381 --TSIDKGSIKT-----ASNLKIGYLSQhEFERDG---------NDTLL----HTFRKKVNVS--EDQARHILAHFMFYG 438
Cdd:PRK13549 318 geIFIDGKPVKIrnpqqAIAQGIAMVPE-DRKRDGivpvmgvgkNITLAaldrFTGGSRIDDAaeLKTILESIQRLKVKT 396
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 488409350 439 KDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAK-EI 485
Cdd:PRK13549 397 ASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKyEI 444
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
333-499 |
3.64e-10 |
|
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: 60.25 E-value: 3.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------------KTASNLKIGYL 399
Cdd:cd03218 1 LRAENLSKRYGKrKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKIlldgqditklpmHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQHeferdgndtllHTFRKKVNVSEDqarhILAHFMFYGKDV---FKKVNE-----------------LSGGEKIRLRWA 459
Cdd:cd03218 81 PQE-----------ASIFRKLTVEEN----ILAVLEIRGLSKkerEEKLEElleefhithlrkskassLSGGERRRVEIA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488409350 460 QLVNTDYNLLVLDEPTNHLD----IDAKEIIEDaLLDFN-GTIIT 499
Cdd:cd03218 146 RALATNPKFLLLDEPFAGVDpiavQDIQKIIKI-LKDRGiGVLIT 189
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-195 |
4.45e-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: 61.27 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 33 GLVGRNGEGKTTLLKLLSGMERPSTGVIS-----W---KKDI-------KIGYlnqipdyeksesvyqciksVFKE---- 93
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRlggevLqdsARGIflpphrrRIGY-------------------VFQEarlf 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 94 --LDTiskqletietkmieeRENInslvaRYGELQTYyEENGGYEIDAkirkVTHGLNIAHLLKAKWGDLSGGERTKVGI 171
Cdd:COG4148 90 phLSV---------------RGNL-----LYGRKRAP-RAERRISFDE----VVELLGIGHLLDRRPATLSGGERQRVAI 144
|
170 180
....*....|....*....|....*
gi 488409350 172 AQ-MLIKPtDLLLLDEPTNHLDVKS 195
Cdd:COG4148 145 GRaLLSSP-RLLLMDEPLAALDLAR 168
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-216 |
5.10e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 60.41 E-value: 5.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKkdikigylNQIPDYEKSE- 81
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQ--------GKPLDYSKRGl 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 -SVYQCIKSVFKELDtisKQLETIEtkmieerenINSLVArygelqtYYEENGGYEIDAKIRKVTHGLNIA---HLLKAK 157
Cdd:PRK13638 73 lALRQQVATVFQDPE---QQIFYTD---------IDSDIA-------FSLRNLGVPEAEITRRVDEALTLVdaqHFRHQP 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 158 WGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN---NDSATVIVSHD 216
Cdd:PRK13638 134 IQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRivaQGNHVIISSHD 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
333-537 |
5.24e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 61.74 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNL----KIGYLSQHEFER- 406
Cdd:TIGR03269 1 IEVKNLTKKFDGKeVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHValceKCGYVERPSKVGe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 407 -----------------DGNDTLLHTFRKKV------------------NVSE--DQARHILAHFMFYGKDVFKKVN--- 446
Cdd:TIGR03269 81 pcpvcggtlepeevdfwNLSDKLRRRIRKRIaimlqrtfalygddtvldNVLEalEEIGYEGKEAVGRAVDLIEMVQlsh 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 447 -------ELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALL----DFNGTIITVSHDRYFLNKLFNTTY 515
Cdd:TIGR03269 161 rithiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeavkASGISMVLTSHWPEVIEDLSDKAI 240
|
250 260
....*....|....*....|..
gi 488409350 516 LLKNKTLEKfEGNYDYIKEKML 537
Cdd:TIGR03269 241 WLENGEIKE-EGTPDEVVAVFM 261
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
332-508 |
5.38e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 60.17 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLK-------IGYL 399
Cdd:PRK13548 2 MLEARNLSVRLGGrTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVrlngRPLADWSpaelarrRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQHEferdgndTLLHTFRkkvnVSE-------------DQARHILAHFM-------FYGKDvfkkVNELSGGEKIRLRWA 459
Cdd:PRK13548 82 PQHS-------SLSFPFT----VEEvvamgraphglsrAEDDALVAAALaqvdlahLAGRD----YPQLSGGEQQRVQLA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 460 ----QL--VNTDYNLLVLDEPTNHLDIDAKEIIEDALLDF----NGTIITVSHDryfLN 508
Cdd:PRK13548 147 rvlaQLwePDGPPRWLLLDEPTSALDLAHQHHVLRLARQLaherGLAVIVVLHD---LN 202
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
301-388 |
8.15e-10 |
|
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: 61.35 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 301 ALNRIQRLEKPL-LDSKKMHITLEEGMNVSNRVIEMENVTKAY----DDVLFR--NVNMLIRRGEHVAIIGDNGTGKTTL 373
Cdd:COG4615 295 ALRKIEELELALaAAEPAAADAAAPPAPADFQTLELRGVTYRYpgedGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTL 374
|
90
....*....|....*
gi 488409350 374 LKIILGLTSIDKGSI 388
Cdd:COG4615 375 AKLLTGLYRPESGEI 389
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
348-510 |
8.22e-10 |
|
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: 59.20 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 348 RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS--IDKGSIKTA----SNLKIG-------YLS-QHEFERDG--NDT 411
Cdd:TIGR01978 17 KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSyeVTSGTILFKgqdlLELEPDeraraglFLAfQYPEEIPGvsNLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 412 LLHTFRKKVNVSEDQARHILAHFMFYGKDVFKK-----------VNE-LSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLD 479
Cdd:TIGR01978 97 FLRSALNARRSARGEEPLDLLDFEKLLKEKLALldmdeeflnrsVNEgFSGGEKKRNEILQMALLEPKLAILDEIDSGLD 176
|
170 180 190
....*....|....*....|....*....|....
gi 488409350 480 IDAKEIIEDALLDF---NGTIITVSHDRYFLNKL 510
Cdd:TIGR01978 177 IDALKIVAEGINRLrepDRSFLIITHYQRLLNYI 210
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-236 |
8.52e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.12 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 26 LNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKdikigylNQIPDYEKSEsvyqcIKSVFKELDTISKQLETIE 105
Cdd:PRK10908 25 MRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSG-------HDITRLKNRE-----VPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 106 TKMIEERENINSLVArygelqtyyeenGGYEIDAKiRKVTHGLNIAHLL-KAKWG--DLSGGERTKVGIAQMLIKPTDLL 182
Cdd:PRK10908 93 DRTVYDNVAIPLIIA------------GASGDDIR-RRVSAALDKVGLLdKAKNFpiQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 183 LLDEPTNHLDVKSIEWLASYIK--NNDSATVIV-SHDRYFLDETVNQIIEIDQKKLH 236
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEefNRVGVTVLMaTHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
22-235 |
9.58e-10 |
|
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: 58.78 E-value: 9.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKIG--YLNQIPDYEKSESVYQCIKSVFKELDTIsk 99
Cdd:cd03254 22 INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKG------QILIDgiDIRDISRKSLRSMIGVVLQDTFLFSGTI-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 100 qletietkmieeRENInslvaRYGELQTYYEEnggYEIDAK-------IRKVTHGLNiaHLLKAKWGDLSGGERTKVGIA 172
Cdd:cd03254 94 ------------MENI-----RLGRPNATDEE---VIEAAKeagahdfIMKLPNGYD--TVLGENGGNLSQGERQLLAIA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 173 QMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIVSHdRYFLDETVNQIIEIDQKKL 235
Cdd:cd03254 152 RAMLRDPKILILDEATSNIDTETEKLIQEALEklMKGRTSIIIAH-RLSTIKNADKILVLDDGKI 215
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-235 |
9.78e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.99 E-value: 9.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKY--TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigyLNQIPDYEKSE 81
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEIL---------LNGQPIADYSE 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVY-QCIKSVFKELDTISKQLetietkmieeRENInsLVARYGElqtyyeenggyeIDAKIRKVTHGLNIAHLLKAK--- 157
Cdd:PRK11160 410 AALrQAISVVSQRVHLFSATL----------RDNL--LLAAPNA------------SDEALIEVLQQVGLEKLLEDDkgl 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 158 --W-GD----LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNdsaTVI-VSHDRYFLdETVN 225
Cdd:PRK11160 466 naWlGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAQNK---TVLmITHRLTGL-EQFD 541
|
250
....*....|
gi 488409350 226 QIIEIDQKKL 235
Cdd:PRK11160 542 RICVMDNGQI 551
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
333-479 |
1.08e-09 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 60.10 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNLKIGYLSQH 402
Cdd:PRK10851 3 IEIANIKKSFGRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRfhgtdvsrlHARDRKVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 E--------FE-----------RDGNDTllHTFRKKVNVSEDQARhiLAHFmfygKDVFKkvNELSGGEKIRLRWAQLVN 463
Cdd:PRK10851 83 YalfrhmtvFDniafgltvlprRERPNA--AAIKAKVTQLLEMVQ--LAHL----ADRYP--AQLSGGQKQRVALARALA 152
|
170
....*....|....*.
gi 488409350 464 TDYNLLVLDEPTNHLD 479
Cdd:PRK10851 153 VEPQILLLDEPFGALD 168
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
336-499 |
1.16e-09 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 58.75 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 336 ENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------------KTASNLKIGYLSQH 402
Cdd:PRK10895 7 KNLAKAYKGrRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 E--FER-DGNDTLLHTFRKKVNVS----EDQARHILAHF-MFYGKDVFKKvnELSGGEKIRLRWAQLVNTDYNLLVLDEP 474
Cdd:PRK10895 87 AsiFRRlSVYDNLMAVLQIRDDLSaeqrEDRANELMEEFhIEHLRDSMGQ--SLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190
....*....|....*....|....*....|
gi 488409350 475 TNHLD----IDAKEIIEDaLLDFN-GTIIT 499
Cdd:PRK10895 165 FAGVDpisvIDIKRIIEH-LRDSGlGVLIT 193
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
8-195 |
1.39e-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: 58.40 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTED---ILfDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK----KDIKIGYL-NQIpdyek 79
Cdd:cd03251 5 NVTFRYPGDgppVL-RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghdvRDYTLASLrRQI----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 sESVYQcikSVFKELDTIskqletietkmieeRENInslvaRYGELqtyyeenggyeiDAKIRKVTHGLNIAHL------ 153
Cdd:cd03251 79 -GLVSQ---DVFLFNDTV--------------AENI-----AYGRP------------GATREEVEEAARAANAhefime 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488409350 154 ----LKAKWGD----LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS 195
Cdd:cd03251 124 lpegYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSALDTES 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-224 |
1.41e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 60.24 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwKKDIKIGYLNqipdyekS 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVL-VAGDDVEALS-------A 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 ESVYQCIKSVFKElDTISKQLeTIETKMIEERENINSLVARYGELQtyyeenggyeiDAKIRKVTHGLNIAHLLKAKWGD 160
Cdd:PRK09536 73 RAASRRVASVPQD-TSLSFEF-DVRQVVEMGRTPHRSRFDTWTETD-----------RAAVERAMERTGVAQFADRPVTS 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD----VKSIEwLASYIKNNDSATVIVSHD-----RYfLDETV 224
Cdd:PRK09536 140 LSGGERQRVLLARALAQATPVLLLDEPTASLDinhqVRTLE-LVRRLVDDGKTAVAAIHDldlaaRY-CDELV 210
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
333-519 |
1.47e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.61 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD----VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNLK--IG 397
Cdd:PRK11160 339 LTLNNVSFTYPDqpqpVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILlngqpiadySEAALRqaIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 YLSQ--HEFerdgNDTLlhtfRK-----KVNVSEDQARHILahfmfygkdvfKKVN--------------------ELSG 450
Cdd:PRK11160 418 VVSQrvHLF----SATL----RDnlllaAPNASDEALIEVL-----------QQVGleklleddkglnawlgeggrQLSG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 451 GEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSHDRYFLNKlFNTTYLLKN 519
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaqNKTVLMITHRLTGLEQ-FDRICVMDN 548
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-195 |
1.61e-09 |
|
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: 58.32 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 17 ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLsgmER---PSTGVISWK-KDIK----------IGYLNQIPDyekses 82
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDgVDIRdlnlrwlrsqIGLVSQEPV------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 VYQCiksvfkeldtiskqleTIetkmieeRENInslvaRYGELQTYYEEN----GGYEIDAKIRKVTHGLNIahLLKAKW 158
Cdd:cd03249 88 LFDG----------------TI-------AENI-----RYGKPDATDEEVeeaaKKANIHDFIMSLPDGYDT--LVGERG 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 488409350 159 GDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS 195
Cdd:cd03249 138 SQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-235 |
1.62e-09 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 60.52 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYT-EDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK----KDIKIGYLNQIPDYE 78
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNgfslKDIDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 79 KSESvYQCIKSVFKELDTISKqlETIETKMIEERENInslvarygelqtyyeenggYEIDAKIRKVTHGLNIAhlLKAKW 158
Cdd:TIGR01193 554 PQEP-YIFSGSILENLLLGAK--ENVSQDEIWAACEI-------------------AEIKDDIENMPLGYQTE--LSEEG 609
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 159 GDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKL 235
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKI 686
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
332-502 |
1.72e-09 |
|
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: 60.53 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAY--DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQHEFERDGn 409
Cdd:TIGR00954 451 GIKFENIPLVTpnGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLG- 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 410 dtllhTFRKKV---NVSEDQAR------------------HILAHFMfyGKDVFKK-VNELSGGEKIRLRWAQLVNTDYN 467
Cdd:TIGR00954 530 -----TLRDQIiypDSSEDMKRrglsdkdleqildnvqltHILEREG--GWSAVQDwMDVLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*
gi 488409350 468 LLVLDEPTNHLDIDAKEIIEDALLDFNGTIITVSH 502
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
335-503 |
1.77e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.54 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 335 MENVTKAYDD--VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASnlkiGYLSQhefERDgnDTL 412
Cdd:PRK11247 15 LNAVSKRYGErtVL-NQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGT----APLAE---ARE--DTR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 413 LhTFR-------KKV--NVS-------EDQARHILAHFmfygkDVFKKVNE----LSGGEKIRLRWAQLVNTDYNLLVLD 472
Cdd:PRK11247 85 L-MFQdarllpwKKVidNVGlglkgqwRDAALQALAAV-----GLADRANEwpaaLSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 488409350 473 EPTNHLD----IDAKEIIEDALLDFNGTIITVSHD 503
Cdd:PRK11247 159 EPLGALDaltrIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-224 |
1.80e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.61 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKYTEDILF--DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkdiKIGYLNQIPDYEK 79
Cdd:PRK13648 6 SIIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--------EIFYNNQAITDDN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SESVYQCIKSVFKEldtiskqletietkmiEERENINSLVArygelqtyYE-----ENGGYEIDAKIRKVTHGLNIAHLL 154
Cdd:PRK13648 78 FEKLRKHIGIVFQN----------------PDNQFVGSIVK--------YDvafglENHAVPYDEMHRRVSEALKQVDML 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 155 -KAKW--GDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVI-VSHDryfLDETV 224
Cdd:PRK13648 134 eRADYepNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVrkvKSEHNITIIsITHD---LSEAM 207
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
346-501 |
2.09e-09 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 58.71 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 346 LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASnlKIGYLSQHEFERDGN--DTLL-----HTFRK 418
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG--RISFSSQFSWIMPGTikENIIfgvsyDEYRY 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 419 KVNVSEDQARHILAHFMFYGKDVFKKVN-ELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDI-DAKEIIEDAL--LDFN 494
Cdd:cd03291 130 KSVVKACQLEEDITKFPEKDNTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVfTEKEIFESCVckLMAN 209
|
....*..
gi 488409350 495 GTIITVS 501
Cdd:cd03291 210 KTRILVT 216
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-221 |
2.14e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.15 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGmerpstgviswkkdikigylnqIPDYEKSESvyqciKSVFKELDTisKQL 101
Cdd:cd03217 19 VNLTIKKGEVHALMGPNGSGKSTLAKTIMG----------------------HPKYEVTEG-----EILFKGEDI--TDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 102 EtietkmIEEReninslvARYGELQTYYEEnggYEIdakirkvtHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDL 181
Cdd:cd03217 70 P------PEER-------ARLGIFLAFQYP---PEI--------PGVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488409350 182 LLLDEPTNHLDVKSIEWLA---SYIKNNDSATVIVSHDRYFLD 221
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAeviNKLREEGKSVLIITHYQRLLD 168
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-188 |
2.38e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 59.66 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK---------KD-IK--IGY 70
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirspRDaIAlgIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 71 LNQ----IPDYekseSVYqciksvfkeldtiskqletietkmieerENInsLVARygelqtyyEENGGYEID-----AKI 141
Cdd:COG3845 85 VHQhfmlVPNL----TVA----------------------------ENI--VLGL--------EPTKGGRLDrkaarARI 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488409350 142 RKV--THGLNIAhlLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPT 188
Cdd:COG3845 123 RELseRYGLDVD--PDAKVEDLSVGEQQRVEILKALYRGARILILDEPT 169
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
361-510 |
2.48e-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: 57.23 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 361 AIIGDNGTGKTTLLKIIL----GLTSIDKGSIK-----TASNLKIGYLSQHEFERDGNDTL----LHTFRKKVNVSEDQA 427
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltGELPPNSKGGAhdpklIREGEVRAQVKLAFENANGKKYTitrsLAILENVIFCHQGES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 428 RHILahfmfygkdvFKKVNELSGGEK------IRLRWAQLVNTDYNLLVLDEPTNHLD---IDAK--EIIEDALLDFNGT 496
Cdd:cd03240 106 NWPL----------LDMRGRCSGGEKvlasliIRLALAETFGSNCGILALDEPTTNLDeenIEESlaEIIEERKSQKNFQ 175
|
170
....*....|....
gi 488409350 497 IITVSHDRYFLNKL 510
Cdd:cd03240 176 LIVITHDEELVDAA 189
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-193 |
3.21e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdikigYLN--QIPDYEKSE 81
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHV---------WLDgeHIQHYASKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqciksVFKELDTISKQLETIETKMIEEreninsLVAR----YGELQTYYEEnggyEIDAKIRKVTHGLNIAHLLKAK 157
Cdd:PRK10253 79 --------VARRIGLLAQNATTPGDITVQE------LVARgrypHQPLFTRWRK----EDEEAVTKAMQATGITHLADQS 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 488409350 158 WGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDV 193
Cdd:PRK10253 141 VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
20-197 |
3.85e-09 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.18 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDIkigyLNQipDYEKSESVYQCIKSVFKEldtis 98
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlGKDL----LGM--KDDEWRAVRSDIQMIFQD----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 99 kQLETIETKMieereNINSLVARygELQTYYEENGGYEIDAKIR----KVthGLnIAHLLKAKWGDLSGGERTKVGIAQM 174
Cdd:PRK15079 107 -PLASLNPRM-----TIGEIIAE--PLRTYHPKLSRQEVKDRVKammlKV--GL-LPNLINRYPHEFSGGQCQRIGIARA 175
|
170 180
....*....|....*....|...
gi 488409350 175 LIKPTDLLLLDEPTNHLDVkSIE 197
Cdd:PRK15079 176 LILEPKLIICDEPVSALDV-SIQ 197
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
333-502 |
3.99e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.03 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------------KTASNLKIGYL 399
Cdd:PRK09700 6 ISMAGIGKSFGPVhALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTItinninynkldhKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQH-----EFERDGNDTLLHTFRKK---VNVSEDQARHILAHFMF----YGKDVFKKVNELSGGEKIRLRWAQLVNTDYN 467
Cdd:PRK09700 86 YQElsvidELTVLENLYIGRHLTKKvcgVNIIDWREMRVRAAMMLlrvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 468 LLVLDEPTNHL---DIDAKEIIEDALLDFNGTIITVSH 502
Cdd:PRK09700 166 VIIMDEPTSSLtnkEVDYLFLIMNQLRKEGTAIVYISH 203
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
333-502 |
4.08e-09 |
|
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: 57.16 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAY----DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIIL-------GLTSIDKGSIKTAsNL-----KI 396
Cdd:cd03249 1 IEFKNVSFRYpsrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLErfydptsGEILLDGVDIRDL-NLrwlrsQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 397 GYLSQ--HEFERDGNDTLLHTfRKKVNVSEDQ--ARHILAHFmF-------YGKDVFKKVNELSGGEKIRLRWAQLVNTD 465
Cdd:cd03249 80 GLVSQepVLFDGTIAENIRYG-KPDATDEEVEeaAKKANIHD-FimslpdgYDTLVGERGSQLSGGQKQRIAIARALLRN 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 466 YNLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSH 502
Cdd:cd03249 158 PKILLLDEATSALDAESEKLVQEALDRAmkGRTTIVIAH 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
321-388 |
4.15e-09 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 58.42 E-value: 4.15e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 321 TLEEGMNVSNRVIEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSFDGkEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRI 71
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
357-500 |
4.40e-09 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 57.52 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 357 GEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTA-SNLKIgyLSQHE-------FERDGNDTLLHTFRKKV-------- 420
Cdd:TIGR03873 27 GSLTGLLGPNGSGKSTLLRLLAGALRPDAGTVDLAgVDLHG--LSRRArarrvalVEQDSDTAVPLTVRDVValgriphr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 421 -----NVSEDQA--RHILA-----HFmfygkdVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIED 488
Cdd:TIGR03873 105 slwagDSPHDAAvvDRALArtelsHL------ADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLA 178
|
170
....*....|..
gi 488409350 489 ALLDFNGTIITV 500
Cdd:TIGR03873 179 LVRELAATGVTV 190
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
18-215 |
5.12e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 57.44 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 18 LFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdiKIGYLNQIPDYEKSEsvyqcIKSVFKELDTI 97
Cdd:PRK13643 22 LFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKV------TVGDIVVSSTSKQKE-----IKPVRKKVGVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 skqLETIETKMIEEreNINSLVArygelqtYYEENGGYEIDAKIRKVTHGLNIAHLLKAKWG----DLSGGERTKVGIAQ 173
Cdd:PRK13643 90 ---FQFPESQLFEE--TVLKDVA-------FGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEkspfELSGGQMRRVAIAG 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488409350 174 MLIKPTDLLLLDEPTNHLDVKS-IEWLASY--IKNNDSATVIVSH 215
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKArIEMMQLFesIHQSGQTVVLVTH 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
360-503 |
5.43e-09 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 57.81 E-value: 5.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 360 VAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNL---------------KIGYLSQ------HEFERdGNdtlLHTFRK 418
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTlfdsrkgiflppekrRIGYVFQearlfpHLSVR-GN---LRYGMK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 419 KVNVSEDQAR-HILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAK-EII---EDALLDF 493
Cdd:TIGR02142 102 RARPSERRISfERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKyEILpylERLHAEF 181
|
170
....*....|
gi 488409350 494 NGTIITVSHD 503
Cdd:TIGR02142 182 GIPILYVSHS 191
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
333-505 |
6.30e-09 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 56.95 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAY-DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL--KIGYLS 400
Cdd:PRK11231 3 LRTENLTVGYgTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFlgdkpismlSSRQLarRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 401 QHEFERDGNdtllhTFRKKVNV-------------SEDQAR--------HIlAHFmfygkdVFKKVNELSGGEKIRLRWA 459
Cdd:PRK11231 83 QHHLTPEGI-----TVRELVAYgrspwlslwgrlsAEDNARvnqameqtRI-NHL------ADRRLTDLSGGQRQRAFLA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488409350 460 QLVNTDYNLLVLDEPTNHLDIDAKEIIEDAL--LDFNG-TIITVSHD-----RY 505
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMreLNTQGkTVVTVLHDlnqasRY 204
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-216 |
6.62e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 57.17 E-value: 6.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI---------SWKKDIK----IGYLNQIPDYEK-SESVYQCI 87
Cdd:PRK13636 25 ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpidySRKGLMKlresVGMVFQDPDNQLfSASVYQDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 88 KsvfkeldtiskqletietkmieereninslvarYGELQTYYEENggyEIDAKIRKVTHGLNIAHLLKAKWGDLSGGERT 167
Cdd:PRK13636 105 S---------------------------------FGAVNLKLPED---EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 168 KVGIAQMLIKPTDLLLLDEPTNHLDVKSI----EWLASYIKNNDSATVIVSHD 216
Cdd:PRK13636 149 RVAIAGVLVMEPKVLVLDEPTAGLDPMGVseimKLLVEMQKELGLTIIIATHD 201
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
18-215 |
6.81e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.89 E-value: 6.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 18 LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-----KDI-------KIGYLNQIPdYEKSESVYQ 85
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdshnlKDInlkwwrsKIGVVSQDP-LLFSNSIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 CIK-SVF--KELDTISKQLETIETKMIEERENINSLVAR----YGELQTYYEENG------GYEI--DAKIRKVTHGLNI 150
Cdd:PTZ00265 479 NIKySLYslKDLEALSNYYNEDGNDSQENKNKRNSCRAKcagdLNDMSNTTDSNEliemrkNYQTikDSEVVDVSKKVLI 558
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 151 AH-----------LLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSiEWLASYIKNN-----DSATVIVS 214
Cdd:PTZ00265 559 HDfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQKTINNlkgneNRITIIIA 637
|
.
gi 488409350 215 H 215
Cdd:PTZ00265 638 H 638
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
332-504 |
7.40e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.04 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAY--DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIktasnlkigYLSQHEFERDGN 409
Cdd:PRK10908 1 MIRFEHVSKAYlgGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKI---------WFSGHDITRLKN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 410 DTLLHTFRKKVNVSEDQarHILAHFMFY-------------GKDVFKKVN-----------------ELSGGEKIRLRWA 459
Cdd:PRK10908 72 REVPFLRRQIGMIFQDH--HLLMDRTVYdnvaipliiagasGDDIRRRVSaaldkvglldkaknfpiQLSGGEQQRVGIA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 460 QLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNGTIITV---SHDR 504
Cdd:PRK10908 150 RAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVlmaTHDI 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
332-509 |
8.12e-09 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 56.25 E-value: 8.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKG-------SIKTAS------NLKIG 397
Cdd:PRK09493 1 MIEFKNVSKHFGPTqVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGdlivdglKVNDPKvderliRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 YLSQhEFERDGNDTLL--------HTFRKKVNVSEDQARHILAhfmfygkdvfkKV----------NELSGGEKIRLRWA 459
Cdd:PRK09493 81 MVFQ-QFYLFPHLTALenvmfgplRVRGASKEEAEKQARELLA-----------KVglaerahhypSELSGGQQQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 460 QLVNTDYNLLVLDEPTNHLDIDAK-EIIE--DALLDFNGTIITVSHDRYFLNK 509
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRhEVLKvmQDLAEEGMTMVIVTHEIGFAEK 201
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
333-503 |
9.03e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 57.02 E-value: 9.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL------FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNLKIGYLSQHEFER 406
Cdd:PRK13651 3 IKVKNIVKIFNKKLptelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 407 DGNDTLLH-TFRKKVNVSEDQARHILAHFMF--------------------YG----------KDVFKKVN--------- 446
Cdd:PRK13651 83 VLEKLVIQkTRFKKIKKIKEIRRRVGVVFQFaeyqlfeqtiekdiifgpvsMGvskeeakkraAKYIELVGldesylqrs 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 447 --ELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLD-IDAKEIIE--DALLDFNGTIITVSHD 503
Cdd:PRK13651 163 pfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEifDNLNKQGKTIILVTHD 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
8-247 |
9.41e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 55.96 E-value: 9.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTED--ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdIKIGYLNQIPDyekSESVYQ 85
Cdd:cd03252 5 HVRFRYKPDgpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRV-----LVDGHDLALAD---PAWLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 CIKSVFKELDTISKQLetietkmieeRENINSlvARYGELQTYYEE----NGGYEIdakIRKVTHGLNiaHLLKAKWGDL 161
Cdd:cd03252 77 QVGVVLQENVLFNRSI----------RDNIAL--ADPGMSMERVIEaaklAGAHDF---ISELPEGYD--TIVGEQGAGL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSiewlASYIKNN-----DSATVIVSHDRYFLDETVNQIIEID----- 231
Cdd:cd03252 140 SGGQRQRIAIARALIHNPRILIFDEATSALDYES----EHAIMRNmhdicAGRTVIIIAHRLSTVKNADRIIVMEkgriv 215
|
250 260
....*....|....*....|
gi 488409350 232 ----QKKLHFYNGNYSYFVE 247
Cdd:cd03252 216 eqgsHDELLAENGLYAYLYQ 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
332-502 |
1.10e-08 |
|
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: 57.53 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS--------IDKGSIKTASNLK------- 395
Cdd:TIGR02633 1 LLEMKGIVKTFGGVkALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgtwdgeiYWSGSPLKASNIRdteragi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 396 ---------IGYLSQHEFERDGNDTLLHTFRKKVNVSEDQARHILAHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDY 466
Cdd:TIGR02633 81 viihqeltlVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 467 NLLVLDEPTNHLDIDAKEIIEDALLDF---NGTIITVSH 502
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLkahGVACVYISH 199
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
337-503 |
1.11e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 56.96 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 337 NVTKAYDDVLF-RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIdkgsikTASNLKIGylsqheferdgndtllht 415
Cdd:PRK11000 8 NVTKAYGDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDI------TSGDLFIG------------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 416 fRKKVNVSEDQARHI--------------LAHFMFYG--------KDVFKKVNE-----------------LSGGEKIRL 456
Cdd:PRK11000 64 -EKRMNDVPPAERGVgmvfqsyalyphlsVAENMSFGlklagakkEEINQRVNQvaevlqlahlldrkpkaLSGGQRQRV 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488409350 457 RWAQLVNTDYNLLVLDEPTNHLD--IDAKEIIEDALLD--FNGTIITVSHD 503
Cdd:PRK11000 143 AIGRTLVAEPSVFLLDEPLSNLDaaLRVQMRIEISRLHkrLGRTMIYVTHD 193
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
312-502 |
1.14e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 57.55 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 312 LLDSKKMHITLEEGMNVSNRVIEMEN---VTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIdKGS 387
Cdd:PRK11174 327 FLETPLAHPQQGEKELASNDPVTIEAedlEILSPDGkTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 388 IKTA----SNL-------KIGYLSQheferdgNDTLLH-TFRK-----KVNVSEDQARHILAHfmfygkdvfKKVNE--- 447
Cdd:PRK11174 406 LKINgielRELdpeswrkHLSWVGQ-------NPQLPHgTLRDnvllgNPDASDEQLQQALEN---------AWVSEflp 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409350 448 ----------------LSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLD--FNGTIITVSH 502
Cdd:PRK11174 470 llpqgldtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasRRQTTLMVTH 542
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-214 |
1.16e-08 |
|
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: 54.86 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGmERPSTGViswKKDIKIgylNQIPDYEKSesVYQCI 87
Cdd:cd03213 15 SSPSKSGKQLLKN-VSGKAKPGELTAIMGPSGAGKSTLLNALAG-RRTGLGV---SGEVLI---NGRPLDKRS--FRKII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 88 KSVFKElDTISKQLeTIetkmieeRENInslvarygelqtyyeenggyEIDAKIRKvthglniahllkakwgdLSGGERT 167
Cdd:cd03213 85 GYVPQD-DILHPTL-TV-------RETL--------------------MFAAKLRG-----------------LSGGERK 118
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488409350 168 KVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVIVS 214
Cdd:cd03213 119 RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlaDTGRTIICS 167
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-388 |
1.29e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 55.86 E-value: 1.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 333 IEMENVTKAY------DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:COG1101 2 LELKNLSKTFnpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSI 63
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-192 |
1.35e-08 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 56.02 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTED-----ILfDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigyLNQI- 74
Cdd:COG4525 1 MSMLTVRHVSVRYPGGgqpqpAL-QDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEIT---------LDGVp 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 ---PDYEKSesVyqciksVFKE---------LDTISKQLETIETKMIEERENINSLVARYGeLQtyyeengGYEiDAKIr 142
Cdd:COG4525 71 vtgPGADRG--V------VFQKdallpwlnvLDNVAFGLRLRGVPKAERRARAEELLALVG-LA-------DFA-RRRI- 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 488409350 143 kvthglniahllkakWgDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:COG4525 133 ---------------W-QLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
356-507 |
1.43e-08 |
|
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: 53.92 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 356 RGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTAsnlkigylsqheferDGNDTLLHTFRKKVNVsedqarhilahfm 435
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI---------------DGEDILEEVLDQLLLI------------- 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 436 fygkDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDF---------NGTIITVSHDRYF 506
Cdd:smart00382 53 ----IVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRlllllksekNLTVILTTNDEKD 128
|
.
gi 488409350 507 L 507
Cdd:smart00382 129 L 129
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
333-503 |
1.45e-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: 57.45 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAY---DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK----TASNLK-------IGY 398
Cdd:COG4618 331 LSVENLTVVPpgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgaDLSQWDreelgrhIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQ---------------------------------HEF-ER--DGNDTllhtfrkkvNVSEDQARhilahfmfygkdvf 442
Cdd:COG4618 411 LPQdvelfdgtiaeniarfgdadpekvvaaaklagvHEMiLRlpDGYDT---------RIGEGGAR-------------- 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 443 kkvneLSGGEKIRLRWAQLVntdYN---LLVLDEPTNHLDIDAKEIIEDALLDF---NGTIITVSHD 503
Cdd:COG4618 468 -----LSGGQRQRIGLARAL---YGdprLVVLDEPNSNLDDEGEAALAAAIRALkarGATVVVITHR 526
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
349-502 |
1.62e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 56.18 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 349 NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKtasnlkigyLSQHEFERDGNDTLLHTFRKKV-------- 420
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVT---------IGERVITAGKKNKKLKPLRKKVgivfqfpe 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 421 -------------------NVSEDQARHiLAHFMFY----GKDVFKKVN-ELSGGEKIRLRWAQLVNTDYNLLVLDEPTN 476
Cdd:PRK13634 96 hqlfeetvekdicfgpmnfGVSEEDAKQ-KAREMIElvglPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTA 174
|
170 180 190
....*....|....*....|....*....|....
gi 488409350 477 HLDIDA-KEIIEdallDF-------NGTIITVSH 502
Cdd:PRK13634 175 GLDPKGrKEMME----MFyklhkekGLTTVLVTH 204
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
330-503 |
1.87e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 55.79 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 330 NRVIEMENVTKAYDDV---LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNL-----------K 395
Cdd:PRK13635 3 EEIIRVEHISFRYPDAatyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVlseetvwdvrrQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 396 IGYLSQ---------------------HEFERDGNDTLLHTFRKKVNVsEDQARHILAHfmfygkdvfkkvneLSGGEKI 454
Cdd:PRK13635 83 VGMVFQnpdnqfvgatvqddvafglenIGVPREEMVERVDQALRQVGM-EDFLNREPHR--------------LSGGQKQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 455 RLRWAQLVNTDYNLLVLDEPTNHLD----IDAKEIIEDALLDFNGTIITVSHD 503
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDprgrREVLETVRQLKEQKGITVLSITHD 200
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
333-502 |
1.92e-08 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 54.42 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------------KTASNLK-IGY 398
Cdd:cd03231 1 LEADELTCERDGrALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVllnggpldfqrdSIARGLLyLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 -------LSQHEferdgNDTLLHTFRKKVNVSEDQARHILAHFmfygKDVfkKVNELSGGEKIRLRWAQLVNTDYNLLVL 471
Cdd:cd03231 81 apgikttLSVLE-----NLRFWHADHSDEQVEEALARVGLNGF----EDR--PVAQLSAGQQRRVALARLLLSGRPLWIL 149
|
170 180 190
....*....|....*....|....*....|....
gi 488409350 472 DEPTNHLDIDAKEIIEDAL---LDFNGTIITVSH 502
Cdd:cd03231 150 DEPTTALDKAGVARFAEAMaghCARGGMVVLTTH 183
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
20-235 |
2.06e-08 |
|
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: 56.65 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK----KDIKIGYL-NQIPdyeksesvyQCIKSVFKEL 94
Cdd:TIGR02203 349 DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdlADYTLASLrRQVA---------LVSQDVVLFN 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 DTISkqletietkmieerENInslvaRYGELQTYyeenggyeIDAKIRKVTHGLNIAHLLKA-----------KWGDLSG 163
Cdd:TIGR02203 420 DTIA--------------NNI-----AYGRTEQA--------DRAEIERALAAAYAQDFVDKlplgldtpigeNGVLLSG 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNdsATVIVSHdRYFLDETVNQIIEIDQKKL 235
Cdd:TIGR02203 473 GQRQRLAIARALLKDAPILILDEATSALDNESerlvQAALERLMQGR--TTLVIAH-RLSTIEKADRIVVMDDGRI 545
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-235 |
2.09e-08 |
|
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: 54.78 E-value: 2.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 25 TLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkkDIKigylnQIPDYEkSESVYQCIKSVFKE--------LDT 96
Cdd:cd03248 36 TLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL--DGK-----PISQYE-HKYLHSKVSLVGQEpvlfarslQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 97 ISKQLETIETKMIEE---RENINSLVArygELQTYYEENGGyeidakirkvthglniahllkAKWGDLSGGERTKVGIAQ 173
Cdd:cd03248 108 IAYGLQSCSFECVKEaaqKAHAHSFIS---ELASGYDTEVG---------------------EKGSQLSGGQKQRVAIAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 174 MLIKPTDLLLLDEPTNHLDVKSIEWL--ASYIKNNDSATVIVSHdRYFLDETVNQIIEIDQKKL 235
Cdd:cd03248 164 ALIRNPQVLILDEATSALDAESEQQVqqALYDWPERRTVLVIAH-RLSTVERADQILVLDGGRI 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
333-502 |
2.47e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 55.44 E-value: 2.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAY------DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI--------KTASNL---- 394
Cdd:PRK13637 3 IKIENLTHIYmegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIiidgvditDKKVKLsdir 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 -KIGYLSQHE----FErdgnDTLLHTFR---KKVNVSEDQARHILAHFMF---YGKDVFKKVN--ELSGGEKIRLRWAQL 461
Cdd:PRK13637 83 kKVGLVFQYPeyqlFE----ETIEKDIAfgpINLGLSEEEIENRVKRAMNivgLDYEDYKDKSpfELSGGQKRRVAIAGV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488409350 462 VNTDYNLLVLDEPTNHLDIDAKE----IIEDALLDFNGTIITVSH 502
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDeilnKIKELHKEYNMTIILVSH 203
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
332-502 |
2.48e-08 |
|
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: 54.78 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAY----DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLKIGYL---- 399
Cdd:cd03248 11 IVKFQNVTFAYptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVlldgKPISQYEHKYLhskv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 ---SQHE--FERDGNDTL---LHTFRKKVNVSEDQARHilAHFMF------YGKDVFKKVNELSGGEKIRLRWAQLVNTD 465
Cdd:cd03248 91 slvGQEPvlFARSLQDNIaygLQSCSFECVKEAAQKAH--AHSFIselasgYDTEVGEKGSQLSGGQKQRVAIARALIRN 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 466 YNLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSH 502
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWpeRRTVLVIAH 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-194 |
2.65e-08 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 56.11 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIkigylNQIPDyEK 79
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgQDI-----THVPA-EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SE--SVYQCIkSVFKELdTIskqletietkmieeRENinslVArYG-ELQTYYEEnggyEIDAKIRKVTHGLNIAHLLKA 156
Cdd:PRK09452 86 RHvnTVFQSY-ALFPHM-TV--------------FEN----VA-FGlRMQKTPAA----EITPRVMEALRMVQLEEFAQR 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 157 KWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVK 194
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
330-503 |
2.66e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 55.13 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 330 NRVIEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------TASNL-----KI 396
Cdd:PRK13647 2 DNIIEVEDLHFRYKDgtKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKvmgrevNAENEkwvrsKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 397 GYLSQheferDGNDTLLHTfrkkvNVSEDQARHILaHFMFYGKDVFKKVNE-----------------LSGGEKIRLRWA 459
Cdd:PRK13647 82 GLVFQ-----DPDDQVFSS-----TVWDDVAFGPV-NMGLDKDEVERRVEEalkavrmwdfrdkppyhLSYGQKKRVAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 488409350 460 QLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG---TIITVSHD 503
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqgkTVIVATHD 197
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
332-496 |
2.73e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.02 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYD-DVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGS----------------------- 387
Cdd:PRK09984 4 IIRVEKLAKTFNqHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshiellgrtvqregrlardirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 388 -----------------IKTASNLKIGYLSQHEFERdgndTLLHTFRKKVNVSEDQA--RHILAHFmfygkdVFKKVNEL 448
Cdd:PRK09984 84 srantgyifqqfnlvnrLSVLENVLIGALGSTPFWR----TCFSWFTREQKQRALQAltRVGMVHF------AHQRVSTL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 449 SGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNGT 496
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQN 201
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
332-503 |
2.85e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 2.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD----VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------KTASNL-----KI 396
Cdd:PRK13650 4 IIEVKNLTFKYKEdqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdlLTEENVwdirhKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 397 GYLSQH--------------EFERDGNDTLLHTFRKKVNvsedQARHILAHFMFygKDvfKKVNELSGGEKIRLRWAQLV 462
Cdd:PRK13650 84 GMVFQNpdnqfvgatveddvAFGLENKGIPHEEMKERVN----EALELVGMQDF--KE--REPARLSGGQKQRVAIAGAV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488409350 463 NTDYNLLVLDEPTNHLD----IDAKEIIEDALLDFNGTIITVSHD 503
Cdd:PRK13650 156 AMRPKIIILDEATSMLDpegrLELIKTIKGIRDDYQMTVISITHD 200
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-225 |
3.00e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.00 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTEDILF--DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW---------KKDI--KIGYLNQ 73
Cdd:PRK13632 11 ENVSFSYPNSENNalKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiskenLKEIrkKIGIIFQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 74 IPDyeksesvYQCIKSVFKelDTISKQLEtietkmieereniNSLVARygelqtyyeenggYEIDAKIRKVTHGLNIAHL 153
Cdd:PRK13632 91 NPD-------NQFIGATVE--DDIAFGLE-------------NKKVPP-------------KKMKDIIDDLAKKVGMEDY 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 154 LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVK---SIEWLASYIKNNDSATVI-VSHDryfLDETVN 225
Cdd:PRK13632 136 LDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKgkrEIKKIMVDLRKTRKKTLIsITHD---MDEAIL 208
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-235 |
3.38e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.33 E-value: 3.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKIGYLNQIPDYEKSES 82
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSG------DLIVDGLKVNDPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 VYQCIKSVFKELDtISKQLETIETKMieereninslvarYGELQTyyeeNGGYEIDAKirkvthglNIAHLLKAKWG--- 159
Cdd:PRK09493 75 IRQEAGMVFQQFY-LFPHLTALENVM-------------FGPLRV----RGASKEEAE--------KQARELLAKVGlae 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 160 -------DLSGGERTKVGIAQML-IKPTdLLLLDEPTNHLD-------VKSIEWLAsyiknNDSAT-VIVSHDRYFLDET 223
Cdd:PRK09493 129 rahhypsELSGGQQQRVAIARALaVKPK-LMLFDEPTSALDpelrhevLKVMQDLA-----EEGMTmVIVTHEIGFAEKV 202
|
250
....*....|..
gi 488409350 224 VNQIIEIDQKKL 235
Cdd:PRK09493 203 ASRLIFIDKGRI 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
326-503 |
4.17e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 54.76 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 326 MNVSNRVIEMENVTKAYD-DVLF--RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI------KTASNLKi 396
Cdd:PRK13648 1 MEDKNSIIVFKNVSFQYQsDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIfynnqaITDDNFE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 397 gYLSQH---EFERDGNDTLLHTFRKKVNVSedqarhiLAHFMFYGKDVFKKVNE-----------------LSGGEKIRL 456
Cdd:PRK13648 80 -KLRKHigiVFQNPDNQFVGSIVKYDVAFG-------LENHAVPYDEMHRRVSEalkqvdmleradyepnaLSGGQKQRV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488409350 457 RWAQLVNTDYNLLVLDEPTNHLDIDAKE----IIEDALLDFNGTIITVSHD 503
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQnlldLVRKVKSEHNITIISITHD 202
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-192 |
4.45e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 54.30 E-value: 4.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkdikigylnqipdyeksesv 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG------------------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 yqciksvfkELDTISKQLETI--ETKMIEEreninslvarygelqtyyeenggyeiDAKI---RKVTHglNIAHLLKAKW 158
Cdd:PRK11247 68 ---------ELLAGTAPLAEAreDTRLMFQ--------------------------DARLlpwKKVID--NVGLGLKGQW 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 159 GD---------------------LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:PRK11247 111 RDaalqalaavgladranewpaaLSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-264 |
4.47e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.25 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKY-TEDILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdIKIGYLN--QIPDYEKSESV 83
Cdd:PRK11124 6 NGINCFYgAHQALFD-ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLN----IAGNHFDfsKTPSDKAIREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIKSVFKELDtISKQLETIETkMIEERENINSLVARygelqtyyeenggyEIDAKIRKVTHGLNIAHLLKAKWGDLSG 163
Cdd:PRK11124 81 RRNVGMVFQQYN-LWPHLTVQQN-LIEAPCRVLGLSKD--------------QALARAEKLLERLRLKPYADRFPLHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLD-------VKSIEWLAsyikNNDSATVIVSHDRYFLDETVNQIIEIDQkklh 236
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDpeitaqiVSIIRELA----ETGITQVIVTHEVEVARKTASRVVYMEN---- 216
|
250 260
....*....|....*....|....*...
gi 488409350 237 fyngnySYFVEERDKRlliEFEAYKTQQ 264
Cdd:PRK11124 217 ------GHIVEQGDAS---CFTQPQTEA 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-192 |
4.54e-08 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 54.32 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKkdikiGYLNQIPDYEKSes 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-----GKPVEGPGAERG-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 vyqcikSVFKE---------LDTISKQLETIETKMIEERENINSLVARYGelqtyYEENGGYEIdakirkvthglniahl 153
Cdd:PRK11248 74 ------VVFQNegllpwrnvQDNVAFGLQLAGVEKMQRLEIAHQMLKKVG-----LEGAEKRYI---------------- 126
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 154 lkakWgDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:PRK11248 127 ----W-QLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
349-502 |
5.05e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 54.35 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 349 NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNL---------------KIGYLSQHEFERDGNDTLL 413
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVvsstskqkeikpvrkKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 414 HTFR---KKVNVSEDQARHILAHFM--------FYGKDVFkkvnELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDA 482
Cdd:PRK13643 104 KDVAfgpQNFGIPKEKAEKIAAEKLemvgladeFWEKSPF----ELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKA 179
|
170 180
....*....|....*....|...
gi 488409350 483 K-EIIE--DALLDFNGTIITVSH 502
Cdd:PRK13643 180 RiEMMQlfESIHQSGQTVVLVTH 202
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
333-506 |
5.87e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 53.99 E-value: 5.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAY-DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK-------TASNLK-----IGYL 399
Cdd:PRK11264 4 IEVKNLVKKFhGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRvgditidTARSLSqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQH------EFERDGNDTLLH------TFRKKV--NVSEDQARHILAHFMFYGK-DVFKKvnELSGGEKIRLRWAQLVNT 464
Cdd:PRK11264 84 RQHvgfvfqNFNLFPHRTVLEniiegpVIVKGEpkEEATARARELLAKVGLAGKeTSYPR--RLSGGQQQRVAIARALAM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488409350 465 DYNLLVLDEPTNHLDID-AKEIIED--ALLDFNGTIITVSHDRYF 506
Cdd:PRK11264 162 RPEVILFDEPTSALDPElVGEVLNTirQLAQEKRTMVIVTHEMSF 206
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-216 |
5.95e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 54.71 E-value: 5.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIS------WKKDIKigYLNQI-----------PDYEKSES 82
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRvlgyvpFKRRKE--FARRIgvvfgqrsqlwWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 vYQCIKSVFKeldtISKQletietkmiEERENINSLVarygELqtyyeenggyeidakirkvthgLNIAHLLKAKWGDLS 162
Cdd:COG4586 117 -FRLLKAIYR----IPDA---------EYKKRLDELV----EL----------------------LDLGELLDTPVRQLS 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 163 GGERTKVGIAQMLI-KPtDLLLLDEPTNHLDVKS----IEWLASYIKNNDsATVIV-SHD 216
Cdd:COG4586 157 LGQRMRCELAAALLhRP-KILFLDEPTIGLDVVSkeaiREFLKEYNRERG-TTILLtSHD 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
8-215 |
6.22e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.30 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdikigylnqipdyeksesvyqci 87
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSI--------------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 88 ksvfkeldtiskQLETIETKMIEERENINSLVAR-YGELQTYYE----EN---------GGYeIDAKIRKVTHGLNIAHL 153
Cdd:PRK11288 62 ------------LIDGQEMRFASTTAALAAGVAIiYQELHLVPEmtvaENlylgqlphkGGI-VNRRLLNYEAREQLEHL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 154 -----LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN-NDSATVI--VSH 215
Cdd:PRK11288 129 gvdidPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRElRAEGRVIlyVSH 198
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-216 |
7.18e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 7.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWkkdikIGY-LNQIPDYEKSESVYQCIKSVFKELDTIS-- 98
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSL-----VGQpLHQMDEEARAKLRAKHVGFVFQSFMLIPtl 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 99 KQLETIETKMIEERENINSLVARYGELqtyyeenggyeidakIRKVTHGLNIAHLLkakwGDLSGGERTKVGIAQMLIKP 178
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKAL---------------LEQLGLGKRLDHLP----AQLSGGEQQRVALARAFNGR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488409350 179 TDLLLLDEPTNHLDVKSIEWLAS--YIKNNDSAT--VIVSHD 216
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADllFSLNREHGTtlILVTHD 206
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
346-479 |
7.21e-08 |
|
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: 53.43 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 346 LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLtsIDKGSIKTASNL-------------KIGYLSQHEFERDG---N 409
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR--VEGGGTTSGQILfngqprkpdqfqkCVAYVRQDDILLPGltvR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 410 DTLLHT-----------FRKKVNVSEDQARHiLAHFMFYGkdvfKKVNELSGGEKIRLRWA-QLVnTDYNLLVLDEPTNH 477
Cdd:cd03234 100 ETLTYTailrlprkssdAIRKKRVEDVLLRD-LALTRIGG----NLVKGISGGERRRVSIAvQLL-WDPKVLILDEPTSG 173
|
..
gi 488409350 478 LD 479
Cdd:cd03234 174 LD 175
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-188 |
1.00e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 52.96 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKdikigylNQIPDYEKS 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG-------KDITDWQTA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 EsvyqciksVFKELDTISKQLETIETKMIEErENInSLVARYGELQTYYEenggyeidaKIRKVTHGLNIAHLLKA-KWG 159
Cdd:PRK11614 76 K--------IMREAVAIVPEGRRVFSRMTVE-ENL-AMGGFFAERDQFQE---------RIKWVYELFPRLHERRIqRAG 136
|
170 180
....*....|....*....|....*....
gi 488409350 160 DLSGGERTKVGIAQMLIKPTDLLLLDEPT 188
Cdd:PRK11614 137 TMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-235 |
1.08e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 54.73 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 25 TLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKkdikigylNQ-IPDYEkSESVYQCIKSVFKELDTISKQLet 103
Cdd:TIGR00958 503 TLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD--------GVpLVQYD-HHYLHRQVALVGQEPVLFSGSV-- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 104 ietkmieeRENINslvarYGELQTYYEE--NGGYEIDAK--IRKVTHGLNIAhlLKAKWGDLSGGERTKVGIAQMLIKPT 179
Cdd:TIGR00958 572 --------RENIA-----YGLTDTPDEEimAAAKAANAHdfIMEFPNGYDTE--VGEKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 180 DLLLLDEPTNHLDVKsIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQKKL 235
Cdd:TIGR00958 637 RVLILDEATSALDAE-CEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-232 |
1.13e-07 |
|
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: 52.53 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKIGYLNQIPDYEKSESV 83
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSG------TIIIDGLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIKSVFKE---------LDTISKQLETIETKMIEERENInslvarygelqtyyeengGYEIDAKIRkvthglnIAHLL 154
Cdd:cd03262 75 RQKVGMVFQQfnlfphltvLENITLAPIKVKGMSKAEAEER------------------ALELLEKVG-------LADKA 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 155 KAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD---VKSIEWLASYIKNNDSATVIVSHDRYFLDETVNQIIEID 231
Cdd:cd03262 130 DAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMD 209
|
.
gi 488409350 232 Q 232
Cdd:cd03262 210 D 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
348-503 |
1.15e-07 |
|
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: 53.03 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 348 RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK---------TASNL------KIGYLSQHeFERDGNDTL 412
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLidgqdiaamSRKELrelrrkKISMVFQS-FALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 413 LH--TFRKKV-----NVSEDQARHILaHFMFYGKDVFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEI 485
Cdd:cd03294 120 LEnvAFGLEVqgvprAEREERAAEAL-ELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180
....*....|....*....|..
gi 488409350 486 IEDALLDFNG----TIITVSHD 503
Cdd:cd03294 199 MQDELLRLQAelqkTIVFITHD 220
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-62 |
1.17e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.01 E-value: 1.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW 62
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHY 65
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
343-481 |
1.24e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 343 DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-------KTASNLK-IGYLSQHEFERDGNDTL-- 412
Cdd:PRK13543 23 EEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktaTRGDRSRfMAYLGHLPGLKADLSTLen 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 413 ------LHTFRKKVNVSEDQARHILAHFmfygKDVFkkVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDID 481
Cdd:PRK13543 103 lhflcgLHGRRAKQMPGSALAIVGLAGY----EDTL--VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-235 |
1.29e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 54.47 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 25 TLNSGDTLGLVGRNGEGKTTLLKLLSG------------MERPSTGVISWKKdiKIGYLNQIPdyeksesvyqciksvfk 92
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNALLGflpyqgslkingIELRELDPESWRK--HLSWVGQNP----------------- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 93 eldtiskQL--ETIetkmieeRENInsLVARY----GELQTYYEENGGYEIdakIRKVTHGLNiaHLLKAKWGDLSGGER 166
Cdd:PRK11174 433 -------QLphGTL-------RDNV--LLGNPdasdEQLQQALENAWVSEF---LPLLPQGLD--TPIGDQAAGLSVGQA 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 167 TKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNN--DSATVIVSHDRYFLDEtVNQIIEIDQKKL 235
Cdd:PRK11174 492 QRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAsrRQTTLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-235 |
1.44e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.29 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 15 EDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigylnqIPDYEKSesvyqciksvfkeL 94
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTIT------------IAGYHIT-------------P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 DTISKQLETIETKMieereninSLVARYGELQTYYE----------ENGGY-EIDAK------IRKVthGLNIAHLLKAK 157
Cdd:PRK13641 74 ETGNKNLKKLRKKV--------SLVFQFPEAQLFENtvlkdvefgpKNFGFsEDEAKekalkwLKKV--GLSEDLISKSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 158 WgDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDSA--TVI-VSHDRYFLDETVNQIIEIDQKK 234
Cdd:PRK13641 144 F-ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAghTVIlVTHNMDDVAEYADDVLVLEHGK 222
|
.
gi 488409350 235 L 235
Cdd:PRK13641 223 L 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-232 |
1.47e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTT----LLKLLsgmerPSTGVIsWKKDIKIGYLNQ---IPDYEKSESVYQciksvfkel 94
Cdd:PRK15134 305 ISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEI-WFDGQPLHNLNRrqlLPVRHRIQVVFQ--------- 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 DTISKqletietkmIEERENINSLVARygELQTYYEENGGYEIDAKIRKVTHGLNIAHLLKAKW-GDLSGGERTKVGIAQ 173
Cdd:PRK15134 370 DPNSS---------LNPRLNVLQIIEE--GLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHRYpAEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 174 MLIKPTDLLLLDEPTNHLDvKSIE-----WLASYIKNNDSATVIVSHDRYFLDETVNQIIEIDQ 232
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLD-KTVQaqilaLLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
3-218 |
1.54e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI--------SWKKDIKIGYLNQI 74
Cdd:PRK13543 11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIqidgktatRGDRSRFMAYLGHL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 PDYEksesvyqciksvfKELDTIskqletietkmieerENINSLVARYGELQTYYEENG-------GYEiDAKIRKvthg 147
Cdd:PRK13543 91 PGLK-------------ADLSTL---------------ENLHFLCGLHGRRAKQMPGSAlaivglaGYE-DTLVRQ---- 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 148 lniahllkakwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK---NNDSATVIVSHDRY 218
Cdd:PRK13543 138 -------------LSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISahlRGGGAALVTTHGAY 198
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-194 |
1.64e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 52.39 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDIKigylnQIPDYEKSesvyq 85
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVdGLDVA-----TTPSRELA----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 ciksvfKELdTISKQLETIETKM-IEEreninsLVA--RY----GELQTyyeenggyEIDAKIRKVTHGLNIAHLlKAKW 158
Cdd:COG4604 75 ------KRL-AILRQENHINSRLtVRE------LVAfgRFpyskGRLTA--------EDREIIDEAIAYLDLEDL-ADRY 132
|
170 180 190
....*....|....*....|....*....|....*..
gi 488409350 159 GD-LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVK 194
Cdd:COG4604 133 LDeLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMK 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-503 |
1.67e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGViswkkdIKIG---YLNQIPDYEK 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGT------LEIGgnpCARLTPAKAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SESVYQCIKS--VFKELDTiskqLETIETKMIEERENINSLVARYGELQtyyeenggyeidakirkvthglniAHL-LKA 156
Cdd:PRK15439 85 QLGIYLVPQEplLFPNLSV----KENILFGLPKRQASMQKMKQLLAALG------------------------CQLdLDS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 157 KWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK---NNDSATVIVSHdryfldetvnqiieidqk 233
Cdd:PRK15439 137 SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRellAQGVGIVFISH------------------ 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 234 KLHfyngnysyfveerdkrlliefeayktqqkkikkmkeSIKQLRTWASQAKPPNAAMFRRAKSMEK-----ALNRIQRl 308
Cdd:PRK15439 199 KLP------------------------------------EIRQLADRISVMRDGTIALSGKTADLSTddiiqAITPAAR- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 309 EKPLLDSKKMHITLEEGMNVSNR---VIEMENVTKAYddvlFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDK 385
Cdd:PRK15439 242 EKSLSASQKLWLELPGNRRQQAAgapVLTVEDLTGEG----FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARG 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 386 GSI----------KTASNLKIG--YLS----QHEFERDG-----------NDTLLHTFRKKVNVSEDQARHILAhFMFYG 438
Cdd:PRK15439 318 GRImlngkeinalSTAQRLARGlvYLPedrqSSGLYLDAplawnvcalthNRRGFWIKPARENAVLERYRRALN-IKFNH 396
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 439 KDvfKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDF---NGTIITVSHD 503
Cdd:PRK15439 397 AE--QAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIaaqNVAVLFISSD 462
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
332-502 |
1.82e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.78 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS--------IDKGSIKTASNLKigylsqh 402
Cdd:PRK13549 5 LLEMKNITKTFGGVkALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgtyegeiIFEGEELQASNIR------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 EFERDGnDTLLH---TFRKKVNVSED--QARHILAH-FMFYGK----------------DVFKKVNELSGGEKIRLRWAQ 460
Cdd:PRK13549 78 DTERAG-IAIIHqelALVKELSVLENifLGNEITPGgIMDYDAmylraqkllaqlkldiNPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 461 LVNTDYNLLVLDEPTNHLdiDAKE------IIEDaLLDFNGTIITVSH 502
Cdd:PRK13549 157 ALNKQARLLILDEPTASL--TESEtavlldIIRD-LKAHGIACIYISH 201
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
332-503 |
2.18e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.39 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNlKIGYlsqheferdGN 409
Cdd:PRK13639 1 ILETRDLKYSYPDgtEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGE-PIKY---------DK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 410 DTLLHtFRKKV--------------NVSEDQARHILaHFMFYGKDVFKKVNE-----------------LSGGEKIRLRW 458
Cdd:PRK13639 71 KSLLE-VRKTVgivfqnpddqlfapTVEEDVAFGPL-NLGLSKEEVEKRVKEalkavgmegfenkpphhLSGGQKKRVAI 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 459 AQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG---TIITVSHD 503
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKegiTIIISTHD 196
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
17-215 |
2.43e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 17 ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLNQ---IPdyeksesvyqciksvfke 93
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVLFLPQrpyLP------------------ 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 94 LDTIskqletietkmieeRENInslvarygelqTYYEENGGYEiDAKIRKVTHGLNIAHLL-----KAKWGD-LSGGERT 167
Cdd:COG4178 439 LGTL--------------REAL-----------LYPATAEAFS-DAELREALEAVGLGHLAerldeEADWDQvLSLGEQQ 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 488409350 168 KVGIAQMLI-KPtDLLLLDEPTNHLDVKSIEWLASYIKNN-DSATVI-VSH 215
Cdd:COG4178 493 RLAFARLLLhKP-DWLFLDEATSALDEENEAALYQLLREElPGTTVIsVGH 542
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-197 |
2.51e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 52.81 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIkigylnqiPDYEKSE--SVYQCIKSVFKE--- 93
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgQDI--------TGLSGRElrPLRRRMQMVFQDpya 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 94 -LDTiSKQLETIetkmIEERENINSLVARyGELQTYyeenggyeIDAKIRKVthGLNIAHLlkakwgD-----LSGGERT 167
Cdd:COG4608 107 sLNP-RMTVGDI----IAEPLRIHGLASK-AERRER--------VAELLELV--GLRPEHA------DrypheFSGGQRQ 164
|
170 180 190
....*....|....*....|....*....|.
gi 488409350 168 KVGIAQMLI-KPtDLLLLDEPTNHLDVkSIE 197
Cdd:COG4608 165 RIGIARALAlNP-KLIVCDEPVSALDV-SIQ 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-217 |
2.61e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.76 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTED--ILFDHIKITLNSGDTLGLVGRNGEGKTTL----LKLLS--------GMERPSTGVISWKKDIKIg 69
Cdd:TIGR01271 1218 MDVQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLlsalLRLLStegeiqidGVSWNSVTLQTWRKAFGV- 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 70 ylnqIPdyeksESVYQCIKSVFKELDTiSKQLETIETKMIEERENINSLVARYGELQTYYEENGGYEidakirkvthgln 149
Cdd:TIGR01271 1297 ----IP-----QKVFIFSGTFRKNLDP-YEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYV------------- 1353
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 150 iahllkakwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDS-ATVIVSHDR 217
Cdd:TIGR01271 1354 -----------LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSnCTVILSEHR 1411
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
332-504 |
3.07e-07 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 52.53 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI---------------------- 388
Cdd:PRK11607 19 LLEIRNLTKSFDGQHaVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQImldgvdlshvppyqrpinmmfq 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 389 --------KTASNLKIGyLSQHEFERDgndtllhtfRKKVNVSEDQArhiLAHFMFYGKdvfKKVNELSGGEKIRLRWAQ 460
Cdd:PRK11607 99 syalfphmTVEQNIAFG-LKQDKLPKA---------EIASRVNEMLG---LVHMQEFAK---RKPHQLSGGQRQRVALAR 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 461 LVNTDYNLLVLDEPTNHLDIDAKEIIE----DALLDFNGTIITVSHDR 504
Cdd:PRK11607 163 SLAKRPKLLLLDEPMGALDKKLRDRMQlevvDILERVGVTCVMVTHDQ 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
332-388 |
3.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 51.91 E-value: 3.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 332 VIEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK13644 1 MIRLENVSYSYPDgtPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV 59
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-192 |
3.20e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.11 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 18 LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKkdikigylnqIPDyeksesvyqciksvfkelDTI 97
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD----------VPD------------------NQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 SKQLETIETkmieereninslVARYGElqtyyeenggyeIDAKIRKVTH-GLNIAHLLKAKWGDLSGGERTKVGIAQMLI 176
Cdd:COG2401 97 GREASLIDA------------IGRKGD------------FKDAVELLNAvGLSDAVLWLRRFKELSTGQKFRFRLALLLA 152
|
170
....*....|....*.
gi 488409350 177 KPTDLLLLDEPTNHLD 192
Cdd:COG2401 153 ERPKLLVIDEFCSHLD 168
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
20-221 |
3.25e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.07 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLgLVGRNGEGKTTLLKLLS----GMERPST-GVISWKKDIKIGylnqipdyEKSESVYQCIKSVFKEL 94
Cdd:cd03240 14 ERSEIEFFSPLTL-IVGQNGAGKTTIIEALKyaltGELPPNSkGGAHDPKLIREG--------EVRAQVKLAFENANGKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 DTISKQLETIEtkmieereniNSLVARYGELQTYYEENGGYeidakirkvthglniahllkakwgdLSGGERTKVGI--- 171
Cdd:cd03240 85 YTITRSLAILE----------NVIFCHQGESNWPLLDMRGR-------------------------CSGGEKVLASLiir 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 172 ---AQMLIKPTDLLLLDEPTNHLDVKSIEW-LASYIKNNDSATV----IVSHDRYFLD 221
Cdd:cd03240 130 lalAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNfqliVITHDEELVD 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
329-503 |
3.87e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 51.72 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 329 SNRVIEMENVTKAYDDV---LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGL--------TSIDKGSIK-TASNL-- 394
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSkkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDGITlTAKTVwd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 ---KIGYLsqheFERDGNDTLLHTFRKKV-------NVSEDQARHILAhfmfygkDVFKKVN----------ELSGGEKI 454
Cdd:PRK13640 82 ireKVGIV----FQNPDNQFVGATVGDDVafglenrAVPRPEMIKIVR-------DVLADVGmldyidsepaNLSGGQKQ 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 455 RLRWAQLVNTDYNLLVLDEPTNHLDIDAKE----IIEDALLDFNGTIITVSHD 503
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEqilkLIRKLKKKNNLTVISITHD 203
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-193 |
3.94e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 51.38 E-value: 3.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 25 TLNSGDTLGLVGRNGEGKTTLLKLLSGMErPSTGVIswkkdikigYLNQIP--DYEKSE-SVYQCIksvfkeldtISKQL 101
Cdd:COG4138 18 QVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEI---------LLNGRPlsDWSAAElARHRAY---------LSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 102 ETIetkmieereninSLVARYGELQTYYEENGG-YEIDAKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQML--IKP 178
Cdd:COG4138 79 SPP------------FAMPVFQYLALHQPAGASsEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqVWP 146
|
170 180
....*....|....*....|
gi 488409350 179 TD-----LLLLDEPTNHLDV 193
Cdd:COG4138 147 TInpegqLLLLDEPMNSLDV 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-62 |
4.02e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 52.49 E-value: 4.02e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW 62
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-479 |
4.48e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 52.40 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKT----TLLKLLsgmerPSTGVISWKKDIKIgylnqipdyeKSESVYQC--------- 86
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSPPVVYPSGDIRF----------HGESLLHAseqtlrgvr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 87 ---IKSVFKE-------LDTISKQL-ETIETKMIEEREninslVARyGELQTYYEENGgyeidakIRKVTHGLN-IAHll 154
Cdd:PRK15134 91 gnkIAMIFQEpmvslnpLHTLEKQLyEVLSLHRGMRRE-----AAR-GEILNCLDRVG-------IRQAAKRLTdYPH-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 155 kakwgDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDV----KSIEWLASYIKNNDSATVIVSHD----RYFLDE-TVN 225
Cdd:PRK15134 156 -----QLSGGERQRVMIAMALLTRPELLIADEPTTALDVsvqaQILQLLRELQQELNMGLLFITHNlsivRKLADRvAVM 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 226 QiieidqkklhfyNGNYsyfVEERDKRLLIEFEAYKTQQkkikkmkesikQLRTWASQAKPPNAAmfrraksmEKAlnri 305
Cdd:PRK15134 231 Q------------NGRC---VEQNRAATLFSAPTHPYTQ-----------KLLNSEPSGDPVPLP--------EPA---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 306 qrleKPLLDSKKMHITLEEGMNVSNRVIEMENVTKayddvlfrNVNMLIRRGEHVAIIGDNGTGKTT----LLKIIlglt 381
Cdd:PRK15134 273 ----SPLLDVEQLQVAFPIRKGILKRTVDHNVVVK--------NISFTLRPGETLGLVGESGSGKSTtglaLLRLI---- 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 382 sidkgsiktASNLKIGYLSQ--HEFER---------------DGNDTL-------------LHTFRKKVNVSEDQARHIL 431
Cdd:PRK15134 337 ---------NSQGEIWFDGQplHNLNRrqllpvrhriqvvfqDPNSSLnprlnvlqiieegLRVHQPTLSAAQREQQVIA 407
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 488409350 432 AhFMFYGKDV---FKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLD 479
Cdd:PRK15134 408 V-MEEVGLDPetrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD 457
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
20-242 |
4.57e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 51.70 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwKKDIKIGYlnqipdyeksesvyqciKSVFKELDTISK 99
Cdd:PRK13646 24 HDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVT-VDDITITH-----------------KTKDKYIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 100 QLETI----ETKMIE---ERENInslvarygelqtYYEENGGYEIDaKIRKVTHGLNIA-----HLLKAKWGDLSGGERT 167
Cdd:PRK13646 86 RIGMVfqfpESQLFEdtvEREII------------FGPKNFKMNLD-EVKNYAHRLLMDlgfsrDVMSQSPFQMSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 168 KVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK----NNDSATVIVSHD-----RYfLDETV----NQIIEIDQKK 234
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslqtDENKTIILVSHDmnevaRY-ADEVIvmkeGSIVSQTSPK 231
|
....*...
gi 488409350 235 LHFYNGNY 242
Cdd:PRK13646 232 ELFKDKKK 239
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
357-503 |
4.75e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 4.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 357 GEHVAIIGDNGTGKTTLLK------------IILGLTSIDKGSIKtASNLKIGYLSQHEFERDGndtllHTFRKKVNV-- 422
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKmlgrhqppsegeILLDAQPLESWSSK-AFARKVAYLPQQLPAAEG-----MTVRELVAIgr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 423 -----------SEDQAR----------HILAHfmfygkdvfKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDI- 480
Cdd:PRK10575 111 ypwhgalgrfgAADREKveeaislvglKPLAH---------RLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIa 181
|
170 180
....*....|....*....|....*.
gi 488409350 481 ---DAKEIIEDALLDFNGTIITVSHD 503
Cdd:PRK10575 182 hqvDVLALVHRLSQERGLTVIAVLHD 207
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-215 |
5.20e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 51.28 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 18 LFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwKKDIKIgylnqipdyeKSESVYQCIKSVFKELdti 97
Cdd:PRK13649 23 LFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVR-VDDTLI----------TSTSKNKDIKQIRKKV--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 skqletietkmieereninSLVARYGELQTYYE----------ENGGY---EIDAKIRKVTHGLNIAHLLKAKWG-DLSG 163
Cdd:PRK13649 88 -------------------GLVFQFPESQLFEEtvlkdvafgpQNFGVsqeEAEALAREKLALVGISESLFEKNPfELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 164 GERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN---NDSATVIVSH 215
Cdd:PRK13649 149 GQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlhqSGMTIVLVTH 203
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-213 |
5.31e-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: 50.69 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKY-TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIKigylnqipDYeKSESVY 84
Cdd:cd03253 4 ENVTFAYdPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDgQDIR--------EV-TLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 85 QCIKSVFKEL----DTIskqletietkmieeRENInslvaRYGELQTYYEENggYE------IDAKIRKVTHGLNiahll 154
Cdd:cd03253 75 RAIGVVPQDTvlfnDTI--------------GYNI-----RYGRPDATDEEV--IEaakaaqIHDKIMRFPDGYD----- 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488409350 155 kAKWGD----LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS-IEWLASYIKNNDSATVIV 213
Cdd:cd03253 129 -TIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTeREIQAALRDVSKGRTTIV 191
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-216 |
5.43e-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: 51.59 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKY-TEDILF---DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERP---STGVISWK-KDikigyLNQI 74
Cdd:COG0444 1 LLEVRNLKVYFpTRRGVVkavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgED-----LLKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 75 PDYEKSESVYQCIKSVFKE----LD---TISKQL-ETIETKMIEERENINSLVArygELqtyyeenggyeidakIRKVth 146
Cdd:COG0444 76 SEKELRKIRGREIQMIFQDpmtsLNpvmTVGDQIaEPLRIHGGLSKAEARERAI---EL---------------LERV-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 147 GLNIAhllkAKWGD-----LSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDVkSI-----EWLASYIKNNDSATVIVSH 215
Cdd:COG0444 136 GLPDP----ERRLDrypheLSGGMRQRVMIARALAlEP-KLLIADEPTTALDV-TIqaqilNLLKDLQRELGLAILFITH 209
|
.
gi 488409350 216 D 216
Cdd:COG0444 210 D 210
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
348-507 |
6.05e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 6.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 348 RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGltsidkgsiKTASNLKIGYLSqheferdgndtllhTFRKKVNVSEDQA 427
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY---------ASGKARLISFLP--------------KFSRNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 428 RHILAHFMFYGKdVFKKVNELSGGEKIRLRWAQ--LVNTDYNLLVLDEPTNHLD-IDAKEIIE--DALLDFNGTIITVSH 502
Cdd:cd03238 69 QFLIDVGLGYLT-LGQKLSTLSGGELQRVKLASelFSEPPGTLFILDEPSTGLHqQDINQLLEviKGLIDLGNTVILIEH 147
|
....*
gi 488409350 503 DRYFL 507
Cdd:cd03238 148 NLDVL 152
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
22-193 |
6.18e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 51.41 E-value: 6.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW--------KKDI-------KIGYLNQ----IPDYekses 82
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLngrvlfdaEKGIclppekrRIGYVFQdarlFPHY----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 vyqcikSVFKELdtiskqletietkmieereninslvaRYGELQTyyeenggyeIDAKIRKVTHGLNIAHLLKAKWGDLS 162
Cdd:PRK11144 92 ------KVRGNL--------------------------RYGMAKS---------MVAQFDKIVALLGIEPLLDRYPGSLS 130
|
170 180 190
....*....|....*....|....*....|.
gi 488409350 163 GGERTKVGIAQMLIKPTDLLLLDEPTNHLDV 193
Cdd:PRK11144 131 GGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
327-522 |
6.37e-07 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 51.04 E-value: 6.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 327 NVSNRVIEMENVTKAYDD--VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK-----TASNLK---I 396
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNghTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISilgqpTRQALQknlV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 397 GYLSQHE---------------FERDGNDTLLH--TFRKKVNVSEDQARHILAHFMfygkdvFKKVNELSGGEKIRLRWA 459
Cdd:PRK15056 81 AYVPQSEevdwsfpvlvedvvmMGRYGHMGWLRraKKRDRQIVTAALARVDMVEFR------HRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 460 QLVNTDYNLLVLDEPTNHLDIDAKEIIED---ALLDFNGTIITVSHDRYFLNKLFNTTYLLKNKTL 522
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISllrELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
28-214 |
6.43e-07 |
|
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: 50.35 E-value: 6.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 28 SGDTLGLVGRNGEGKTTLLKLLSGMERPS---TGVI----------SWKKdiKIGYLNQIPDYEKSESVYQCIksvfkel 94
Cdd:cd03234 32 SGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQIlfngqprkpdQFQK--CVAYVRQDDILLPGLTVRETL------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 dTISKQLETIETKMIEERENInslVARYGELQtyyeenggyeidakirkvthgLNIAHLLKAKWGDLSGGERTKVGIAQM 174
Cdd:cd03234 103 -TYTAILRLPRKSSDAIRKKR---VEDVLLRD---------------------LALTRIGGNLVKGISGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 488409350 175 LIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNdsATVIVS 214
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTalnlVSTLSQLARRN--RIVILT 199
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
330-503 |
7.68e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 50.86 E-value: 7.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 330 NRVIEMENVTKAYD---DV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK------TASNL----- 394
Cdd:PRK13642 2 NKILEVENLVFKYEkesDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKidgellTAENVwnlrr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 KIGYLsqheFERDGNDTLLHTFRKKVNVS--------EDQARHILAHFMFYGKDVFK--KVNELSGGEKIRLRWAQLVNT 464
Cdd:PRK13642 82 KIGMV----FQNPDNQFVGATVEDDVAFGmenqgiprEEMIKRVDEALLAVNMLDFKtrEPARLSGGQKQRVAVAGIIAL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488409350 465 DYNLLVLDEPTNHLDIDAK----EIIEDALLDFNGTIITVSHD 503
Cdd:PRK13642 158 RPEIIILDESTSMLDPTGRqeimRVIHEIKEKYQLTVLSITHD 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-235 |
8.05e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 8.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKY------TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI------------SWK 63
Cdd:PRK13633 3 EMIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtsdeenLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 64 KDIKIGYLNQIPDyeksesvYQCIKSVFKELDTISKQLETIETKMIEERENiNSLvarygelqtyyEENGGYEidakIRK 143
Cdd:PRK13633 83 IRNKAGMVFQNPD-------NQIVATIVEEDVAFGPENLGIPPEEIRERVD-ESL-----------KKVGMYE----YRR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 144 vthglNIAHLlkakwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN---NDSATVI-VSHdryF 219
Cdd:PRK13633 140 -----HAPHL-------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnkKYGITIIlITH---Y 204
|
250
....*....|....*...
gi 488409350 220 LDETV--NQIIEIDQKKL 235
Cdd:PRK13633 205 MEEAVeaDRIIVMDSGKV 222
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-248 |
1.05e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 50.62 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTED-----ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIsWKKDIKIGylnqipdy 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTI-QVGDIYIG-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 78 EKSESVYQCIKSVFKELDTISKQLETIetkmieereninSLVARYGELQTY---YEEN--------GGYEIDAKIRKVTH 146
Cdd:PRK13631 92 DKKNNHELITNPYSKKIKNFKELRRRV------------SMVFQFPEYQLFkdtIEKDimfgpvalGVKKSEAKKLAKFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 147 ----GLNIAHLLKAKWGdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSHDRYF 219
Cdd:PRK13631 160 lnkmGLDDSYLERSPFG-LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLIldaKANNKTVFVITHTMEH 238
|
250 260
....*....|....*....|....*....
gi 488409350 220 LDETVNQIIEIDQKKLHFYNGNYSYFVEE 248
Cdd:PRK13631 239 VLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
348-491 |
1.10e-06 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 50.08 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 348 RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIkTASNLKI-------GYLSQHEferdgndTLLHTFRKKV 420
Cdd:PRK11248 18 EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSI-TLDGKPVegpgaerGVVFQNE-------GLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 421 NVS-------------EDQARHILAHFMFYGKDVfKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIE 487
Cdd:PRK11248 90 NVAfglqlagvekmqrLEIAHQMLKKVGLEGAEK-RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
....
gi 488409350 488 DALL 491
Cdd:PRK11248 169 TLLL 172
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
333-502 |
1.17e-06 |
|
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: 49.41 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAY----DDVLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTasnlkigylsqheferDG 408
Cdd:cd03244 3 IEFKNVSLRYrpnlPPVL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI----------------DG 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 409 NDTL---LHTFRKKVNV----------------------SEDQARHIL--AHF------MFYGKDvfKKVNE----LSGG 451
Cdd:cd03244 66 VDISkigLHDLRSRISIipqdpvlfsgtirsnldpfgeySDEELWQALerVGLkefvesLPGGLD--TVVEEggenLSVG 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 452 EKirlrwaQLVN------TDYNLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSH 502
Cdd:cd03244 144 QR------QLLClarallRKSKILVLDEATASVDPETDALIQKTIREAfkDCTVLTIAH 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
8-235 |
1.19e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 50.37 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDI-LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIsWKKDIKIGylnqipDYEKSESVYQC 86
Cdd:PRK13644 6 NVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKV-LVSGIDTG------DFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 87 IKSVFKELD------TISKQL----ETIETKMIEERENINSLVARYGelqtyyeenggyeidakIRKVTHglniaHLLKA 156
Cdd:PRK13644 79 VGIVFQNPEtqfvgrTVEEDLafgpENLCLPPIEIRKRVDRALAEIG-----------------LEKYRH-----RSPKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 157 kwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN---NDSATVIVSHDryfLDE--TVNQIIEID 231
Cdd:PRK13644 137 ----LSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKlheKGKTIVYITHN---LEElhDADRIIVMD 209
|
....
gi 488409350 232 QKKL 235
Cdd:PRK13644 210 RGKI 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
349-503 |
1.41e-06 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 49.60 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 349 NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNlKIGYLSQHEFERDGndtLLHTFR-----KKVNVS 423
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ-HIEGLPGHQIARMG---VVRTFQhvrlfREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 424 ED----QARHILAHFmFYGkdVFK--------------------KVN----------ELSGGEKIRLRWAQLVNTDYNLL 469
Cdd:PRK11300 99 ENllvaQHQQLKTGL-FSG--LLKtpafrraesealdraatwleRVGllehanrqagNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 488409350 470 VLDEPTNHLD----IDAKEIIEDALLDFNGTIITVSHD 503
Cdd:PRK11300 176 MLDEPAAGLNpketKELDELIAELRNEHNVTVLLIEHD 213
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
333-388 |
1.75e-06 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.74 E-value: 1.75e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 333 IEMENVTKAYDDVLFR--NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK10522 323 LELRNVTFAYQDNGFSvgPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-192 |
2.01e-06 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 50.08 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKY-----TEDILfDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkdikigylnqipdyekse 81
Cdd:COG1135 5 ENLSKTFptkggPVTAL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSG----------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqcikSVF---KELDTISkqletiETKMIEERENI-------NSLVARygelqTYYE------ENGGY---EIDAKIR 142
Cdd:COG1135 61 -------SVLvdgVDLTALS------ERELRAARRKIgmifqhfNLLSSR-----TVAEnvalplEIAGVpkaEIRKRVA 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 143 K----VthGLniAHLLKAKWGDLSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLD 192
Cdd:COG1135 123 EllelV--GL--SDKADAYPSQLSGGQKQRVGIARALAnNP-KVLLCDEATSALD 172
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
342-509 |
2.26e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 342 YDDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK-TASNLK---IGYLSQ-----HEFERDGNDTL 412
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILfERQSIKkdlCTYQKQlcfvgHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 413 -------LHTFRKKVNVSEDQARHILAHFMFYgkdvfkKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEI 485
Cdd:PRK13540 92 renclydIHFSPGAVGITELCRLFSLEHLIDY------PCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLT 165
|
170 180
....*....|....*....|....*..
gi 488409350 486 IEDALLDF---NGTIITVSHDRYFLNK 509
Cdd:PRK13540 166 IITKIQEHrakGGAVLLTSHQDLPLNK 192
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
3-230 |
2.27e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 50.49 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYT---EDI-LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkdikigylnqipdye 78
Cdd:PRK10535 4 LLELKDIRRSYPsgeEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSG-------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 79 ksesVYQCIKSVFKELDtiSKQLETIetkmieERENINSLVARYG-----------ELQTYYEENGGYEIDAKIRKVTHG 147
Cdd:PRK10535 64 ----TYRVAGQDVATLD--ADALAQL------RREHFGFIFQRYHllshltaaqnvEVPAVYAGLERKQRLLRAQELLQR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 148 LNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVI-VSHDryflDETV 224
Cdd:PRK10535 132 LGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHqlRDRGHTVIiVTHD----PQVA 207
|
....*....
gi 488409350 225 NQ---IIEI 230
Cdd:PRK10535 208 AQaerVIEI 216
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
336-503 |
2.44e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 49.15 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 336 ENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLKIGYLSQ--------- 401
Cdd:PRK11701 10 RGLTKLYGPRKgCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmRDGQLRDLYALSEaerrrllrt 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 402 -----HEFERDGndtllhtFRKKV----NVSED----QARHilahfmfYGK------DVFKKVnEL------------SG 450
Cdd:PRK11701 90 ewgfvHQHPRDG-------LRMQVsaggNIGERlmavGARH-------YGDiratagDWLERV-EIdaariddlpttfSG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 451 GEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDAL----LDFNGTIITVSHD 503
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrglvRELGLAVVIVTHD 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-215 |
2.50e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 49.25 E-value: 2.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 18 LFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdiKIGylnqipdyeksESVYQCIKSvfkeldti 97
Cdd:PRK13634 23 LYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTV------TIG-----------ERVITAGKK-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 SKQLETIETKMieereninSLVARYGELQTYYE----------ENGGY---EIDAKIRKVTH--GLNIAHLLKAKWgDLS 162
Cdd:PRK13634 77 NKKLKPLRKKV--------GIVFQFPEHQLFEEtvekdicfgpMNFGVseeDAKQKAREMIElvGLPEELLARSPF-ELS 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 163 GGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSH 215
Cdd:PRK13634 148 GGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGrkemMEMFYKLHKEKGLTTVLVTH 204
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
327-504 |
2.60e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.96 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 327 NVSNRViEMENVTKAYD-------DVLFRnvnmlIRRGEHVAIIGDNGTGKTTLLKII-------LGLTSIDKGSIKT-- 390
Cdd:PRK13657 330 RVKGAV-EFDDVSFSYDnsrqgveDVSFE-----AKPGQTVAIVGPTGAGKSTLINLLqrvfdpqSGRILIDGTDIRTvt 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 391 ----------------------ASNLKIGylsqhefERDGNDTLLHTFRKKVNVSEdqarHILAHFMFYGKDVFKKVNEL 448
Cdd:PRK13657 404 raslrrniavvfqdaglfnrsiEDNIRVG-------RPDATDEEMRAAAERAQAHD----FIERKPDGYDTVVGERGRQL 472
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 449 SGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDAlLDfngtiiTVSHDR 504
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA-LD------ELMKGR 521
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-216 |
2.79e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.89 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKY---TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswKKDIKIGYLNqipdyeksesvy 84
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKI--KVDGKVLYFG------------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 85 qciKSVFKeLDTISKQLETietKMIEERENINSLVARYGELQTYYEENGGYE-------IDAKIRKVTHGLNIAHLLKAK 157
Cdd:PRK14246 78 ---KDIFQ-IDAIKLRKEV---GMVFQQPNPFPHLSIYDNIAYPLKSHGIKEkreikkiVEECLRKVGLWKEVYDRLNSP 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 158 WGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDV---KSIEWLASYIKnNDSATVIVSHD 216
Cdd:PRK14246 151 ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIvnsQAIEKLITELK-NEIAIVIVSHN 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-260 |
3.10e-06 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 48.52 E-value: 3.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 16 DILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGME--RPSTGVISWK-KDIK-----------IGYLNQIPdyekSE 81
Cdd:COG0396 14 EILKG-VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDgEDILelspderaragIFLAFQYP----VE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 svyqcIKSVfkeldTISKQLETIETKMIEERENINSLVArygelqtyyeenggyEIDAKIRKVthGLNIAHLLKAKWGDL 161
Cdd:COG0396 89 -----IPGV-----SVSNFLRTALNARRGEELSAREFLK---------------LLKEKMKEL--GLDEDFLDRYVNEGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 162 SGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSHDRYFLDEtvnqiIEIDqkKLH-F 237
Cdd:COG0396 142 SGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVnklRSPDRGILIITHYQRILDY-----IKPD--FVHvL 214
|
250 260
....*....|....*....|....*
gi 488409350 238 YNGNysyFVEERDKRLL--IEFEAY 260
Cdd:COG0396 215 VDGR---IVKSGGKELAleLEEEGY 236
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-222 |
3.23e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 48.96 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTED---ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI-----------SWKKDI 66
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIiidgdllteenVWDIRH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 67 KIGYLNQIPDyeksesvyqciksvfkeldtiskqletietkmieereniNSLVARYGELQTYYE-ENGGYEIDAKIRKVT 145
Cdd:PRK13650 82 KIGMVFQNPD---------------------------------------NQFVGATVEDDVAFGlENKGIPHEEMKERVN 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 146 HGLNIAHLLKAKWGD---LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN---NDSATVI-VSHDry 218
Cdd:PRK13650 123 EALELVGMQDFKEREparLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGirdDYQMTVIsITHD-- 200
|
....
gi 488409350 219 fLDE 222
Cdd:PRK13650 201 -LDE 203
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
3.33e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 49.03 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDI-LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDikigylnQIPDyEK 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE-------PITK-EN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SESVYQCIKSVFKELDtiskqlETIETKMIEEReninslVArYGELQTYYEENggyEIDAKIRKVTHGLNIAHLLKAKWG 159
Cdd:PRK13652 73 IREVRKFVGLVFQNPD------DQIFSPTVEQD------IA-FGPINLGLDEE---TVAHRVSSALHMLGLEELRDRVPH 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 488409350 160 DLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK 204
Cdd:PRK13652 137 HLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLN 181
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
342-503 |
3.47e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 49.01 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 342 YDDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI---------KTASNL------KIGYLSQ----H 402
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVtvdditithKTKDKYirpvrkRIGMVFQfpesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 EFERDGNDTLL---HTFRKKVNVSEDQARHILAHFMFyGKDVFKKVN-ELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHL 478
Cdd:PRK13646 98 LFEDTVEREIIfgpKNFKMNLDEVKNYAHRLLMDLGF-SRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180
....*....|....*....|....*....
gi 488409350 479 DIDAK----EIIEDALLDFNGTIITVSHD 503
Cdd:PRK13646 177 DPQSKrqvmRLLKSLQTDENKTIILVSHD 205
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
287-520 |
3.68e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 3.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 287 PNAAMFRRAKSMEKALNRIQRlEKPLLDSKkmhitlEEGMNVSN-RVIEMENVTKAYD---DV-LFRNVNMLIRRGEHVA 361
Cdd:PTZ00265 343 PNITEYMKSLEATNSLYEIIN-RKPLVENN------DDGKKLKDiKKIQFKNVRFHYDtrkDVeIYKDLNFTLTEGKTYA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 362 IIGDNGTGKTTLLKIILGLTSIDKGSI--KTASNL----------KIGYLSQ---------------------------H 402
Cdd:PTZ00265 416 FVGESGCGKSTILKLIERLYDPTEGDIiiNDSHNLkdinlkwwrsKIGVVSQdpllfsnsiknnikyslyslkdlealsN 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 EFERDGNDT-----------------------------LLHTfRKKVNVSEDQ-----ARHILAHFMF------YGKDVF 442
Cdd:PTZ00265 496 YYNEDGNDSqenknkrnscrakcagdlndmsnttdsneLIEM-RKNYQTIKDSevvdvSKKVLIHDFVsalpdkYETLVG 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 443 KKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNGT----IITVSHdRYFLNKLFNTTYLLK 518
Cdd:PTZ00265 575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNenriTIIIAH-RLSTIRYANTIFVLS 653
|
..
gi 488409350 519 NK 520
Cdd:PTZ00265 654 NR 655
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
333-503 |
3.98e-06 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 49.72 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYD------DVLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTA----SNLKIGYLSQH 402
Cdd:PRK10535 5 LELKDIRRSYPsgeeqvEVL-KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAgqdvATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 EFERDG----NDTLLHTFRKKVNV--------SEDQARHILAHFMF----YGKDVFKKVNELSGGEKIRLRWAQLVNTDY 466
Cdd:PRK10535 84 RREHFGfifqRYHLLSHLTAAQNVevpavyagLERKQRLLRAQELLqrlgLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 488409350 467 NLLVLDEPTNHLDIDAKE---IIEDALLDFNGTIITVSHD 503
Cdd:PRK10535 164 QVILADEPTGALDSHSGEevmAILHQLRDRGHTVIIVTHD 203
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-216 |
4.03e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 48.39 E-value: 4.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 25 TLNSGDTLGLVGRNGEGKTTLLKLLSGMeRPSTGVIswkkdikigYLNQIP--DYEKSE-SVYQCIksvfkeldtISKQl 101
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSI---------QFAGQPleAWSAAElARHRAY---------LSQQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 102 etietkmieERENINSLVARYgeLQTYYEENGG-YEIDAKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQML--IKP 178
Cdd:PRK03695 78 ---------QTPPFAMPVFQY--LTLHQPDKTRtEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqVWP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 488409350 179 T-----DLLLLDEPTNHLDVKSIEWLASYIKNNDSA--TVIVS-HD 216
Cdd:PRK03695 147 DinpagQLLLLDEPMNSLDVAQQAALDRLLSELCQQgiAVVMSsHD 192
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
345-491 |
4.23e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.78 E-value: 4.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 345 VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASNlkIGYLSQHEF--------------ERDGND 410
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERS--IAYVPQQAWimnatvrgnilffdEEDAAR 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 411 tlLHtfrKKVNVSEDQArhilahfmfygkDVF------------KKVNeLSGGEKIRLRWAQLVNTDYNLLVLDEPTNHL 478
Cdd:PTZ00243 752 --LA---DAVRVSQLEA------------DLAqlgggleteigeKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170
....*....|....
gi 488409350 479 DIDAKE-IIEDALL 491
Cdd:PTZ00243 814 DAHVGErVVEECFL 827
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
333-502 |
5.04e-06 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 47.41 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDDVL---FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTasnlkigylsqheferDGN 409
Cdd:cd03369 7 IEVENLSVRYAPDLppvLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI----------------DGI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 410 DTL---LHTFRKKVN-VSEDQA------RHILAHF-MFYGKDVFK--KVNE----LSGGEKIRLRWAQLVNTDYNLLVLD 472
Cdd:cd03369 71 DIStipLEDLRSSLTiIPQDPTlfsgtiRSNLDPFdEYSDEEIYGalRVSEgglnLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|..
gi 488409350 473 EPTNHLDIDAKEIIEDALLD-FNG-TIITVSH 502
Cdd:cd03369 151 EATASIDYATDALIQKTIREeFTNsTILTIAH 182
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
333-388 |
6.00e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 47.65 E-value: 6.00e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 333 IEMENVTKAYDDVLFRnVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK10771 2 LKLTDITWLYHHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL 56
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
333-388 |
6.31e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 48.30 E-value: 6.31e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 333 IEMENVTKAYD---DVLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK11650 4 LKLQAVRKSYDgktQVI-KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEI 61
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
333-502 |
6.51e-06 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAY--DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTaSNLKIGYLSqHEFERDG-- 408
Cdd:PRK10790 341 IDIDNVSFAYrdDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL-DGRPLSSLS-HSVLRQGva 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 409 ---ND--TLLHTFRKKV----NVSEDQARHIL--------AHFMFYG--KDVFKKVNELSGGEKIRLRWAQ-LVNTDyNL 468
Cdd:PRK10790 419 mvqQDpvVLADTFLANVtlgrDISEEQVWQALetvqlaelARSLPDGlyTPLGEQGNNLSVGQKQLLALARvLVQTP-QI 497
|
170 180 190
....*....|....*....|....*....|....*.
gi 488409350 469 LVLDEPTNHLDIDAKEIIEDAL--LDFNGTIITVSH 502
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALaaVREHTTLVVIAH 533
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
17-195 |
7.99e-06 |
|
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: 48.66 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 17 ILFDhIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKIGylNQ-IPDYeKSESVYQCIKSV----- 90
Cdd:COG5265 373 ILKG-VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSG------RILID--GQdIRDV-TQASLRAAIGIVpqdtv 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 91 -FKelDTIskqletietkmieeRENInslvaRYGELQTYYEEnggyeIDAKIRKVT-HGLnIAHL------------LKa 156
Cdd:COG5265 443 lFN--DTI--------------AYNI-----AYGRPDASEEE-----VEAAARAAQiHDF-IESLpdgydtrvgergLK- 494
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 157 kwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS 195
Cdd:COG5265 495 ----LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRT 529
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-60 |
8.36e-06 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 48.18 E-value: 8.36e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 2 NILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI 60
Cdd:PRK11432 5 NFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQI 63
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
337-503 |
9.08e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 47.35 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 337 NVTKAY----DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIKTASnlKIGYLSQHEFERDGNdtl 412
Cdd:PRK14246 12 NISRLYlyinDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDG--KVLYFGKDIFQIDAI--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 413 lhTFRKKVNVSEDQArHILAHFMFYG-------------------------------KDVFKKVN----ELSGGEKIRLR 457
Cdd:PRK14246 87 --KLRKEVGMVFQQP-NPFPHLSIYDniayplkshgikekreikkiveeclrkvglwKEVYDRLNspasQLSGGQQQRLT 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 488409350 458 WAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG--TIITVSHD 503
Cdd:PRK14246 164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNeiAIVIVSHN 211
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
333-502 |
9.08e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 47.43 E-value: 9.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD-------VLFrNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK--------TASNLKIG 397
Cdd:PRK13649 3 INLQNVSYTYQAgtpfegrALF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRvddtlitsTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 398 YLSQH---EFERDGNDTLLHTFRKKV-------NVSEDQARHILA---HFMFYGKDVFKKVN-ELSGGEKIRLRWAQLVN 463
Cdd:PRK13649 82 QIRKKvglVFQFPESQLFEETVLKDVafgpqnfGVSQEEAEALAReklALVGISESLFEKNPfELSGGQMRRVAIAGILA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 488409350 464 TDYNLLVLDEPTNHLDIDA-KEIIE--DALLDFNGTIITVSH 502
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGrKELMTlfKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-216 |
1.01e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 47.38 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDIL-FDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIKigylnqipdYEKS 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgEPIK---------YDKK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 E--SVYQCIKSVFKELDtiskqlETIETKMIEEReninslVArYGELQTYYEENggyEIDAKIRKVTHGLNIAHLLKAKW 158
Cdd:PRK13639 72 SllEVRKTVGIVFQNPD------DQLFAPTVEED------VA-FGPLNLGLSKE---EVEKRVKEALKAVGMEGFENKPP 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 159 GDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD---VKSIEWLAsYIKNNDSATVIVS-HD 216
Cdd:PRK13639 136 HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDpmgASQIMKLL-YDLNKEGITIIIStHD 196
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
20-193 |
1.07e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 48.03 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswKKD-IKIGYLNQipdyeksESVYQCIKSVFKELDTIS 98
Cdd:PRK13657 352 EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI--LIDgTDIRTVTR-------ASLRRNIAVVFQDAGLFN 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 99 KqleTIetkmieeRENInslvaRYG-ELQTYYEENGGYEIDAK---IRKVTHGLNIahLLKAKWGDLSGGERTKVGIAQM 174
Cdd:PRK13657 423 R---SI-------EDNI-----RVGrPDATDEEMRAAAERAQAhdfIERKPDGYDT--VVGERGRQLSGGERQRLAIARA 485
|
170
....*....|....*....
gi 488409350 175 LIKPTDLLLLDEPTNHLDV 193
Cdd:PRK13657 486 LLKDPPILILDEATSALDV 504
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
305-529 |
1.28e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 305 IQRLEKPLLDSKKM---HITLEEGMNVsnrvIEMENVTKAYDDVL----FRNVNMLIRRGEHVAIIGDNGTGKTTLLKII 377
Cdd:PLN03232 588 LQRIEELLLSEERIlaqNPPLQPGAPA----ISIKNGYFSWDSKTskptLSDINLEIPVGSLVAIVGGTGEGKTSLISAM 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 378 LG------LTSID-KGSIKTASNL----------KIGYLSQHEFERdgndtllhtFRKKVNVSEDQarHILAhfMFYGKD 440
Cdd:PLN03232 664 LGelshaeTSSVViRGSVAYVPQVswifnatvreNILFGSDFESER---------YWRAIDVTALQ--HDLD--LLPGRD 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 441 VF----KKVNeLSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALL--DFNG-TIITVSHDRYFLNKLfnT 513
Cdd:PLN03232 731 LTeigeRGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMkdELKGkTRVLVTNQLHFLPLM--D 807
|
250
....*....|....*.
gi 488409350 514 TYLLKNKTLEKFEGNY 529
Cdd:PLN03232 808 RIILVSEGMIKEEGTF 823
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-193 |
1.36e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.71 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdikigylnqIPDYEKSESVY----QCIKSVFKELDTi 97
Cdd:PRK15112 32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELL------------IDDHPLHFGDYsyrsQRIRMIFQDPST- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 skqletietkMIEERENINSLVARYGELQTYYE-ENGGYEIDAKIRKV----THGLNIAHLlkakwgdLSGGERTKVGIA 172
Cdd:PRK15112 99 ----------SLNPRQRISQILDFPLRLNTDLEpEQREKQIIETLRQVgllpDHASYYPHM-------LAPGQKQRLGLA 161
|
170 180
....*....|....*....|.
gi 488409350 173 QMLIKPTDLLLLDEPTNHLDV 193
Cdd:PRK15112 162 RALILRPKVIIADEALASLDM 182
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
155-228 |
1.53e-05 |
|
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: 45.64 E-value: 1.53e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488409350 155 KAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK----NNDSATVIVSHDRYFLDETVNQII 228
Cdd:cd03222 66 KPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRrlseEGKKTALVVEHDLAVLDYLSDRIH 143
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
332-503 |
1.59e-05 |
|
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: 46.97 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDD-------VlfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGL---TSIDKGSIKtasnLK---IGY 398
Cdd:COG0444 1 LLEVRNLKVYFPTrrgvvkaV--DGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEIL----FDgedLLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 399 LSQHEFERdgndtllhtFRKKvNVS----------------EDQ-ARHILAHFMFYGKDVFKKV---------------- 445
Cdd:COG0444 75 LSEKELRK---------IRGR-EIQmifqdpmtslnpvmtvGDQiAEPLRIHGGLSKAEARERAiellervglpdperrl 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 446 ----NELSGGEKIRL---RwAQLVNTDynLLVLDEPTNHLD--IDAkEIIEdaLL-----DFNGTIITVSHD 503
Cdd:COG0444 145 drypHELSGGMRQRVmiaR-ALALEPK--LLIADEPTTALDvtIQA-QILN--LLkdlqrELGLAILFITHD 210
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
333-503 |
1.70e-05 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 46.99 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD------VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIkTASNLKIGYLSQHEfer 406
Cdd:COG1135 2 IELENLSKTFPTkggpvtAL-DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSV-LVDGVDLTALSERE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 407 dgndtlLHTFRKKVNVsedqarhILAHF-MFYGKDVF------------------KKVNE-----------------LSG 450
Cdd:COG1135 77 ------LRAARRKIGM-------IFQHFnLLSSRTVAenvalpleiagvpkaeirKRVAEllelvglsdkadaypsqLSG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 451 GEKIRLRWAQ-LVNtDYNLLVLDEPTNHLDIDA-KEIIEdaLLD-----FNGTIITVSHD 503
Cdd:COG1135 144 GQKQRVGIARaLAN-NPKVLLCDEATSALDPETtRSILD--LLKdinreLGLTIVLITHE 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
158-231 |
1.80e-05 |
|
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: 45.22 E-value: 1.80e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 158 WGD-LSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDVKSIEWLASYIKnNDSATVI-VSHdRYFLDETVNQIIEID 231
Cdd:cd03223 88 WDDvLSGGEQQRLAFARLLLhKP-KFVFLDEATSALDEESEDRLYQLLK-ELGITVIsVGH-RPSLWKFHDRVLDLD 161
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-192 |
1.81e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 11 KKYTEDILfDHIKITLNSGDTLGLVGRNGEGKTTLLKLLS----GMERPSTGVISWKkdikiGY-LNQIPDYEKSESVYQ 85
Cdd:TIGR00956 70 DTKTFDIL-KPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYD-----GItPEEIKKHYRGDVVYN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 ciksvfKELDTISKQLETIETKmieereninSLVARYGELQTYYEENGGYEIDAKIRKV---THGLNiaHLLKAKWGD-- 160
Cdd:TIGR00956 144 ------AETDVHFPHLTVGETL---------DFAARCKTPQNRPDGVSREEYAKHIADVymaTYGLS--HTRNTKVGNdf 206
|
170 180 190
....*....|....*....|....*....|....*
gi 488409350 161 ---LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:TIGR00956 207 vrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
332-379 |
1.91e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 1.91e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488409350 332 VIEMENVTKAYDDVL-FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILG 379
Cdd:NF040905 1 ILEMRGITKTFPGVKaLDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-215 |
2.04e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.32 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISkkYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKL--------------LSGMERPSTGVIsWkkDIK- 67
Cdd:PRK10938 262 VLNNGVVS--YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndltLFGRRRGSGETI-W--DIKk 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 68 -IGYL-NQIP-DYEKSESVYQCIKSVFkeLDTIskqletietkmieereninslvarygelqtyyeenGGYEI--DAKIR 142
Cdd:PRK10938 337 hIGYVsSSLHlDYRVSTSVRNVILSGF--FDSI-----------------------------------GIYQAvsDRQQK 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 143 KVTHGLNIAHL----LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD------VKSieWLASYIKNNDSATVI 212
Cdd:PRK10938 380 LAQQWLDILGIdkrtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDplnrqlVRR--FVDVLISEGETQLLF 457
|
...
gi 488409350 213 VSH 215
Cdd:PRK10938 458 VSH 460
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-227 |
2.15e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 46.72 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK---KDIKigyLNQIPDYEKSESVYQCIKSVFKELDT 96
Cdd:PRK15093 24 DRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRmrfDDID---LLRLSPRERRKLVGHNVSMIFQEPQS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 97 ISKQLETIETKMIEereNINSLvarygelqTYyeeNGGYEIDAKIRK-----VTHGLNI-AH--LLKAKWGDLSGGERTK 168
Cdd:PRK15093 101 CLDPSERVGRQLMQ---NIPGW--------TY---KGRWWQRFGWRKrraieLLHRVGIkDHkdAMRSFPYELTEGECQK 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409350 169 VGIAQMLIKPTDLLLLDEPTNHLDVKS----IEWLASYIKNNDSATVIVSHDRYFLDETVNQI 227
Cdd:PRK15093 167 VMIAIALANQPRLLIADEPTNAMEPTTqaqiFRLLTRLNQNNNTTILLISHDLQMLSQWADKI 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-193 |
2.49e-05 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 46.99 E-value: 2.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTL----LKLLsgmerPSTGVISWKKdikigylnqipdyeksesvyqciksvfKELD 95
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDG---------------------------QDLD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 96 TISKQletietKMIEERENI--------NSL-----VAR-YGE-LQTYYEENGGYEIDAKIRKVTH--GLNIAHLlkakw 158
Cdd:COG4172 351 GLSRR------ALRPLRRRMqvvfqdpfGSLsprmtVGQiIAEgLRVHGPGLSAAERRARVAEALEevGLDPAAR----- 419
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 488409350 159 gD-----LSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDV 193
Cdd:COG4172 420 -HrypheFSGGQRQRIAIARALIlEP-KLLVLDEPTSALDV 458
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
343-388 |
2.89e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 45.91 E-value: 2.89e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 488409350 343 DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-193 |
3.55e-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: 46.83 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswKKDIKIGYLNQ----IPDYEKSESVYQCIKSVFKELDTI 97
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--KHSGRISFSPQtswiMPGTIKDNIIFGLSYDEYRYTSVI 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 SK-QLETIETKMIEERENInslvarYGElqtyyeenGGyeidakirkVThglniahllkakwgdLSGGERTKVGIAQMLI 176
Cdd:TIGR01271 523 KAcQLEEDIALFPEKDKTV------LGE--------GG---------IT---------------LSGGQRARISLARAVY 564
|
170
....*....|....*..
gi 488409350 177 KPTDLLLLDEPTNHLDV 193
Cdd:TIGR01271 565 KDADLYLLDSPFTHLDV 581
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
332-401 |
3.60e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 3.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTK------AYDDVLFRnvnmlIRRGEHVAIIGDNGTGKTTLLKIILGL---TS---------IDKGSIKTasN 393
Cdd:NF033858 266 AIEARGLTMrfgdftAVDHVSFR-----IRRGEIFGFLGSNGCGKSTTMKMLTGLlpaSEgeawlfgqpVDAGDIAT--R 338
|
....*...
gi 488409350 394 LKIGYLSQ 401
Cdd:NF033858 339 RRVGYMSQ 346
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-194 |
3.74e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.99 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDH-IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkDIKIG--YLNQIpdy 77
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKTQVIKgIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSG------EIWIGgrVVNEL--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 78 EKSEsvyQCIKSVFkeldtiskqletietkmieereninslvarygelQTY--Y-----EENGGY----------EIDAK 140
Cdd:PRK11650 72 EPAD---RDIAMVF----------------------------------QNYalYphmsvRENMAYglkirgmpkaEIEER 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 488409350 141 IRKVTHGLNIAHLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVK 194
Cdd:PRK11650 115 VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
330-473 |
3.84e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.42 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 330 NRVIEMENVTKAYD----------DVLFR-----------NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK13545 2 NYKVKFEHVTKKYKmynkpfdklkDLFFRskdgeyhyalnNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 389 K---TASNLKIGYLSQHEFERDGNDTL--LHTFRKKVNVSEDQARHIlaHFMFYGKDVFKKVNELSGGEKIRLRWAQLVN 463
Cdd:PRK13545 82 DikgSAALIAISSGLNGQLTGIENIELkgLMMGLTKEKIKEIIPEII--EFADIGKFIYQPVKTYSSGMKSRLGFAISVH 159
|
170
....*....|
gi 488409350 464 TDYNLLVLDE 473
Cdd:PRK13545 160 INPDILVIDE 169
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
349-503 |
4.05e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 45.77 E-value: 4.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 349 NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGS--------------IKTASNLK--IGYLSQHEFERDGNDTL 412
Cdd:PRK13645 29 NTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanlkkIKEVKRLRkeIGLVFQFPEYQLFQETI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 413 LHTFR-KKVNVSEDQARHI-----LAHFMFYGKDVFKKVN-ELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEI 485
Cdd:PRK13645 109 EKDIAfGPVNLGENKQEAYkkvpeLLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180
....*....|....*....|..
gi 488409350 486 IEDALLDFNGT----IITVSHD 503
Cdd:PRK13645 189 FINLFERLNKEykkrIIMVTHN 210
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
8-217 |
4.77e-05 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 45.23 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTED--ILFDHIKITLNSGDTLGLVGRNGEGKTTL----LKLLSGMERPSTGVISWkkdikigylNQIPDYEKSE 81
Cdd:cd03289 7 DLTAKYTEGgnAVLENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLNTEGDIQIDGVSW---------NSVPLQKWRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVYQCIKSVFKELDTISKQLETI------ETKMIEERENINSLVARYGELQTYYEENGGYEidakirkvthglniahllk 155
Cdd:cd03289 78 AFGVIPQKVFIFSGTFRKNLDPYgkwsdeEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCV------------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409350 156 akwgdLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDS-ATVIVSHDR 217
Cdd:cd03289 139 -----LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAdCTVILSEHR 196
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-216 |
4.78e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 44.98 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDikigYLNQIPDYEKSES----VYQCIKsVFKELD 95
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQ----HIEGLPGHQIARMgvvrTFQHVR-LFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 96 TIskqletietkmieerENInsLVARYGELQTYYeENGGYEIDAKIRKVTHGLNIAhllkAKW--------------GDL 161
Cdd:PRK11300 97 VI---------------ENL--LVAQHQQLKTGL-FSGLLKTPAFRRAESEALDRA----ATWlervgllehanrqaGNL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 162 SGGERTKVGIAQ-MLIKPtDLLLLDEPTNHLDVKSIEWLASYI----KNNDSATVIVSHD 216
Cdd:PRK11300 155 AYGQQRRLEIARcMVTQP-EILMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLIEHD 213
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
22-221 |
5.00e-05 |
|
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: 44.94 E-value: 5.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGmeRPSTGVISWKKDIKIGYLNQIPDYEKSE----------------SVYQ 85
Cdd:TIGR01978 19 VNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSYEVTSGTILFKGQDLLELEPDERARaglflafqypeeipgvSNLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 CIKSVfkeLDTISKQLETIETKMIEERENINSLVARYGELQTYYEenggyeidakiRKVTHGLniahllkakwgdlSGGE 165
Cdd:TIGR01978 97 FLRSA---LNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLN-----------RSVNEGF-------------SGGE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 166 RTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSHDRYFLD 221
Cdd:TIGR01978 150 KKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGInrlREPDRSFLIITHYQRLLN 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-235 |
5.41e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 45.18 E-value: 5.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKY--TEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTgviswKKDIKIGYLNQIPDYEK 79
Cdd:PRK13640 4 NIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-----NPNSKITVDGITLTAKT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 80 SESVYQCIKSVFKELDtiskqletietkmieereniNSLV-ARYGELQTYYEENGGY---EIDAKIRKVTHGLNIAHLLK 155
Cdd:PRK13640 79 VWDIREKVGIVFQNPD--------------------NQFVgATVGDDVAFGLENRAVprpEMIKIVRDVLADVGMLDYID 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 156 AKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVI-VSHDryfLDETV--NQIIE 229
Cdd:PRK13640 139 SEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIrklKKKNNLTVIsITHD---IDEANmaDQVLV 215
|
....*.
gi 488409350 230 IDQKKL 235
Cdd:PRK13640 216 LDDGKL 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
355-503 |
5.58e-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: 45.93 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 355 RRGEHVAIIGDNGTGKTTLLKIILG------------------------------LTSIDKGSIKTAsnLKIGYLSQHEF 404
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrfrgtelqdyFKKLANGEIKVA--HKPQYVDLIPK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 405 ERDGN-DTLLhtfrKKVNvSEDQARHI-----LAHFMfygkDvfKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHL 478
Cdd:COG1245 175 VFKGTvRELL----EKVD-ERGKLDELaeklgLENIL----D--RDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243
|
170 180
....*....|....*....|....*....
gi 488409350 479 DID----AKEIIEDaLLDFNGTIITVSHD 503
Cdd:COG1245 244 DIYqrlnVARLIRE-LAEEGKYVLVVEHD 271
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
20-195 |
6.65e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 45.78 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK----KDIKIGYL-NQIPDYekSESVYqciksVFKel 94
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghdlRDYTLASLrNQVALV--SQNVH-----LFN-- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 DTISKQLeTIETKMIEERENINSlVARYGelqtyyeenggYEIDAkIRKVTHGLNIahLLKAKWGDLSGGERTKVGIAQM 174
Cdd:PRK11176 431 DTIANNI-AYARTEQYSREQIEE-AARMA-----------YAMDF-INKMDNGLDT--VIGENGVLLSGGQRQRIAIARA 494
|
170 180
....*....|....*....|.
gi 488409350 175 LIKPTDLLLLDEPTNHLDVKS 195
Cdd:PRK11176 495 LLRDSPILILDEATSALDTES 515
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
329-502 |
6.80e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 44.69 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 329 SNRVIEMENVTKAYDD-------VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI-------KTASNL 394
Cdd:PRK13633 1 MNEMIKCKNVSYKYESneestekLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdgldtSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 -----KIGYLSQHE--------FERD---GNDTL----------LHTFRKKVNVSE--DQARHIlahfmfygkdvfkkvn 446
Cdd:PRK13633 81 wdirnKAGMVFQNPdnqivatiVEEDvafGPENLgippeeirerVDESLKKVGMYEyrRHAPHL---------------- 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 447 eLSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNG----TIITVSH 502
Cdd:PRK13633 145 -LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkygiTIILITH 203
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
354-507 |
7.70e-05 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 45.71 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 354 IRRGEHVAIIGDNGTGKTTLLKIILGltSIDKGSIKTASNLKIGYLSQHEFERdgNDTLL------HTFRKKVNVSEDQA 427
Cdd:TIGR00957 661 IPEGALVAVVGQVGCGKSSLLSALLA--EMDKVEGHVHMKGSVAYVPQQAWIQ--NDSLRenilfgKALNEKYYQQVLEA 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 428 RHILAHF-MFYGKD---VFKKVNELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDID-AKEIIEDAL----LDFNGTII 498
Cdd:TIGR00957 737 CALLPDLeILPSGDrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpegVLKNKTRI 816
|
....*....
gi 488409350 499 TVSHDRYFL 507
Cdd:TIGR00957 817 LVTHGISYL 825
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
8-285 |
7.98e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTEDILF-----DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGV--------------ISWKKDIK- 67
Cdd:PRK13645 11 NVSYTYAKKTPFefkalNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgdyaipanlkkIKEVKRLRk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 68 -IGYLNQIPDYEksesVYQciksvfkelDTISKQLETIETKMIEERENINSLVARYGELQTYYEEnggyeidakirkvth 146
Cdd:PRK13645 91 eIGLVFQFPEYQ----LFQ---------ETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPED--------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 147 glniahLLKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI----KNNDSATVIVSHDRYFLDE 222
Cdd:PRK13645 143 ------YVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYKKRIIMVTHNMDQVLR 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 223 TVNQIIEIDQKKLHFYNGNYSYFveeRDKRLLIEFE---------AYKTQQKKIKKMKESIKQLRTWASQAK 285
Cdd:PRK13645 217 IADEVIVMHEGKVISIGSPFEIF---SNQELLTKIEidppklyqlMYKLKNKGIDLLNKNIRTIEEFAKELA 285
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-197 |
1.01e-04 |
|
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: 43.19 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTedilFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWK-KDIKIGylnqipdyekse 81
Cdd:cd03215 4 VLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDgKPVTRR------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 82 SVYQCIKsvfKELDTISkqletietkmiEEReninslvARYGELQTY-YEENggyeidakirkvthgLNIAHLLkakwgd 160
Cdd:cd03215 68 SPRDAIR---AGIAYVP-----------EDR-------KREGLVLDLsVAEN---------------IALSSLL------ 105
|
170 180 190
....*....|....*....|....*....|....*..
gi 488409350 161 lSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIE 197
Cdd:cd03215 106 -SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
332-503 |
1.18e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 44.07 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 332 VIEMENVTKAYDDVL--FRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI----KTASNLKIGYLSQHE-- 403
Cdd:PRK13636 5 ILKVEELNYNYSDGThaLKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgKPIDYSRKGLMKLREsv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 404 ---FERDGNDTLLHTFRKKVN-------VSEDQARHILAHFM-----FYGKDvfKKVNELSGGEKIRLRWAQLVNTDYNL 468
Cdd:PRK13636 85 gmvFQDPDNQLFSASVYQDVSfgavnlkLPEDEVRKRVDNALkrtgiEHLKD--KPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 469 LVLDEPTNHLD-IDAKEIIE---DALLDFNGTIITVSHD 503
Cdd:PRK13636 163 LVLDEPTAGLDpMGVSEIMKllvEMQKELGLTIIIATHD 201
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-239 |
1.39e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 43.61 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMerpstgviswkkdikiGYLNqiPDYEKSES 82
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRM----------------NDLN--PEVTITGS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 VyqciksVFKELDTISKQLETIETK----MIEERENINSLvarygelqTYYEE-------NGGYE---IDAKIRKVTHGL 148
Cdd:PRK14239 67 I------VYNGHNIYSPRTDTVDLRkeigMVFQQPNPFPM--------SIYENvvyglrlKGIKDkqvLDEAVEKSLKGA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 149 NIAHLLKAKWGD----LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS---IEWLASYIKnNDSATVIVSH------ 215
Cdd:PRK14239 133 SIWDEVKDRLHDsalgLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISagkIEETLLGLK-DDYTMLLVTRsmqqas 211
|
250 260
....*....|....*....|....*....
gi 488409350 216 ---DR--YFLDetvNQIIEIDQKKLHFYN 239
Cdd:PRK14239 212 risDRtgFFLD---GDLIEYNDTKQMFMN 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
335-388 |
1.41e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 44.34 E-value: 1.41e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 335 MENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK10982 1 MSNISKSFPGVkALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSI 55
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
161-216 |
1.78e-04 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 42.85 E-value: 1.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 161 LSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDV---KSI-EWLASYIKNNDSATVIVSHD 216
Cdd:COG4136 134 LSGGQRARVALLRALLaEP-RALLLDEPFSKLDAalrAQFrEFVFEQIRQRGIPALLVTHD 193
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
445-507 |
1.85e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 1.85e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 445 VNELSGGEK------IRLRWAQLVNTDYNLLVLDEPTNHLDIDA----KEIIEDALLDFNG--TIITVSHDRYFL 507
Cdd:PRK01156 799 IDSLSGGEKtavafaLRVAVAQFLNNDKSLLIMDEPTAFLDEDRrtnlKDIIEYSLKDSSDipQVIMISHHRELL 873
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-215 |
1.89e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.95 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 7 SNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGviswkkdiKIGYLNQIPDYEKS-ESVYQ 85
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSG--------SILFQGKEIDFKSSkEALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 86 CIKSVFKELDTIsKQLETIEtkmieereniNSLVARYGELQTYYEENGGYEiDAKirKVTHGLNIAHLLKAKWGDLSGGE 165
Cdd:PRK10982 74 GISMVHQELNLV-LQRSVMD----------NMWLGRYPTKGMFVDQDKMYR-DTK--AIFDELDIDIDPRAKVATLSVSQ 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 166 RTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSH 215
Cdd:PRK10982 140 MQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIrklKERGCGIVYISH 192
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
330-388 |
1.93e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 42.94 E-value: 1.93e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 330 NRVIEMENVTKAYDDV-LFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRI 62
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-248 |
1.96e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 43.55 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 4 LNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMErpstgviswkkdikigylNQIPDYEKSESV 83
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMN------------------DKVSGYRYSGDV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 YQCIKSVFKELDtiskqletietkMIEERENINSLVARYGELQTYYEEN--GGYEIDAKI-RKVTHGLNIAHLLKAKWGD 160
Cdd:PRK14271 84 LLGGRSIFNYRD------------VLEFRRRVGMLFQRPNPFPMSIMDNvlAGVRAHKLVpRKEFRGVAQARLTEVGLWD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 161 ------------LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN-NDSATVIVshdryfLDETVNQI 227
Cdd:PRK14271 152 avkdrlsdspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSlADRLTVII------VTHNLAQA 225
|
250 260
....*....|....*....|.
gi 488409350 228 IEIDQKKLHFYNGNysyFVEE 248
Cdd:PRK14271 226 ARISDRAALFFDGR---LVEE 243
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
348-388 |
2.06e-04 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 43.14 E-value: 2.06e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 488409350 348 RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK10419 29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNV 69
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
161-205 |
2.35e-04 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 42.25 E-value: 2.35e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKN 205
Cdd:cd03233 119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRT 163
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
326-377 |
2.50e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 42.72 E-value: 2.50e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 488409350 326 MNVSNRVIEMENVTKAYDD--VLfRNVNMLIRRGEHVAIIGDNGTGKTTLLKII 377
Cdd:COG1117 5 ASTLEPKIEVRNLNVYYGDkqAL-KDINLDIPENKVTALIGPSGCGKSTLLRCL 57
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
154-215 |
2.70e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.91 E-value: 2.70e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 154 LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD---VKSIEWLASYIKnNDSATVIVSH 215
Cdd:PRK14267 143 LNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDpvgTAKIEELLFELK-KEYTIVLVTH 206
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-230 |
2.88e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 42.80 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 2 NILNASNISKKYTEDI-LFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdikigylnQIPDYEKS 80
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV------------KVMGREVN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 81 ESVYQCIKS----VFKELDtiskqlETIETKMIEEReninslVArYGELQTyyeENGGYEIDAKIRKVTHGLNIAHLLKA 156
Cdd:PRK13647 71 AENEKWVRSkvglVFQDPD------DQVFSSTVWDD------VA-FGPVNM---GLDKDEVERRVEEALKAVRMWDFRDK 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 157 KWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIVS-HDRYFLDETVNQIIEI 230
Cdd:PRK13647 135 PPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDrlHNQGKTVIVAtHDVDLAAEWADQVIVL 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-58 |
2.95e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.25 E-value: 2.95e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 7 SNISKKYTED----ILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTG 58
Cdd:PRK11153 5 KNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSG 60
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
161-195 |
3.26e-04 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 43.33 E-value: 3.26e-04
10 20 30
....*....|....*....|....*....|....*.
gi 488409350 161 LSGGERTKVGIA-QMLIKPTdLLLLDEPTNHLDVKS 195
Cdd:PLN03211 207 ISGGERKRVSIAhEMLINPS-LLILDEPTSGLDATA 241
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-229 |
3.90e-04 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 42.29 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdikigYLNQIPDYEKSES 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTI---------TVDGEDLTDSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 83 VYQCIKSV---------FKELdTIskqLETIetkMI----------EERENInslvARygELqtyyeenggyeidakIRK 143
Cdd:COG1126 72 INKLRRKVgmvfqqfnlFPHL-TV---LENV---TLapikvkkmskAEAEER----AM--EL---------------LER 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 144 VthGLniAHLLKAKWGDLSGGERTKVGIAQML-IKPtDLLLLDEPTNHLD-------VKSIEWLAsyiknNDSAT-VIVS 214
Cdd:COG1126 124 V--GL--ADKADAYPAQLSGGQQQRVAIARALaMEP-KVMLFDEPTSALDpelvgevLDVMRDLA-----KEGMTmVVVT 193
|
250 260
....*....|....*....|....*
gi 488409350 215 H---------DR-YFLDEtvNQIIE 229
Cdd:COG1126 194 HemgfarevaDRvVFMDG--GRIVE 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
340-389 |
4.70e-04 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 42.98 E-value: 4.70e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 488409350 340 KAYDDVLFRnvnmlIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSIK 389
Cdd:PRK11288 18 KALDDISFD-----CRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL 62
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-193 |
5.86e-04 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.77 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswKKDIKIGYLNQ----IPDYEKSESVYQCIKSVFKELDTI 97
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--KHSGRISFSSQfswiMPGTIKENIIFGVSYDEYRYKSVV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 98 SK-QLETIETKMIEERENInslvarYGElqtyyeenGGYeidakirkvthglniahllkakwgDLSGGERTKVGIAQMLI 176
Cdd:cd03291 134 KAcQLEEDITKFPEKDNTV------LGE--------GGI------------------------TLSGGQRARISLARAVY 175
|
170
....*....|....*..
gi 488409350 177 KPTDLLLLDEPTNHLDV 193
Cdd:cd03291 176 KDADLYLLDSPFGYLDV 192
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
332-388 |
6.80e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 42.10 E-value: 6.80e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 332 VIEMENVTKAYDD-----VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK11153 1 MIELKNISKVFPQggrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRV 62
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
343-508 |
7.80e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 343 DDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLT--SIDKGSI--KTASNLKIG---------YLS-QHEFERDG 408
Cdd:PRK09580 13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVefKGKDLLELSpedragegiFMAfQYPVEIPG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 409 --NDTLLHTFRKKVNVSEDQA---RHILAHFMFYGKDVFK--------KVNE-LSGGEKIRLRWAQLVNTDYNLLVLDEP 474
Cdd:PRK09580 93 vsNQFFLQTALNAVRSYRGQEpldRFDFQDLMEEKIALLKmpedlltrSVNVgFSGGEKKRNDILQMAVLEPELCILDES 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 488409350 475 TNHLDIDAKEIIE---DALLDFNGTIITVSHDRYFLN 508
Cdd:PRK09580 173 DSGLDIDALKIVAdgvNSLRDGKRSFIIVTHYQRILD 209
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-228 |
7.90e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 7.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 19 FDHIKITLNSGDTLgLVGRNGEGKTTLLKLLSG-MERPSTGVISwKKDIKIGYLNQIPDYEKSESVYQCIKSVFKEL--- 94
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLlLGPSSSRKFD-EEDFYLGDDPDLPEIEIELTFGSLLSRLLRLLlke 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 95 ---DTISKQLETIETKMIEERENINSLVARYGELqtyYEENGGYEIDAKIRKVTHGLNIAHLLkakwgdLSGGERTKV-- 169
Cdd:COG3593 92 edkEELEEALEELNEELKEALKALNELLSEYLKE---LLDGLDLELELSLDELEDLLKSLSLR------IEDGKELPLdr 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488409350 170 ---GIAQMLI-------------KPTDLLLLDEPTNHLDVKSIEWLASYIKN--NDSATVIVS-HDRYFLDET-VNQII 228
Cdd:COG3593 163 lgsGFQRLILlallsalaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKElsEKPNQVIITtHSPHLLSEVpLENIR 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
22-60 |
8.36e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.88 E-value: 8.36e-04
10 20 30
....*....|....*....|....*....|....*....
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI 60
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-60 |
8.75e-04 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 41.29 E-value: 8.75e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVI 60
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI 64
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
340-382 |
9.58e-04 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 41.98 E-value: 9.58e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 488409350 340 KAYDDVLFRnvnmlIRRGEHVAIIGDNGTGKTTLLKIILGLTS 382
Cdd:COG4172 300 KAVDGVSLT-----LRRGETLGLVGESGSGKSTLGLALLRLIP 337
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
437-502 |
1.03e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 437 YGKdvfkkvnELSGGEKIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDF----NGTIITVSH 502
Cdd:PTZ00265 1355 YGK-------SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdkaDKTIITIAH 1417
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
161-230 |
1.15e-03 |
|
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: 40.00 E-value: 1.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 161 LSGGERTKVGIAQMLIKPTD--LLLLDEPTNHLDVKSIEWLASYIK---NNDSATVIVSHDRYFLDeTVNQIIEI 230
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKgliDLGNTVILIEHNLDVLS-SADWIIDF 161
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
329-503 |
1.31e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.84 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 329 SNRVIEMENVTKAYDDVLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSidKGSIKTASNL-------------- 394
Cdd:PRK10418 1 MPQQIELRNIALQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILP--AGVRQTAGRVlldgkpvapcalrg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 395 -KIGYLSQ--------------HEFE------RDGND-TLLHTFRKkvnVSEDQARHILAHFMFygkdvfkkvnELSGGE 452
Cdd:PRK10418 79 rKIATIMQnprsafnplhtmhtHAREtclalgKPADDaTLTAALEA---VGLENAARVLKLYPF----------EMSGGM 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 453 KIRLRWAQLVNTDYNLLVLDEPTNHLDIDAKEIIEDALLDFNGT----IITVSHD 503
Cdd:PRK10418 146 LQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKralgMLLVTHD 200
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
345-503 |
1.61e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 40.58 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 345 VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKI---------------ILGLTSIDKGSIKTASNLKIGYL-------SQH 402
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdltgggaprgarVTGDVTLNGEPLAAIDAPRLARLravlpqaAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 403 EFERDGNDTLL-----HTFRKKVNVSEDQ--ARHILAhfmFYGKD--VFKKVNELSGGEKIRLRWAQLV---------NT 464
Cdd:PRK13547 95 AFAFSAREIVLlgrypHARRAGALTHRDGeiAWQALA---LAGATalVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 488409350 465 DYNLLVLDEPTNHLDIDAK----EIIEDALLDFNGTIITVSHD 503
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLGVLAIVHD 214
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
332-388 |
1.71e-03 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 40.54 E-value: 1.71e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 332 VIEMENVTKA--YDDVLFR--------NVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTSIDKGSI 388
Cdd:PRK15112 4 LLEVRNLSKTfrYRTGWFRrqtveavkPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEL 70
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
65-234 |
1.75e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 41.26 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 65 DIKIGYLNQIPDYEKSESVYQCIKSVFKELDTISKQLETIETKMIEER---ENINSLVARYGElqtyyeenGGYEIDA-K 140
Cdd:COG4694 399 ELKEDLSRYKAEVEELIEELKTIKALKKALEDLKTEISELEAELSSVDeaaDEINEELKALGF--------DEFSLEAvE 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 141 IRKVTHGLNIAHLLKAKWGD-LSGGERTKVG----IAQMLIKPTDL----LLLDEPTNHLDVKSIEWLASYIKN--NDSA 209
Cdd:COG4694 471 DGRSSYRLKRNGENDAKPAKtLSEGEKTAIAlayfLAELEGDENDLkkkiVVIDDPVSSLDSNHRFAVASLLKElsKKAK 550
|
170 180
....*....|....*....|....*.
gi 488409350 210 TVIV-SHDRYFLDETVNQIIEIDQKK 234
Cdd:COG4694 551 QVIVlTHNLYFLKELRDLADEDNKKK 576
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-215 |
1.78e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 40.28 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 1 MNILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLK------------------LLSGMERPSTGVISW 62
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrlielypearvsgevYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 63 KKDIKIGYlnQIPDYEKSESVYQCIKSVFKeldtiskqletietkmieerenINSLVARYGELQtyyeenggyeidakiR 142
Cdd:PRK14247 81 RRRVQMVF--QIPNPIPNLSIFENVALGLK----------------------LNRLVKSKKELQ---------------E 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 143 KVTHGLNIAHL-------LKAKWGDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLD---VKSIEWLASYIKnNDSATVI 212
Cdd:PRK14247 122 RVRWALEKAQLwdevkdrLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDpenTAKIESLFLELK-KDMTIVL 200
|
...
gi 488409350 213 VSH 215
Cdd:PRK14247 201 VTH 203
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
8-215 |
1.84e-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: 39.78 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 8 NISKKYTED---ILfDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISW-KKDIkigylNQIPdyeksesv 83
Cdd:cd03244 7 NVSLRYRPNlppVL-KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIdGVDI-----SKIG-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 84 yqciksvfkeLDTISKQLETI--ETKMIEE--RENINSlvarygeLQTYYEEnggyEI-----DAKIRKVTHGLNIAHLL 154
Cdd:cd03244 73 ----------LHDLRSRISIIpqDPVLFSGtiRSNLDP-------FGEYSDE----ELwqaleRVGLKEFVESLPGGLDT 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 155 KAKWGD--LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKSIEWLASYIKNNDS-ATVI-VSH 215
Cdd:cd03244 132 VVEEGGenLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIREAFKdCTVLtIAH 196
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
161-228 |
2.22e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 40.50 E-value: 2.22e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDV----KSIEWLASYIKNNDSATVIVSHDRYFLDETVNQII 228
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaQIIELLLELQQKENMALVLITHDLALVAEAAHKII 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
161-193 |
2.33e-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: 2.33e-03
10 20 30
....*....|....*....|....*....|....
gi 488409350 161 LSGGERTKVGIAQMLI-KPtDLLLLDEPTNHLDV 193
Cdd:COG4172 157 LSGGQRQRVMIAMALAnEP-DLLIADEPTTALDV 189
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
159-216 |
2.35e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 40.76 E-value: 2.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488409350 159 GDLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDV---KSIEWLASYIKNNDSATVIVSHD 216
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVgakKEIYQLINQFKAEGLSIILVSSE 454
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
18-192 |
2.81e-03 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 39.57 E-value: 2.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 18 LFDHIK----ITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVIswkkdikigYLNQIpDYEKSESVYQCIKSVFKE 93
Cdd:PRK10771 10 LYHHLPmrfdLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSL---------TLNGQ-DHTTTPPSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 94 LDTISkQLeTIEtkmieerENIN-SLvarygelqtyyeeNGGYEIDA----KIRKVTHGLNIAHLLKAKWGDLSGGERTK 168
Cdd:PRK10771 80 NNLFS-HL-TVA-------QNIGlGL-------------NPGLKLNAaqreKLHAIARQMGIEDLLARLPGQLSGGQRQR 137
|
170 180
....*....|....*....|....
gi 488409350 169 VGIAQMLIKPTDLLLLDEPTNHLD 192
Cdd:PRK10771 138 VALARCLVREQPILLLDEPFSALD 161
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
360-503 |
3.56e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 38.84 E-value: 3.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 360 VAIIGDNGTGKTTLLKII-LGLTSIDKGSIKTASNLkIGYLSQH-----EFERDGN------------------------ 409
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIrYALYGKARSRSKLRSDL-INVGSEEasvelEFEHGGKryrierrqgefaefleakpserke 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 410 --DTLLHT-----FRKKVNVSEDQARHILAHF---------MFYGKDVFKKVNELSGGEKIRLRWAQLVNtdynlLVLDe 473
Cdd:COG0419 105 alKRLLGLeiyeeLKERLKELEEALESALEELaelqklkqeILAQLSGLDPIETLSGGERLRLALADLLS-----LILD- 178
|
170 180 190
....*....|....*....|....*....|
gi 488409350 474 pTNHLDIDAKEIIEDALLDfngtIITVSHD 503
Cdd:COG0419 179 -FGSLDEERLERLLDALEE----LAIITHV 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
348-485 |
3.74e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 39.77 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 348 RNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLT-----------------------SIDKG-----------------S 387
Cdd:NF040905 277 DDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygrnisgtvfkdgkevdvstvsdAIDAGlayvtedrkgyglnlidD 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 388 IK---TASNL----KIGYLSQHEFERDGNDtllhtFRKKVNvsedqarhILAHfmfygkDVFKKVNELSGG--EKIRL-R 457
Cdd:NF040905 357 IKrniTLANLgkvsRRGVIDENEEIKVAEE-----YRKKMN--------IKTP------SVFQKVGNLSGGnqQKVVLsK 417
|
170 180
....*....|....*....|....*....
gi 488409350 458 WaqlVNTDYNLLVLDEPTNHLDIDAK-EI 485
Cdd:NF040905 418 W---LFTDPDVLILDEPTRGIDVGAKyEI 443
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-221 |
4.30e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.24 E-value: 4.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 22 IKITLNSGDTLGLVGRNGEGKTTLLKLLSGmeRPSTGVISwkKDIKIGYLNqIPDYEKSESVYQCIKSVFKEldtiskql 101
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAYKILE--GDILFKGES-ILDLEPEERAHLGIFLAFQY-------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 102 eTIEtkmIEERENINSLVARYGELQTYYEENggyEIDA---------KIRKVthGLNIAHLLKAKWGDLSGGERTKVGIA 172
Cdd:CHL00131 93 -PIE---IPGVSNADFLRLAYNSKRKFQGLP---ELDPlefleiineKLKLV--GMDPSFLSRNVNEGFSGGEKKRNEIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 488409350 173 QMLIKPTDLLLLDEPTNHLDVKSIEWLASYI---KNNDSATVIVSHDRYFLD 221
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGInklMTSENSIILITHYQRLLD 215
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
161-216 |
5.03e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 38.11 E-value: 5.03e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488409350 161 LSGGERTKVGIAQML----IKPTDLLLLDEPTNHLDVKSIEWLASYIK--NNDSATVIV-SHD 216
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILehLVKGAQVIViTHL 140
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
160-220 |
5.18e-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: 38.47 E-value: 5.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488409350 160 DLSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVK-----SIEWLASYIKNNDSATVIVSHDRYFL 220
Cdd:cd03290 140 NLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlsdhlMQEGILKFLQDDKRTLVLVTHKLQYL 205
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
20-72 |
5.69e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 38.64 E-value: 5.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488409350 20 DHIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISWKKDIKIGYLN 72
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAIS 93
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
333-502 |
6.46e-03 |
|
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: 39.51 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 333 IEMENVTKAYDD---VLFRNVNMLIRRGEHVAIIGDNGTGKTTLLKIILGLTS------IDKGSIKTASNLK----IGYL 399
Cdd:TIGR01271 1218 MDVQGLTAKYTEagrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLStegeiqIDGVSWNSVTLQTwrkaFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 400 SQHEFERDGndtllhTFRKKVNVSE---DQARHILAHFM--------FYGKDVFKKVNE---LSGGEKIRLRWAQLVNTD 465
Cdd:TIGR01271 1298 PQKVFIFSG------TFRKNLDPYEqwsDEEIWKVAEEVglksvieqFPDKLDFVLVDGgyvLSNGHKQLMCLARSILSK 1371
|
170 180 190
....*....|....*....|....*....|....*....
gi 488409350 466 YNLLVLDEPTNHLDIDAKEIIEDALLDF--NGTIITVSH 502
Cdd:TIGR01271 1372 AKILLLDEPSAHLDPVTLQIIRKTLKQSfsNCTVILSEH 1410
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-224 |
6.72e-03 |
|
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: 38.39 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 21 HIKITLNSGDTLGLVGRNGEGKTTLLKLLSGMERPSTGVISwkkdIKIGYLNQIPDYEKSESVYQCIKSVFKE------- 93
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVL----IDGQDIAAMSRKELRELRRKKISMVFQSfallphr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488409350 94 --LDTISKQLEtIETKMIEEREninslvarygelqtyyeenggyeidAKIRKVTHGLNIAHLLKAKWGDLSGGERTKVGI 171
Cdd:cd03294 118 tvLENVAFGLE-VQGVPRAERE-------------------------ERAAEALELVGLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 488409350 172 AQMLIKPTDLLLLDEPTNHLD-VKSIEW---LASYIKNNDSATVIVSHDryfLDETV 224
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDpLIRREMqdeLLRLQAELQKTIVFITHD---LDEAL 225
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-51 |
8.17e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 38.27 E-value: 8.17e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 488409350 3 ILNASNISKKYTEDILFDHIKITLNSGDTLGLVGRNGEGKTTLLKLLSG 51
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAG 49
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
161-212 |
8.29e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.24 E-value: 8.29e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 488409350 161 LSGGERTKVGIAQMLIKPTDLLLLDEPTNHLDVKS---IEWLASYIKNNDSATVI 212
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeklIEKTIVDIKDKADKTII 1413
|
|
| |
